GLKA_PYRAB
ID GLKA_PYRAB Reviewed; 452 AA.
AC Q9UYQ3; G8ZIL7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00809};
DE EC=2.7.1.147 {ECO:0000255|HAMAP-Rule:MF_00809};
DE AltName: Full=ADP-dependent glucokinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=ADP-GK {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=ADPGK {ECO:0000255|HAMAP-Rule:MF_00809};
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=PYRAB14540;
GN ORFNames=PAB0967;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
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 -!- 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 -!- 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, ECO:0000305}.
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DR EMBL; AJ248287; CAB50359.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70900.1; -; Genomic_DNA.
DR PIR; B75058; B75058.
DR RefSeq; WP_010868569.1; NC_000868.1.
DR AlphaFoldDB; Q9UYQ3; -.
DR SMR; Q9UYQ3; -.
DR STRING; 272844.PAB0967; -.
DR EnsemblBacteria; CAB50359; CAB50359; PAB0967.
DR GeneID; 1495729; -.
DR KEGG; pab:PAB0967; -.
DR PATRIC; fig|272844.11.peg.1545; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OMA; IHYIYEF; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; Q9UYQ3; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Transferase.
FT CHAIN 1..452
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_0000184771"
FT DOMAIN 1..452
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 33
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 87
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 111..112
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 174
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 290
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 339..340
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 426
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 436
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 437
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
SQ SEQUENCE 452 AA; 51572 MW; 4212E6CE9D4FC4E9 CRC64;
MSWDEMYRDA YERVLNSIGK IKGVMLAYNT NIDAIKYLKR EDLERRIEEA GKDEVLRYSD
ELPKKINTIQ QLLGSILWSV KRGKAAELLV EDREVRNYMR QWGWDELRMG GQVGIMANLL
GGVYGIPVIA HVPQISKLQA SLFLDGPIYV PTFEEGLKLV HPRNFEGNEE DCIHYIYEFP
RGFKVLNFTA PRENRFIGAA DDYNPRLYIR KEWVERFEEI AERAELAIVS GLHSLTEETY
REPIKVVREH LKVLKDLNIK THLEFAFTAD EKVRREILGL LSLVYSVGLN EVELASVLEI
MNERELADRI LAKDPADPVA VIEGLMKLIE EGVERIHFHT YGYYLAITKY RGEHVRDALL
FSALAAATKA MLGNIEKLDD LRKGLEVPIG RQGLEVYEVV KREFNVEKGI GEVGDYQIAF
VPTKIVEKPK STVGIGDTIS SSAFVSEFSL SS
