(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIK5_GEOS0

ID   A0A0F6BIK5_GEOS0        Unreviewed;       394 AA.
AC   A0A0F6BIK5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041088};
DE            EC=2.7.2.3 {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041088};
GN   Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN   OrderedLocusNames=GY4MC1_0415 {ECO:0000313|EMBL:ADP73256.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73256.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73256.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73256.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + ATP = 3-phospho-D-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC         EC=2.7.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00145,
CC         ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS01120514};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145, ECO:0000256|RuleBase:RU000695,
CC       ECO:0000256|SAAS:SAAS00041112}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145,
CC       ECO:0000256|SAAS:SAAS00041091}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145,
CC       ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00041072}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532,
CC       ECO:0000256|SAAS:SAAS01085159}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}.
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DR   EMBL; CP002293; ADP73256.1; -; Genomic_DNA.
DR   RefSeq; WP_003248109.1; NC_014650.1.
DR   EnsemblBacteria; ADP73256; ADP73256; GY4MC1_0415.
DR   GeneID; 29236925; -.
DR   KEGG; gmc:GY4MC1_0415; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 462069at2; -.
DR   BioCyc; GSP581103:G1GOQ-462-MONOMER; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002034; 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; A0A0F6BIK5.
DR   SWISS-2DPAGE; A0A0F6BIK5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|PIRSR:PIRSR000724-2, ECO:0000256|SAAS:SAAS00041066};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|SAAS:SAAS00041081};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00041106};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041108,
KW   ECO:0000313|EMBL:ADP73256.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|SAAS:SAAS00041094};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041076,
KW   ECO:0000313|EMBL:ADP73256.1}.
FT   NP_BIND     350    353       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
FT   REGION       21     23       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00145, ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   REGION       59     62       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00145, ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING      36     36       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     118    118       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     151    151       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     201    201       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
FT   BINDING     323    323       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
FT   MOD_RES     183    183       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145}.
FT   MOD_RES     299    299       Phosphothreonine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00145}.
SQ   SEQUENCE   394 AA;  42338 MW;  042AEA16770E354A CRC64;
     MNKKTIQDVD VKGKRVFCRV DFNVPMENGA ITDDTRIRAA LPTIRYLIEQ GAKVILASHL
     GRPKGKVVEE LRLNAVAERL SELLGKQVVK TDEAYGEAVK TAIAGMKEGD VLLLENVRFY
     PGEEKNDPEL AKAFAELADI YVNDAFGAAH RAHASTEGIA HYLPAVAGFL MEKEIEVLGK
     ALSNPERPFT AIIGGAKVKD KIGVIENLLN KVDNLIIGGG LAYTFVKALG HEVGKSLLEE
     DKIELAKSFM EKAKEKGVNF YMPVDAVVAD RFANDANTKV VAIDAIPSDW EALDIGPKTC
     ELYRDVIMKS KLVVWNGPMG VFEMDAFAGG TKAVAQALAD AADTYSVIGG GDSAAAVEKF
     GLADKMDHIS TGGGASLEFM EGKQLPGVVA LNDK
//

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