ID G2T1D6_ROSHA Unreviewed; 362 AA.
AC G2T1D6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-APR-2013, entry version 12.
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-1237-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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA: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 PANTHER; PTHR21152:SF1; PTHR21152:SF1; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
PE 3: Inferred from homology;
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).
FT BINDING 101 101 Pyridoxal phosphate (By similarity).
FT BINDING 151 151 Pyridoxal phosphate (By similarity).
FT BINDING 171 171 Pyridoxal phosphate (By similarity).
FT BINDING 194 194 Pyridoxal phosphate (By similarity).
FT MOD_RES 195 195 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
