KAD3_HUMAN
ID KAD3_HUMAN Reviewed; 227 AA.
AC Q9UIJ7; B4DP58; D3DRI1; E7ET30; Q5VYW6; Q9H576; Q9HC01; Q9NPB4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03169};
DE EC=2.7.4.10 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE Short=AK 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 alpha-like 1 {ECO:0000255|HAMAP-Rule:MF_03169};
GN Name=AK3 {ECO:0000255|HAMAP-Rule:MF_03169}; Synonyms=AK3L1, AK6, AKL3L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11485571; DOI=10.1042/0264-6021:3580225;
RA Noma T., Fujisawa K., Yamashiro Y., Shinohara M., Nakazawa A., Gondo T.,
RA Ishihara T., Yoshinobu K.;
RT "Structure and expression of human mitochondrial adenylate kinase targeted
RT to the mitochondrial matrix.";
RL Biochem. J. 358:225-232(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pheochromocytoma;
RA Li Y., Peng Y., Jiang Z., Gu W., Han Z., Chen Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Structure of human adenylate kinase 3-like 1.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase
CC activities. {ECO:0000255|HAMAP-Rule:MF_03169,
CC ECO:0000269|PubMed:11485571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-
CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03169,
CC ECO:0000269|PubMed:11485571};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169}.
CC -!- INTERACTION:
CC Q9UIJ7; P02649: APOE; NbExp=3; IntAct=EBI-3916527, EBI-1222467;
CC Q9UIJ7; Q92624: APPBP2; NbExp=6; IntAct=EBI-3916527, EBI-743771;
CC Q9UIJ7; P23560-2: BDNF; NbExp=3; IntAct=EBI-3916527, EBI-12275524;
CC Q9UIJ7; P23142-4: FBLN1; NbExp=3; IntAct=EBI-3916527, EBI-11956479;
CC Q9UIJ7; P04406: GAPDH; NbExp=3; IntAct=EBI-3916527, EBI-354056;
CC Q9UIJ7; P28799: GRN; NbExp=3; IntAct=EBI-3916527, EBI-747754;
CC Q9UIJ7; P42858: HTT; NbExp=9; IntAct=EBI-3916527, EBI-466029;
CC Q9UIJ7; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-3916527, EBI-1055254;
CC Q9UIJ7; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-3916527, EBI-10171774;
CC Q9UIJ7; O76024: WFS1; NbExp=3; IntAct=EBI-3916527, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03169, ECO:0000269|PubMed:11485571}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UIJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIJ7-2; Sequence=VSP_043090;
CC Name=3;
CC IsoId=Q9UIJ7-3; Sequence=VSP_044876;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC liver, moderately expressed in pancreas and kidney, and weakly
CC expressed in placenta, brain and lung. {ECO:0000269|PubMed:11485571}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon GTP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent GTP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000305|Ref.10}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03169}.
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DR EMBL; AB021870; BAA87913.1; -; mRNA.
DR EMBL; AF183419; AAG09688.1; -; mRNA.
DR EMBL; AK001553; BAA91753.1; -; mRNA.
DR EMBL; AK001951; BAA91996.1; -; mRNA.
DR EMBL; AK027534; BAB55183.1; -; mRNA.
DR EMBL; AK098205; BAG53592.1; -; mRNA.
DR EMBL; AK298200; BAG60470.1; -; mRNA.
DR EMBL; AL136231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58779.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58780.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58781.1; -; Genomic_DNA.
DR EMBL; BC013771; AAH13771.1; -; mRNA.
DR CCDS; CCDS56561.1; -. [Q9UIJ7-2]
DR CCDS; CCDS56562.1; -. [Q9UIJ7-3]
DR CCDS; CCDS6455.1; -. [Q9UIJ7-1]
DR RefSeq; NP_001186781.1; NM_001199852.1. [Q9UIJ7-3]
DR RefSeq; NP_001186782.1; NM_001199853.1. [Q9UIJ7-2]
DR RefSeq; NP_001186784.1; NM_001199855.1. [Q9UIJ7-2]
DR RefSeq; NP_001186785.1; NM_001199856.1. [Q9UIJ7-2]
DR RefSeq; NP_057366.2; NM_016282.3. [Q9UIJ7-1]
DR PDB; 1ZD8; X-ray; 1.48 A; A=1-227.
DR PDB; 6ZJB; X-ray; 1.82 A; A/B/C/D/E/F=1-227.
DR PDB; 6ZJD; X-ray; 1.75 A; A=1-227.
DR PDB; 6ZJE; X-ray; 1.48 A; A=1-227.
DR PDBsum; 1ZD8; -.
DR PDBsum; 6ZJB; -.
DR PDBsum; 6ZJD; -.
DR PDBsum; 6ZJE; -.
DR AlphaFoldDB; Q9UIJ7; -.
DR SMR; Q9UIJ7; -.
DR BioGRID; 119127; 61.
DR IntAct; Q9UIJ7; 20.
DR MINT; Q9UIJ7; -.
DR STRING; 9606.ENSP00000371230; -.
DR CarbonylDB; Q9UIJ7; -.
DR iPTMnet; Q9UIJ7; -.
DR PhosphoSitePlus; Q9UIJ7; -.
DR BioMuta; AK3; -.
DR DMDM; 23831297; -.
DR OGP; Q9UIJ7; -.
DR REPRODUCTION-2DPAGE; IPI00465256; -.
DR UCD-2DPAGE; Q9UIJ7; -.
DR EPD; Q9UIJ7; -.
DR jPOST; Q9UIJ7; -.
DR MassIVE; Q9UIJ7; -.
DR MaxQB; Q9UIJ7; -.
DR PaxDb; Q9UIJ7; -.
DR PeptideAtlas; Q9UIJ7; -.
DR PRIDE; Q9UIJ7; -.
DR ProteomicsDB; 18112; -.
DR ProteomicsDB; 84535; -. [Q9UIJ7-1]
DR ProteomicsDB; 84536; -. [Q9UIJ7-2]
DR TopDownProteomics; Q9UIJ7-1; -. [Q9UIJ7-1]
DR TopDownProteomics; Q9UIJ7-3; -. [Q9UIJ7-3]
DR Antibodypedia; 24061; 400 antibodies from 28 providers.
DR DNASU; 50808; -.
DR Ensembl; ENST00000359883.6; ENSP00000352948.2; ENSG00000147853.17. [Q9UIJ7-2]
DR Ensembl; ENST00000381809.8; ENSP00000371230.3; ENSG00000147853.17. [Q9UIJ7-1]
DR Ensembl; ENST00000447596.4; ENSP00000413933.2; ENSG00000147853.17. [Q9UIJ7-3]
DR Ensembl; ENST00000611749.4; ENSP00000482308.1; ENSG00000147853.17. [Q9UIJ7-2]
DR GeneID; 50808; -.
DR KEGG; hsa:50808; -.
DR MANE-Select; ENST00000381809.8; ENSP00000371230.3; NM_016282.4; NP_057366.2.
DR UCSC; uc003ziq.4; human. [Q9UIJ7-1]
DR CTD; 50808; -.
DR DisGeNET; 50808; -.
DR GeneCards; AK3; -.
DR HGNC; HGNC:17376; AK3.
DR HPA; ENSG00000147853; Tissue enhanced (skeletal).
DR MIM; 609290; gene.
DR neXtProt; NX_Q9UIJ7; -.
DR OpenTargets; ENSG00000147853; -.
DR PharmGKB; PA164741184; -.
DR VEuPathDB; HostDB:ENSG00000147853; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000155120; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR InParanoid; Q9UIJ7; -.
DR OMA; MSPVIAW; -.
DR PhylomeDB; Q9UIJ7; -.
DR TreeFam; TF312916; -.
DR BRENDA; 2.7.4.10; 2681.
DR PathwayCommons; Q9UIJ7; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9UIJ7; -.
DR BioGRID-ORCS; 50808; 40 hits in 1105 CRISPR screens.
DR ChiTaRS; AK3; human.
DR EvolutionaryTrace; Q9UIJ7; -.
DR GenomeRNAi; 50808; -.
DR Pharos; Q9UIJ7; Tbio.
DR PRO; PR:Q9UIJ7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UIJ7; protein.
DR Bgee; ENSG00000147853; Expressed in cardiac muscle of right atrium and 192 other tissues.
DR Genevisible; Q9UIJ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IDA:BHF-UCL.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IDA:BHF-UCL.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0046039; P:GTP metabolic process; IDA:BHF-UCL.
DR GO; GO:0046041; P:ITP metabolic process; IDA:BHF-UCL.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046051; P:UTP metabolic process; IDA:BHF-UCL.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03169; Adenylate_kinase_AK3; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR028586; AK3/Ak4_mitochondrial.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; GTP-binding; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..227
FT /note="GTP:AMP phosphotransferase AK3, mitochondrial"
FT /id="PRO_0000158922"
FT REGION 37..66
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|Ref.10"
FT REGION 127..164
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|Ref.10"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 38
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 64..66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 91..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 137..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 161
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT MOD_RES 20
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 64
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 64
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 189
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 189
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_043090"
FT VAR_SEQ 51..90
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044876"
FT CONFLICT 5
FT /note="A -> G (in Ref. 1; BAA87913)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="S -> R (in Ref. 1; BAA87913)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> Q (in Ref. 1; BAA87913)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..71
FT /note="DVM -> YVT (in Ref. 1; BAA87913)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="K -> E (in Ref. 3; BAG60470)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1ZD8"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6ZJE"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:1ZD8"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1ZD8"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:1ZD8"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 166..189
FT /evidence="ECO:0007829|PDB:1ZD8"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1ZD8"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:1ZD8"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1ZD8"
SQ SEQUENCE 227 AA; 25565 MW; 98A0EDF4FD9C9CEF CRC64;
MGASARLLRA VIMGAPGSGK GTVSSRITTH FELKHLSSGD LLRDNMLRGT EIGVLAKAFI
DQGKLIPDDV MTRLALHELK NLTQYSWLLD GFPRTLPQAE ALDRAYQIDT VINLNVPFEV
IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ REDDKPETVI KRLKAYEDQT
KPVLEYYQKK GVLETFSGTE TNKIWPYVYA FLQTKVPQRS QKASVTP
