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PGK_SACS2
ID   PGK_SACS2               Reviewed;         408 AA.
AC   P50317; Q9UWT3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=SSO0527; ORFNames=C22_024;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8521845; DOI=10.1111/j.1432-1033.1995.800_3.x;
RA   Jones C.E., Fleming T.M., Cowan D.A., Littlechild J.A., Piper P.W.;
RT   "The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase
RT   genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-
RT   bp. Isolation, sequencing of the genes and expression in Escherichia
RT   coli.";
RL   Eur. J. Biochem. 233:800-808(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB57772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X80178; CAA56459.1; -; Genomic_DNA.
DR   EMBL; Y18930; CAB57772.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE006641; AAK40847.1; ALT_INIT; Genomic_DNA.
DR   PIR; H90198; H90198.
DR   PIR; S63528; S63528.
DR   RefSeq; WP_009991049.1; NC_002754.1.
DR   AlphaFoldDB; P50317; -.
DR   SMR; P50317; -.
DR   STRING; 273057.SSO0527; -.
DR   PRIDE; P50317; -.
DR   EnsemblBacteria; AAK40847; AAK40847; SSO0527.
DR   GeneID; 1454814; -.
DR   GeneID; 44129551; -.
DR   KEGG; sso:SSO0527; -.
DR   PATRIC; fig|273057.12.peg.526; -.
DR   eggNOG; arCOG00496; Archaea.
DR   HOGENOM; CLU_025427_0_2_2; -.
DR   InParanoid; P50317; -.
DR   OMA; DMIFDIG; -.
DR   PhylomeDB; P50317; -.
DR   BRENDA; 2.7.2.3; 6163.
DR   SABIO-RK; P50317; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
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;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..408
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146071"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  44396 MW;  9EBF90068315C099 CRC64;
     MGDLTIPTMD DIDIQSKKVL LRIDINSPVD ENGKIIDDSR IKAHIGTIKE LINKGNSVVL
     ISHQGRPGDK DFTSLEEHAK LISKYLDREV IFVDDVIGPY AREMIKKLEN NGILLLDNIR
     LISEELIEAP PQQHVKSFLV KKLAPLFDIY INDAFATAHR SQPSIVGFPL ALPSAAGRVM
     EREVSALAKI FNAEDTPKIF TLGGGKVHDT IRIIENLVRK RIADRILTGG LVAELFSVAK
     GMNLNPKNME ILEKLGILSL IPRARKLLLS GAPIEIPVDY KVEINGNVIE EPASKVTGII
     KDIGSTTAEI YSSFIKDAKV VVLRGPMGVI EDERFKSGSK SVLKASLEGQ GYVIIGGGHM
     ISALDEDMKI DSSKVHISTG GGALLLFLSG ERLPALEALS MSVVNSGD
 
 
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