ID G2JD88_ACIBA Unreviewed; 373 AA.
AC G2JD88;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 29-MAY-2013, entry version 12.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; ORFNames=ABZJ_03044;
OS Acinetobacter baumannii MDR-ZJ06.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter;
OC Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=497978;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MDR-ZJ06;
RX PubMed=21788470; DOI=10.1128/AAC.01134-10;
RA Zhou H., Zhang T., Yu D., Pi B., Yang Q., Zhou J., Hu S., Yu Y.;
RT "Genomic Analysis of the Multidrug-Resistant Acinetobacter baumannii
RT Strain MDR-ZJ06 Widely Spread in China.";
RL Antimicrob. Agents Chemother. 55:4506-4512(2011).
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 -!- 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; CP001937; AEP07504.1; -; Genomic_DNA.
DR RefSeq; YP_005527000.1; NC_017171.1.
DR EnsemblBacteria; AEP07504; AEP07504; ABZJ_03044.
DR GeneID; 12115574; -.
DR KEGG; abz:ABZJ_03044; -.
DR KO; K00831; -.
DR BioCyc; ABAU497978:GL7S-3093-MONOMER; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
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 GO; GO:0008615; P:pyridoxine 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Pyridoxine biosynthesis; Serine biosynthesis;
KW Transferase.
FT REGION 89 90 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 250 251 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 55 55 L-glutamate (By similarity).
FT BINDING 115 115 Pyridoxal phosphate (By similarity).
FT BINDING 166 166 Pyridoxal phosphate (By similarity).
FT BINDING 185 185 Pyridoxal phosphate (By similarity).
FT BINDING 208 208 Pyridoxal phosphate (By similarity).
FT MOD_RES 209 209 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 373 AA; 41095 MW; 684CC629D083FBAC CRC64;
MPFFIVFHFY KGKIMRAYNF CAGPAALPTA VLEKAQQELL DWQGKGLSIM EMSHRSADYV
AVAEKAEADL RKLMNIPENY KVLFLQGGAS LQFSAIPLNL LGKNNKADYI HTGIWSEKAL
KEAKRYGDIN VVEAGIKVDG KFAISEQSEW NLSDDAAYVH YADNETIGGL QFAGVPDVKA
PLVCDFSSSI LSAPLDVSKF GLIYAGAQKN IGPAGLTIVI IRDDLLDQAK AEIPSILKYA
DQAKNGSMVN TPSTYAWYLS GLVFEWLLEQ GGVDAIHKVN LEKAQLLYGY IDSSDFYNNP
IAIPNRSIMN VPFTLADEAL EKQFLKEAEE NHLLNLAGHR SVGGMRASIY NAVPLEGVQA
LIRFMDDFAK RNG
//
