(data stored in ACNUC7421 zone)

SWISSPROT: PGK_HISS2

ID   PGK_HISS2               Reviewed;         389 AA.
AC   B0UV33;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 65.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=HSM_0075;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00145}.
DR   EMBL; CP000947; ACA32418.1; -; Genomic_DNA.
DR   RefSeq; WP_012341575.1; NC_010519.1.
DR   SMR; B0UV33; -.
DR   EnsemblBacteria; ACA32418; ACA32418; HSM_0075.
DR   GeneID; 31486353; -.
DR   KEGG; hsm:HSM_0075; -.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 462069at2; -.
DR   BioCyc; HSOM228400:G1GB8-79-MONOMER; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000008543; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B0UV33.
DR   SWISS-2DPAGE; B0UV33.
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..389
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000076590"
FT   NP_BIND         342..345
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          21..23
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          59..62
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         36
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         112
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         145
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         196
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         313
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   389 AA;  41187 MW;  7B75DE6D99B45DCF CRC64;
     MSVIKMTDLD LAGKRVFIRA DLNVPVKEGK VTSDARIKAT IPTLKLALEK GAKVMVTSHL
     GRPTEGEFKP EDSLQPVVDY LKGAGFNVRL AQDYLNGVEV NEGEIVVLEN VRVNKGEKKN
     DPELSKKYAA LCDVFVMDAF GTAHRAQAST YGVAEFAPVA CAGPLLAAEL EALGKALKEP
     QRPMLAIVGG SKVSTKLTVL DSLSKIADQL IVGGGIANTF IAAEGHNVGK SLYEADLIPE
     AQRLSKVTNI PVPVDVRVGT EFSETALSTE KSVADVSGEE SIFDIGDKSA EQLADIIRNA
     KTILWNGPVG VFEFPNFRKG TEIVSNAIAE ATANGAFSIA GGGDTLAAID LFGIKDKISY
     ISTGGGAFLE FVEGKVLPAV EILEKRANG
//

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