GLKA_PYRHO
ID GLKA_PYRHO Reviewed; 457 AA.
AC O58328;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000305};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00809};
DE EC=2.7.1.147 {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29784881};
DE AltName: Full=ADP-dependent glucokinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:29784881};
DE Short=ADP-GK {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=ADPGK {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:29784881};
DE AltName: Full=Glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=GlcN kinase {ECO:0000255|HAMAP-Rule:MF_00809};
GN Name=glkA {ECO:0000255|HAMAP-Rule:MF_00809}; OrderedLocusNames=PH0589;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2] {ECO:0007744|PDB:1L2L}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=12237466; DOI=10.1110/ps.0215602;
RA Tsuge H., Sakuraba H., Kobe T., Kujime A., Katunuma N., Ohshima T.;
RT "Crystal structure of the ADP-dependent glucokinase from Pyrococcus
RT horikoshii at 2.0-A resolution: a large conformational change in ADP-
RT dependent glucokinase.";
RL Protein Sci. 11:2456-2463(2002).
RN [3] {ECO:0007744|PDB:5O0I, ECO:0007744|PDB:5O0J}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 5-457 OF APOENZYME AND IN COMPLEX
RP WITH GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF PHE-272.
RX PubMed=29784881; DOI=10.1074/jbc.ra117.001562;
RA Grudnik P., Kaminski M.M., Rembacz K.P., Kuska K., Madej M., Potempa J.,
RA Dawidowski M., Dubin G.;
RT "Structural basis for ADP-dependent glucokinase inhibition by 8-bromo-
RT substituted adenosine nucleotide.";
RL J. Biol. Chem. 293:11088-11099(2018).
CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to
CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29784881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.1.147; Evidence={ECO:0000255|HAMAP-Rule:MF_00809,
CC ECO:0000269|PubMed:29784881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate + H(+);
CC Xref=Rhea:RHEA:62084, ChEBI:CHEBI:15378, ChEBI:CHEBI:58723,
CC ChEBI:CHEBI:58725, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00809};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00809};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00809};
CC -!- ACTIVITY REGULATION: Inhibited by 8-bromoadenosine phosphate (8-Br-
CC AMP). {ECO:0000269|PubMed:29784881}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for glucose {ECO:0000269|PubMed:29784881};
CC KM=0.13 mM for ADP {ECO:0000269|PubMed:29784881};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00809}.
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00809}.
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DR EMBL; BA000001; BAA29678.1; -; Genomic_DNA.
DR PIR; A71174; A71174.
DR PDB; 1L2L; X-ray; 2.00 A; A=1-457.
DR PDB; 5O0I; X-ray; 2.00 A; A=4-457.
DR PDB; 5O0J; X-ray; 1.81 A; A=5-457.
DR PDBsum; 1L2L; -.
DR PDBsum; 5O0I; -.
DR PDBsum; 5O0J; -.
DR AlphaFoldDB; O58328; -.
DR SMR; O58328; -.
DR STRING; 70601.3256995; -.
DR EnsemblBacteria; BAA29678; BAA29678; BAA29678.
DR KEGG; pho:PH0589; -.
DR eggNOG; arCOG03370; Archaea.
DR OMA; IHYIYEF; -.
DR BRENDA; 2.7.1.147; 5244.
DR UniPathway; UPA00109; -.
DR EvolutionaryTrace; O58328; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00809; ADP_glucokinase; 1.
DR InterPro; IPR007666; ADP_PFK/GK.
DR InterPro; IPR015990; ADP_PFK/GK_arc.
DR InterPro; IPR031299; GlkA.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..457
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_0000184773"
FT DOMAIN 5..457
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 37
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:29784881"
FT BINDING 91
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:29784881"
FT BINDING 115..116
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:29784881"
FT BINDING 179
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:29784881"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 295
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 345..346
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 432
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 442
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 443
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:29784881"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT MUTAGEN 272
FT /note="F->A: Does not impact activity and inhibition by 8-
FT Br-AMP."
FT /evidence="ECO:0000269|PubMed:29784881"
FT HELIX 7..21
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1L2L"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5O0J"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1L2L"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5O0J"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 359..378
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:5O0J"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:5O0J"
FT HELIX 441..456
FT /evidence="ECO:0007829|PDB:5O0J"
SQ SEQUENCE 457 AA; 52090 MW; A30EF1398FA9BC94 CRC64;
MITMTNWESL YEKALDKVEA SIRKVRGVLL AYNTNIDAIK YLKREDLEKR IEKVGKEEVL
RYSEELPKEI ETIPQLLGSI LWSIKRGKAA ELLVVSREVR EYMRKWGWDE LRMGGQVGIM
ANLLGGVYGI PVIAHVPQLS ELQASLFLDG PIYVPTFERG ELRLIHPREF RKGEEDCIHY
IYEFPRNFKV LDFEAPRENR FIGAADDYNP ILYVREEWIE RFEEIAKRSE LAIISGLHPL
TQENHGKPIK LVREHLKILN DLGIRAHLEF AFTPDEVVRL EIVKLLKHFY SVGLNEVELA
SVVSVMGEKE LAERIISKDP ADPIAVIEGL LKLIKETGVK RIHFHTYGYY LALTREKGEH
VRDALLFSAL AAATKAMKGN IEKLSDIREG LAVPIGEQGL EVEKILEKEF SLRDGIGSIE
DYQLTFIPTK VVKKPKSTVG IGDTISSSAF VSEFSLH
