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SERC_SCHPO
ID   SERC_SCHPO              Reviewed;         389 AA.
AC   Q10349;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Putative phosphoserine aminotransferase;
DE            Short=PSAT;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
GN   ORFNames=SPAC1F12.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine.
CC       {ECO:0000250|UniProtKB:P10658}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC         oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC         ChEBI:CHEBI:58538; EC=2.6.1.52;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93811.1; -; Genomic_DNA.
DR   PIR; T38065; S67450.
DR   RefSeq; NP_594333.1; NM_001019754.2.
DR   AlphaFoldDB; Q10349; -.
DR   SMR; Q10349; -.
DR   BioGRID; 278738; 9.
DR   IntAct; Q10349; 1.
DR   STRING; 4896.SPAC1F12.07.1; -.
DR   iPTMnet; Q10349; -.
DR   MaxQB; Q10349; -.
DR   PaxDb; Q10349; -.
DR   PRIDE; Q10349; -.
DR   EnsemblFungi; SPAC1F12.07.1; SPAC1F12.07.1:pep; SPAC1F12.07.
DR   GeneID; 2542269; -.
DR   KEGG; spo:SPAC1F12.07; -.
DR   PomBase; SPAC1F12.07; -.
DR   VEuPathDB; FungiDB:SPAC1F12.07; -.
DR   eggNOG; KOG2790; Eukaryota.
DR   HOGENOM; CLU_034866_0_0_1; -.
DR   InParanoid; Q10349; -.
DR   OMA; GYRASMY; -.
DR   PhylomeDB; Q10349; -.
DR   Reactome; R-SPO-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   PRO; PR:Q10349; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; ISO:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; ISO:PomBase.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43247; PTHR43247; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01364; serC_1; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Pyridoxal phosphate;
KW   Reference proteome; Serine biosynthesis; Transferase.
FT   CHAIN           1..389
FT                   /note="Putative phosphoserine aminotransferase"
FT                   /id="PRO_0000150140"
FT   BINDING         45
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..266
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  42798 MW;  F0841298496BCC36 CRC64;
     MSSREEVVNF AAGPAAMITS VVEEFGKDFV NFQGLGMGVA EISHRSKQGS GIVTSAESNF
     RKLYNIPENF HILFMQGGGT EQFAACLYNV YAHHALKNGN AKSLVANYII TGAWSKKAYA
     EAERLGFPCH VAVDMKELAG KYGSLPEDKD LKFTPDGETS LVYYCDNETV HGVEFNEPPT
     NIPKGAIRVC DVSSNFISRK IDFTKHDIIF AGAQKNAGPA GITVVFVRDS VLARPTPAEL
     HKLNIPVSPT VSDYKIMADN HSLYNTLPVA TLHAINLGLE YMLEHGGLVA LEASSIEKSK
     LLYDTLDKHD LYISVVEPAA RSRMNVTFRI EPQELESEFL AEAEKHHLVQ LKGYRSVGGI
     RASLYNAISV EQTRRLIDLL ESFAKAHSN
 
 
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