ID N6X8P9_9ACTO Unreviewed; 396 AA.
AC N6X8P9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:ENO17528.1};
GN ORFNames=HMPREF9004_1438 {ECO:0000313|EMBL:ENO17528.1};
OS Schaalia cardiffensis F0333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO17528.1, ECO:0000313|Proteomes:UP000013015};
RN [1] {ECO:0000313|EMBL:ENO17528.1, ECO:0000313|Proteomes:UP000013015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0333 {ECO:0000313|EMBL:ENO17528.1,
RC ECO:0000313|Proteomes:UP000013015};
RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT "Reference genome for the Human Microbiome Project.";
RL Submitted (MAR-2013) 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|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
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:ENO17528.1}.
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DR EMBL; AQHZ01000024; ENO17528.1; -; Genomic_DNA.
DR RefSeq; WP_005963763.1; NZ_KB822675.1.
DR AlphaFoldDB; N6X8P9; -.
DR STRING; 888050.HMPREF9004_1438; -.
DR PATRIC; fig|888050.3.peg.1375; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_11; -.
DR OrthoDB; 9808460at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000013015; 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 CDD; cd00318; Phosphoglycerate_kinase; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000013015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00145}.
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 204
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 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
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 352..355
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 396 AA; 41647 MW; E7CAE61767066D8B CRC64;
MRTIETLGDL RSKRVLVRSD FNVPLKDGKI TDDGRIRAAL PTLTRLVEAG AKVVVMAHLG
RPKGKVDPAF SLAPVAKRLG ELIDAPVTLA KDVVGESAKA TVEALKDGEI ALLENVRYDA
RETSKVDEER GELAAAYAEL GDAFVSDGFG VVHRKQASVY DIAKLLPSAS GLLVLKEIES
LRKATDNPER PYGVVLGGSK VSDKLGVIAN LLKKADRLFI GGGMAFTFLA AQGHSVGKSL
LEEEQIDTVK GYIAEAAERG VELILPIDVV VAPEFAADAP ASVVTVDQIP ADQMGLDIGP
ESRKLFAEKI SSAKTVAWNG PMGVFEFPAF AEGTKAVAKA LSEGDMFSVI GGGDSAAAVR
LLGFDESTFS HISTGGGASL ELLEGKVLPG IAVLED
//
