(data stored in ACNUC5340 zone)

SWISSPROT: PGK_ACAM1

ID   PGK_ACAM1               Reviewed;         401 AA.
AC   B0CD95;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 70.
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=AM1_0637;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW25686.1; -; Genomic_DNA.
DR   RefSeq; WP_012161281.1; NC_009925.1.
DR   SMR; B0CD95; -.
DR   STRING; 329726.AM1_0637; -.
DR   PRIDE; B0CD95; -.
DR   EnsemblBacteria; ABW25686; ABW25686; AM1_0637.
DR   KEGG; amr:AM1_0637; -.
DR   eggNOG; ENOG4105BZA; Bacteria.
DR   eggNOG; COG0126; LUCA.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 462069at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000268; 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   CDD; cd00318; Phosphoglycerate_kinase; 1.
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; B0CD95.
DR   SWISS-2DPAGE; B0CD95.
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000076577"
FT   NP_BIND         357..360
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          24..26
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          63..66
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         40
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         122
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         155
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         206
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         297
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         328
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   401 AA;  41862 MW;  7D414EB97EC3D54D CRC64;
     MSKKTIANLT SADLSGKRVL VRADFNVPLD GDGKITDDTR IRAALPTIQD LTSKGAKVIL
     ASHFGRPKGQ VNESMRLTPV AARLSELLGQ AVTKCDDCIG DEVAAKVGAL QNGQVALLEN
     VRFHSGEEAN DPEFARQLAS VADLYVNDAF GTAHRAHAST EGVTHHLSPS VAGYLIEKEL
     KYLQAAIEGP QRPLAAIVGG SKVSSKIGVI ETLLDKVDKL LIGGGMIFTF YKARGLAVGK
     SLVEEDKLDL ARTLEAKAKE KGVALLLPSD VVVADNFAAD ANAQTVSINN IPDGWMGLDI
     GPNSVKEFQA ALSDCKTVIW NGPMGVFEFD KFAAGTDAVA HSLAAITETG ADTIIGGGDS
     VAAVEKVGVA EKMSHISTGG GASLELLEGK VLPGIAALDE A
//

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