PGK_XANFL
ID PGK_XANFL Reviewed; 397 AA.
AC P50314;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk;
OS Xanthobacter flavus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=281;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H4-14;
RX PubMed=7928974; DOI=10.1128/jb.176.19.6120-6126.1994;
RA Meijer W.G.;
RT "The Calvin cycle enzyme phosphoglycerate kinase of Xanthobacter flavus
RT required for autotrophic CO2 fixation is not encoded by the cbb operon.";
RL J. Bacteriol. 176:6120-6126(1994).
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; U08462; AAA62185.1; -; Genomic_DNA.
DR EMBL; U33064; AAA96748.1; -; Genomic_DNA.
DR AlphaFoldDB; P50314; -.
DR SMR; P50314; -.
DR UniPathway; UPA00109; UER00185.
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;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..397
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146046"
FT BINDING 23..25
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 354..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 41727 MW; 2492392F0AEBDBF8 CRC64;
MIAFRTLDDA VDLADKRVLV RVDLNVPMES GRVTDATRLK AILPTIRDIT GKGGKAVLLA
HLGRPKGRDE SQSLAPVAKA LEGELGRKVA FASDCIGDEA KSAVSRLASG EVIVLENTRF
HAGEEKNAPD FIEALASLGD IYVNDAFSTA HRAHASTEGL ARKLPAYAGR SMESEIEALT
KALEAPQRPV LAVVGGSKVS SKLELLGNLV KKVDILVIGG GMANTFLAAL GKKVGKSLCE
HDLANTARDI LKKAEAAGCE IVLPVDAVVA TEFKANAAHR VTSVDDVKDD EMMLDAGPET
VGIVKQKLDG AKTVVWNGPF GAFEMTPFDA ATVAVARYVG DLTHKGRLLS VAGGGDTVAA
LNHAGTAERF SYVSTAGGAF LEWLEGKALP GVEALRR
