ACKA_THEMA
ID ACKA_THEMA Reviewed; 403 AA.
AC Q9WYB1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; OrderedLocusNames=TM_0274;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=10074080; DOI=10.1128/jb.181.6.1861-1867.1999;
RA Bock A.-K., Glasemacher J., Schmidt R., Schoenheit P.;
RT "Purification and characterization of two extremely thermostable enzymes,
RT phosphate acetyltransferase and acetate kinase, from the hyperthermophilic
RT eubacterium Thermotoga maritima.";
RL J. Bacteriol. 181:1861-1867(1999).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. Phosphorylates propionate
CC (54%) in addition to acetate (100%). Uses GTP (100%), ITP (163%), UTP
CC (56%), and CTP (21%) as phosphoryl donors in addition to ATP (100%).
CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:10074080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00020, ECO:0000269|PubMed:10074080};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:10074080};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:10074080};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:10074080};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:10074080};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:10074080};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:10074080}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:10074080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; AE000512; AAD35363.1; -; Genomic_DNA.
DR PIR; H72397; H72397.
DR RefSeq; NP_228087.1; NC_000853.1.
DR RefSeq; WP_004082978.1; NZ_CP011107.1.
DR PDB; 2IIR; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J=1-403.
DR PDBsum; 2IIR; -.
DR AlphaFoldDB; Q9WYB1; -.
DR SMR; Q9WYB1; -.
DR DIP; DIP-2899N; -.
DR STRING; 243274.THEMA_03355; -.
DR EnsemblBacteria; AAD35363; AAD35363; TM_0274.
DR KEGG; tma:TM0274; -.
DR eggNOG; COG0282; Bacteria.
DR InParanoid; Q9WYB1; -.
DR OMA; KIITCHI; -.
DR OrthoDB; 537106at2; -.
DR BioCyc; MetaCyc:MON-428; -.
DR BRENDA; 2.7.2.1; 6331.
DR UniPathway; UPA00340; UER00458.
DR EvolutionaryTrace; Q9WYB1; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00020; Acetate_kinase; 1.
DR InterPro; IPR004372; Ac/propionate_kinase.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR21060; PTHR21060; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00016; ackA; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..403
FT /note="Acetate kinase"
FT /id="PRO_0000107631"
FT ACT_SITE 147
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 207..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 283..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 331..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 179
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 240
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2IIR"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:2IIR"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2IIR"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2IIR"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 202..218
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:2IIR"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 296..320
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:2IIR"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:2IIR"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:2IIR"
SQ SEQUENCE 403 AA; 44804 MW; 98340ACB2AC04A7E CRC64;
MRVLVINSGS SSIKYQLIEM EGEKVLCKGI AERIGIEGSR LVHRVGDEKH VIERELPDHE
EALKLILNTL VDEKLGVIKD LKEIDAVGHR VVHGGERFKE SVLVDEEVLK AIEEVSPLAP
LHNPANLMGI KAAMKLLPGV PNVAVFDTAF HQTIPQKAYL YAIPYEYYEK YKIRRYGFHG
TSHRYVSKRA AEILGKKLEE LKIITCHIGN GASVAAVKYG KCVDTSMGFT PLEGLVMGTR
SGDLDPAIPF FIMEKEGISP QEMYDILNKK SGVYGLSKGF SSDMRDIEEA ALKGDEWCKL
VLEIYDYRIA KYIGAYAAAM NGVDAIVFTA GVGENSPITR EDVCSYLEFL GVKLDKQKNE
ETIRGKEGII STPDSRVKVL VVPTNEELMI ARDTKEIVEK IGR
