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Database: UniProt
Entry: A0A148N852_9GAMM
LinkDB: A0A148N852_9GAMM
Original site: A0A148N852_9GAMM 
ID   A0A148N852_9GAMM        Unreviewed;       392 AA.
AC   A0A148N852;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN   ORFNames=AXA67_00685 {ECO:0000313|EMBL:KXJ40703.1};
OS   Methylothermaceae bacteria B42.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylothermaceae.
OX   NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ40703.1, ECO:0000313|Proteomes:UP000074680};
RN   [1] {ECO:0000313|EMBL:KXJ40703.1, ECO:0000313|Proteomes:UP000074680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B42 {ECO:0000313|EMBL:KXJ40703.1};
RX   PubMed=26779119; DOI=10.3389/fmicb.2015.01425;
RA   Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., Mullin S.,
RA   Chan K.Y., Gradinaru V., Orphan V.J.;
RT   "Genomic Reconstruction of an Uncultured Hydrothermal Vent
RT   Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates
RT   Multiple Adaptations to Oxygen Limitation.";
RL   Front. Microbiol. 6:1425-1425(2015).
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:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC         Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|HAMAP-Rule:MF_00145,
CC       ECO:0000256|RuleBase:RU000532}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXJ40703.1}.
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DR   EMBL; LSNW01000023; KXJ40703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A148N852; -.
DR   STRING; 1798802.AXA67_00685; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000074680; Unassembled WGS sequence.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00145};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00145}.
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         346..349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   392 AA;  42123 MW;  3C55D44C4D54BF42 CRC64;
     MTIKKMIDLD LKGKRVLIRA DLNVPIKDGE VTSDTRIRAS VPTIRQALEQ GARCVMVMSH
     LGRPKEGEYD PQYSLAPVAE RLSELLGQPV RLIKDWIDGV KTESGEVVLL ENVRFLKGEK
     TNDPELGKKM AALCDVFVMD AFGTAHRAQA STHAVAQFAP EVCAGLLLAQ ELEALGKALQ
     NPDRPLLAIV GGSKVSTKLK VLETLAQKVD QLIVGGGIAN TFIAAAGFPV GKSLYEPDLI
     PDAKRLMEQA KARGADIPIP EDVVVAKEFS EDAEATVKKV NEVADDDLIL DIGPETAQYY
     ADLIKKAGTI VWNGPVGVFE IDQFAEGTRV LAEAIAESKA FSIAGGGDTL AAIEKFGIGD
     KVSYQSTGGG AFLEFLEGRK LPAVEILEQR DC
//
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