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Database: UniProt/TrEMBL
Entry: G2T1D6_ROSHA
LinkDB: G2T1D6_ROSHA
Original site: G2T1D6_ROSHA 
ID   G2T1D6_ROSHA            Unreviewed;       362 AA.
AC   G2T1D6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   09-JUL-2014, entry version 18.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
GN   Name=serC; OrderedLocusNames=RHOM_06235;
OS   Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Roseburia.
OX   NCBI_TaxID=585394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16839 / NCIMB 14029 / A2-183;
RA   Mulder I.E., Aminov R.I., Travis A.J., Lan A., Gaboriau-Routhiau V.,
RA   Garden K., Logan E., Delday M., Coutts A.G.P., Grant G.,
RA   Patterson A.M., Cerf-Bensussan N., Kelly D.;
RT   "Bi-directional cross-talk between a Clostridium symbiont, Roseburia
RT   hominis, the gut immune system and appetite regulation.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC       (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC       phosphonooxypyruvate + 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-glycerate: step 2/3.
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; CP003040; AEN96366.1; -; Genomic_DNA.
DR   RefSeq; YP_004838298.1; NC_015977.1.
DR   EnsemblBacteria; AEN96366; AEN96366; RHOM_06235.
DR   GeneID; 11146454; -.
DR   KEGG; rho:RHOM_06235; -.
DR   KO; K00831; -.
DR   BioCyc; RHOM585394:GHYQ-1279-MONOMER; -.
DR   UniPathway; UPA00135; UER00197.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-HAMAP.
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/Cys_dSase.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR003248; Pser_aminoTfrase_subgr.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01364; serC_1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Serine biosynthesis; Transferase.
FT   REGION       76     77       Pyridoxal phosphate binding (By
FT                                similarity).
FT   REGION      237    238       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      42     42       L-glutamate (By similarity){EA15}.
FT   BINDING     101    101       Pyridoxal phosphate (By
FT                                similarity){EA15}.
FT   BINDING     151    151       Pyridoxal phosphate (By
FT                                similarity){EA15}.
FT   BINDING     171    171       Pyridoxal phosphate (By
FT                                similarity){EA15}.
FT   BINDING     194    194       Pyridoxal phosphate (By
FT                                similarity){EA15}.
FT   MOD_RES     195    195       N6-(pyridoxal phosphate)lysine (By
FT                                similarity){EA15}.
SQ   SEQUENCE   362 AA;  40450 MW;  6CCC1A105B5D1F0A CRC64;
     MSRVYNFSAG PAVLPEEVLK EAADEMLDYR GSGMSVMEMS HRSKVYDNII KEAEQDLRDL
     MNIPDNYKVL FLQGGASQQF AMIPMNLMKN RKAGYIVTGQ WAKKAYQEAQ IYGEAVKLAS
     SEDKTFSYIP DCSDLDIPED LDYVYICENN TIYGTKYKKL PNTKGHTLVA DVSSCFLSEP
     VDVTKYGVIY GGVQKNVGPA GVVIVIIRED LITEDTLPGT PTMLKYKTHA DADSLYNTPP
     CYGIYICGKV FKWLKKMGGL SVMKERNEEK AKILYDFLDQ SKLFHGTVVP EDRSLMNVPF
     VTGNEELDAK FVKEATAAGF VNLKGHRTVG GMRASIYNAM PKEGVEKLVA FMKKFEEENA
     NA
//
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