ID   SERC_MYCBO              Reviewed;         376 AA.
AC   P63515; Q10534;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Putative phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
DE            Short=PSAT;
GN   Name=serC; OrderedLocusNames=Mb0908c;
OS   Mycobacterium bovis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine (By similarity).
CC   -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC       phosphonooxypyruvate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC       (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC   -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glyceric acid: step 2/3.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 3/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
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DR   EMBL; BX248336; CAD93769.1; -; Genomic_DNA.
DR   RefSeq; NP_854565.1; -.
DR   SMR; P63515; 8-376.
DR   GeneID; 1092794; -.
DR   GenomeReviews; BX248333_GR; Mb0908c.
DR   KEGG; mbo:Mb0908c; -.
DR   HOGENOM; P63515; -.
DR   OMA; P63515; RDAPPGL.
DR   BRENDA; 2.6.1.52; 3091.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotran...; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00160; -; 1.
DR   InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR006272; Ser_trans_bac.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   TIGRFAMs; TIGR01366; serC_3; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW   Serine biosynthesis; Transferase.
FT   CHAIN         1    376       Putative phosphoserine aminotransferase.
FT                                /FTId=PRO_0000150189.
FT   REGION       84     85       Pyridoxal phosphate binding (By
FT                                similarity).
FT   REGION      251    252       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      50     50       L-glutamate (By similarity).
FT   BINDING     108    108       Pyridoxal phosphate (By similarity).
FT   BINDING     154    154       Pyridoxal phosphate (By similarity).
FT   BINDING     176    176       Pyridoxal phosphate (By similarity).
FT   BINDING     199    199       Pyridoxal phosphate (By similarity).
FT   MOD_RES     200    200       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
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
//