ID   SERC_LEPIN              Reviewed;         363 AA.
AC   Q8F930;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
DE            Short=PSAT;
GN   Name=serC; OrderedLocusNames=LA_0366;
OS   Leptospira interrogans.
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
RX   MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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; AE010300; AAN47566.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_710548.2; -.
DR   HSSP; P23721; 1BJN.
DR   GeneID; 1149710; -.
DR   GenomeReviews; AE010300_GR; LA_0366.
DR   KEGG; lil:LA0366; -.
DR   HOGENOM; Q8F930; -.
DR   BioCyc; LINT189518:LA0367-MON; -.
DR   BRENDA; 2.6.1.52; 258108.
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; IPR003248; Pser_amintransf.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   ProDom; PD001544; Pser_amintransf; 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; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW   Serine biosynthesis; Transferase.
FT   CHAIN         1    363       Phosphoserine aminotransferase.
FT                                /FTId=PRO_0000150182.
FT   REGION       80     81       Pyridoxal phosphate binding (By
FT                                similarity).
FT   REGION      241    242       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      46     46       L-glutamate (By similarity).
FT   BINDING     106    106       Pyridoxal phosphate (By similarity).
FT   BINDING     156    156       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   363 AA;  40587 MW;  07747CC7A2F7A554 CRC64;
     MYLFQERIYN FGAGPAMLPN EVMEIAAAEF LNYKGSGMSV MEVSHREPLF EDVITEAEIL
     LRKLLNLGED YSIAFFSGGA TLHFSALPLN LLKEGESFDV AHTGIWTKKA WEEGLKFNEV
     NVIYDSTNNH FTDVPVLTDS NLSGKGKYLH ITSNNTIYGT QYPEIPKIKQ IPLVADMTSE
     LLSRKIDVKD FGVIFAGAQK NIGPSGLSLA IIRNDLLGIS GRKIPILLDY SVMVKNRSLY
     NTPSTYSIYI AKLVFEWLLK LGGIEAIEKV NEQKAKLIYD FIDSSSLYVC PVQKRARSKM
     NVVFLLKDKN LDSKFLDEAE KNGLHGLGGH RLVGGFRASI YNSMPLTGVQ KLVSFMKDFE
     SKI
//