ID E6YJ74_BARC7 Unreviewed; 407 AA.
AC E6YJ74;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:CBI76912.1};
GN OrderedLocusNames=BARCL_1240 {ECO:0000313|EMBL:CBI76912.1};
OS Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76912.1, ECO:0000313|Proteomes:UP000009101};
RN [1] {ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L.,
RA Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.;
RT "Genome sequencing of Bartonella species and comparative genomics.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBI76912.1, ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
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}.
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DR EMBL; FN645454; CBI76912.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YJ74; -.
DR STRING; 696125.BARCL_1240; -.
DR KEGG; bcd:BARCL_1240; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_5; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000009101; 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 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 31..33
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 69..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 211
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 333
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 363..366
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 407 AA; 44685 MW; 23B38EA2F76BA053 CRC64;
MKDKEKEKTV MEFRTLDDVD VTGKRVLVRV DFNVPMLKGK VCDETRIECH KDTLVELQKR
GAKVIILSHC GRPKGQVVPE FTVRPVVETL EKIIKKPIFF ANDCIGDAAQ KAVNKVQDGE
ILLLENVRFY SGEEKNEHSF AKALAQNGDL YVNDAFSVSH RAHASIEGIT HLLPSYAGRA
LQRELQALKK GLDHPTHPVV AVVGGAKVSS KLFVLNHLVE KVDYLVIGGG MANSFLAAQG
VSVGKSLCEE TLMGTIKEII EKAYQSHCKL LLPLDVVVGF HFEKETPHQC YALEEIPEKG
MILDIGPRSI AHIQAAIDKA KTLVWNGPLG VFEMSPFDQG TVTVARYVAE RSQRRQLVSI
AGGGDTVFAL NHAGVANDFT YLSTAGGAFL EWMEGKSLPG IFALQQV
//
