(data stored in ACNUC8465 zone)

SWISSPROT: B6H903_PENRW

ID   B6H903_PENRW            Unreviewed;       417 AA.
AC   B6H903;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|RuleBase:RU000532};
GN   Name=pgkA {ECO:0000313|EMBL:CAP93143.1};
GN   ORFNames=PCH_Pc16g04730 {ECO:0000313|EMBL:CAP93143.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93143.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP93143.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC       D-glyceroyl phosphate. {ECO:0000256|RuleBase:RU000532}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|RuleBase:RU000532}.
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DR   EMBL; AM920431; CAP93143.1; -; Genomic_DNA.
DR   RefSeq; XP_002560824.1; XM_002560778.1.
DR   STRING; 500485.XP_002560824.1; -.
DR   EnsemblFungi; CAP93143; CAP93143; PCH_Pc16g04730.
DR   GeneID; 8304566; -.
DR   KEGG; pcs:Pc16g04730; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   eggNOG; COG0126; LUCA.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; EOG092C2GKC; -.
DR   BioCyc; PCHR:PC16G04730-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 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   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H903.
DR   SWISS-2DPAGE; B6H903.
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000724-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Kinase {ECO:0000256|RuleBase:RU000532, ECO:0000313|EMBL:CAP93143.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000724-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU000532}.
FT   NP_BIND     373    376       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
FT   REGION       24     26       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   REGION       64     67       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING      40     40       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     123    123       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     171    171       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     220    220       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
FT   BINDING     313    313       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000724-2}.
FT   BINDING     344    344       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
SQ   SEQUENCE   417 AA;  44078 MW;  5EE77C497A66AF61 CRC64;
     MSLSNKLPVT DVDLKGKRVL IRVDFNVPLD ENKNVTNPQR IVGALPTIKY AIDNGAKAVV
     LMSHLGRPDG KVNPKYSLKP VVPVLEELLG KSVTFTEDCV GPQTEETVNK ASDGQVILLE
     NLRFHAEEEG SSKDAEGKKV KADKADVDAF RKGLTALGDV YVNDAFGTAH RAHSSMVGVD
     LPQKAAGFLV KKELEYFAKA LESPARPFLA ILGGAKVSDK IQLIDNLLPK VNSLIITGGM
     AFTFKKTLEN VKIGNSLFDE AGSKIVGEIV EKAKKHNVEI VLPVDYVTAD KFSADATVGA
     ATDASGIPDG YMGLDVGPES VKLYQKTIAE AKTILWNGPP GVFELKPFAK ATEATLDAAV
     KAAESGSIVI IGGGDTATVA AKYKAEDKIS HVSTGGGASL ELLEGKELPG VAALSSK
//

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