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Database: UniProt
Entry: K0KTL4_WICCF
LinkDB: K0KTL4_WICCF
Original site: K0KTL4_WICCF 
ID   K0KTL4_WICCF            Unreviewed;       385 AA.
AC   K0KTL4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 36.
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=PGK2 {ECO:0000313|EMBL:CCH45362.1};
GN   ORFNames=BN7_4944 {ECO:0000313|EMBL:CCH45362.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH45362.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH45362.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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}.
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:CCH45362.1}.
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DR   EMBL; CAIF01000194; CCH45362.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0KTL4; -.
DR   STRING; 1206466.K0KTL4; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   HOGENOM; CLU_025427_0_0_1; -.
DR   InParanoid; K0KTL4; -.
DR   Proteomes; UP000009328; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
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; 2.
DR   PIRSF; PIRSF000724; Pgk; 2.
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:UP000009328};
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         168
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         326..329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   385 AA;  42565 MW;  A68331A2F45B2EBF CRC64;
     MSLKNKLSIK DVDLKDKRVL IRVDYNVPHI DKKILDNQRI IATLLTIKYA LEQNPKVIIL
     ATHLGKPNGK ITKELSLDFI AKELSKLLDQ EVELLPDCIG PKVEKVINES SKGKIYLLEN
     LRFHIEEEGF RKYGFKEFAS TRNVEKFRSD LSKLGDVYIN DAFGTCHREH SSIVGINIKE
     RASGLLLSKE IEYFEKTLKS EPARPFLAIV GGGKINDKID SIDSLLDKVD TLLIGGGMSC
     TFLKVLKNMN IGHATVEEGI PHFWQVLDIG PKTRELYDSK LSKAQTIIWN GPLGVVKFSS
     FAKGTKTIVD SVIKYADMGK KVIIGGGDTA TMVYETGQAD KLDHVATGSG ATLCILEGRD
     LPGVTHLSNK ESGDDLVAKI KGLSI
//
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