GenomeNet

Database: UniProt
Entry: A0A109LY77_9SPHN
LinkDB: A0A109LY77_9SPHN
Original site: A0A109LY77_9SPHN 
ID   A0A109LY77_9SPHN        Unreviewed;       399 AA.
AC   A0A109LY77;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-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   ECO:0000313|EMBL:KWV95836.1};
GN   ORFNames=ASS64_00960 {ECO:0000313|EMBL:KWV95836.1};
OS   Erythrobacter sp. AP23.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV95836.1, ECO:0000313|Proteomes:UP000058666};
RN   [1] {ECO:0000313|EMBL:KWV95836.1, ECO:0000313|Proteomes:UP000058666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP23 {ECO:0000313|EMBL:KWV95836.1,
RC   ECO:0000313|Proteomes:UP000058666};
RA   Lin W., Zheng Q.;
RT   "Draft genome sequence of Erythrobacter sp. AP23.";
RL   Submitted (NOV-2015) 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: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:KWV95836.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNBY01000001; KWV95836.1; -; Genomic_DNA.
DR   RefSeq; WP_067688484.1; NZ_LNBY01000001.1.
DR   AlphaFoldDB; A0A109LY77; -.
DR   STRING; 499656.ASS64_00960; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000058666; 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; 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.
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         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         61..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         203
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         326
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         356..359
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   399 AA;  41488 MW;  067055CAAAB2E33F CRC64;
     MSNFKTLDDL GDITGKVALV RVDLNLPMKD GSATDVTRVE AVKPTILELA DKGAKILLLA
     HFGRPKGQRH STMSTSFVQG DVEKVLGKEI MFIPEVMGPV VEQSIGILGN GDIGLLDNVR
     FWPGEESNDP EFAKGIAAHG DFYVNDAFSA AHRAHASTEG LAHHLPAHAG RAMEAELKAL
     DAALGTPEPP VAAVVGGAKV STKLDVLTNL VGKVQHLIIG GGMANTFLAA KGVDVGKSLC
     EHDLTATANT IMDEADHAGC TVHLPYDVVV AKEFAANPDS LRTCNVHEVA EDEMILDVGP
     LATEALGDVL KTCRTLVWNG PLGAFETEPF DTATAALAKT AAALTQDGSL TSVAGGGDTV
     AALAHAGVKD DFTFVSTAGG AFLEWMEGKA LPGVAALMA
//
DBGET integrated database retrieval system