ID I2H3I0_TETBL Unreviewed; 416 AA.
AC I2H3I0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00016471, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN Name=TBLA0D04360 {ECO:0000313|EMBL:CCH60932.1};
GN ORFNames=TBLA_0D04360 {ECO:0000313|EMBL:CCH60932.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60932.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60932.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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,
CC ECO:0000256|RuleBase:RU000532};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR EMBL; HE806319; CCH60932.1; -; Genomic_DNA.
DR RefSeq; XP_004180451.1; XM_004180403.1.
DR AlphaFoldDB; I2H3I0; -.
DR STRING; 1071380.I2H3I0; -.
DR GeneID; 14495968; -.
DR KEGG; tbl:TBLA_0D04360; -.
DR eggNOG; KOG1367; Eukaryota.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; I2H3I0; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 5477183at2759; -.
DR Proteomes; UP000002866; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
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; 3.
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:SF0; PHOSPHOGLYCERATE KINASE; 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|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 371..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 416 AA; 44433 MW; 51C84CB93EBCAB99 CRC64;
MSLSSKLTVK DLQLEGKRVF IRVDFNVPLD GETITSNQRI VAALPTIQYV LEHKPQYIVL
ASHLGRPNGE RVAKYSLKPV AKELEKLLGQ KVTFLNDCVG AEVEAATKAA APGSVILLEN
LRYHIEEEGS QKVDGKKVKA SPEAVTKFRK ELCSLADVYV NDAFGTAHRA HSSIVGFDLP
QRAAGFLLAK ELQYFGKALE NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIIIGGGMAF
TFKKVIENAE IGDSIFDKAG AEIVPKLMEK AKAKGVKVVL PVDFVIADDF SATANTKTVT
DKEGIPAGWQ GLDNGPASRK LFAAAVAEAK TIVWNGPPGV FEFEKFSAGT KALLDEVVES
CSKGNTVIIG GGDTATVAKK FGVTDKISHV STGGGASLEL LEGKELPGVA FLSEKK
//
