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SERC_MYCTU
ID   SERC_MYCTU              Reviewed;         376 AA.
AC   P9WQ73; L0T803; P63514; Q10534;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
DE            Short=PSAT;
GN   Name=serC; OrderedLocusNames=Rv0884c; ORFNames=MTCY31.12c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-18.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP   COFACTOR, AND SUBUNIT.
RX   PubMed=22525753; DOI=10.1107/s0907444912004829;
RA   Coulibaly F., Lassalle E., Baker H.M., Baker E.N.;
RT   "Structure of phosphoserine aminotransferase from Mycobacterium
RT   tuberculosis.";
RL   Acta Crystallogr. D 68:553-563(2012).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000250}.
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:0000269|PubMed:22525753};
CC       Note=Binds 1 pyridoxal phosphate per subunit.
CC       {ECO:0000269|PubMed:22525753};
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:0000269|PubMed:22525753}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AL123456; CCP43632.1; -; Genomic_DNA.
DR   PIR; A70781; A70781.
DR   RefSeq; NP_215399.1; NC_000962.3.
DR   RefSeq; WP_003404623.1; NZ_NVQJ01000001.1.
DR   PDB; 2FYF; X-ray; 1.50 A; A/B=1-376.
DR   PDB; 3VOM; X-ray; 2.10 A; A/B=1-376.
DR   PDBsum; 2FYF; -.
DR   PDBsum; 3VOM; -.
DR   AlphaFoldDB; P9WQ73; -.
DR   SMR; P9WQ73; -.
DR   STRING; 83332.Rv0884c; -.
DR   iPTMnet; P9WQ73; -.
DR   PaxDb; P9WQ73; -.
DR   DNASU; 885140; -.
DR   GeneID; 885140; -.
DR   KEGG; mtu:Rv0884c; -.
DR   TubercuList; Rv0884c; -.
DR   eggNOG; COG1932; Bacteria.
DR   OMA; TAFWDIA; -.
DR   PhylomeDB; P9WQ73; -.
DR   BRENDA; 2.6.1.52; 3445.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR   GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01366; serC_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW   Cytoplasm; Direct protein sequencing; Pyridoxal phosphate;
KW   Pyridoxine biosynthesis; Reference proteome; Serine biosynthesis;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:34915127,
FT                   ECO:0007744|PubMed:21969609"
FT   CHAIN           2..376
FT                   /note="Phosphoserine aminotransferase"
FT                   /id="PRO_0000150188"
FT   BINDING         50
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..85
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   BINDING         108
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:22525753"
FT   BINDING         176
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:22525753"
FT   BINDING         199
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:22525753"
FT   BINDING         251..252
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           31..35
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   TURN            39..46
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           52..68
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           84..94
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           107..118
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   TURN            178..183
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           215..226
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           255..271
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           274..294
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   STRAND          310..317
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           323..332
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:3VOM"
FT   STRAND          346..352
FT                   /evidence="ECO:0007829|PDB:2FYF"
FT   HELIX           359..374
FT                   /evidence="ECO:0007829|PDB:2FYF"
SQ   SEQUENCE   376 AA;  40233 MW;  32677398E8967D1E CRC64;
     MADQLTPHLE IPTAIKPRDG RFGSGPSKVR LEQLQTLTTT AAALFGTSHR QAPVKNLVGR
     VRSGLAELFS LPDGYEVILG NGGATAFWDA AAFGLIDKRS LHLTYGEFSA KFASAVSKNP
     FVGEPIIITS DPGSAPEPQT DPSVDVIAWA HNETSTGVAV AVRRPEGSDD ALVVIDATSG
     AGGLPVDIAE TDAYYFAPQK NFASDGGLWL AIMSPAALSR IEAIAATGRW VPDFLSLPIA
     VENSLKNQTY NTPAIATLAL LAEQIDWLVG NGGLDWAVKR TADSSQRLYS WAQERPYTTP
     FVTDPGLRSQ VVGTIDFVDD VDAGTVAKIL RANGIVDTEP YRKLGRNQLR VAMFPAVEPD
     DVSALTECVD WVVERL
 
 
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