(data stored in ACNUC7421 zone)

HOGENOM: BACPZ_1_PE1006

ID   BACPZ_1_PE1006                       STANDARD;      PRT;   359 AA.
AC   BACPZ_1_PE1006; E0TXW5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphoserine aminotransferase; EC=2.6.1 52;AltName:
DE   Full=Phosphohydroxythreonine aminotransferase; (BACPZ_1.PE1006).
GN   Name=serC; OrderedLocusNames=BSUW23_05070;
OS   BACILLUS SUBTILIS SUBSP. SPIZIZENII STR. W23.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACPZ_1.PE1006.
CC       Bacillus subtilis subsp. spizizenii str. W23 chromosome, complete genom
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E0TXW5_BACPZ
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   -!- COFACTOR: Pyridoxal phosphate (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.
CC   -!- GENE_FAMILY: HOG000088965 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E0TXW5; -.
DR   EMBL; CP002183; ADM37067.1; -; Genomic_DNA.
DR   RefSeq; YP_003865376.1; NC_014479.1.
DR   GeneID; 9722005; -.
DR   GenomeReviews; CP002183_GR; BSUW23_05070.
DR   KEGG; bss:BSUW23_05070; -.
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   HAMAP; MF_00160; SerC_aminotrans_5; 1; -.
DR   InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR003248; Pser_aminoTfrase_subgr.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR   HOGENOMDNA; BACPZ_1.PE1006; -.
KW   phosphoserine aminotransferase;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Serine biosynthesis; Transferase.
SQ   SEQUENCE   359 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MERTTNFNAG PAALPLEVLQ KAQKEFIDFN TSGMSVMELS HRSKEYEAVH QKAKSLLTEL
     MGIPEDYDIL FLQGGASLQF SMLPMNFLTP EKTAHFVMTG AWSEKALAEA KLFGNTSVTA
     TSEGDHYSYI PEIELTDVKD GAYLHITSNN TIFGTQWQEF PNSPIPLVAD MSSDILSRKI
     DVSKFDVIYG GAQKNLGPSG VTVVIMKKTW LQNENANVPK ILKYSTHVKA DSLYNTPPTF
     AIYMLSLVLE WLKENGGVEA AEQRNEQKAQ VLYSCIDESN GFYKGHARTD SRSRMNVTFT
     LRDDELTKTF VQEAKEAKMI GLGGHRSVGG CRASIYNAVS LEDCEKLAAF MKKFQQENE
//

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