ID SERC_PSEAE Reviewed; 361 AA.
AC Q9HZ66;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; OrderedLocusNames=PA3167;
OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS 12228).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT opportunistic pathogen.";
RL Nature 406:959-964(2000).
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-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; AE004091; AAG06555.1; -; Genomic_DNA.
DR PIR; H83250; H83250.
DR RefSeq; NP_251857.1; NC_002516.2.
DR ProteinModelPortal; Q9HZ66; -.
DR SMR; Q9HZ66; 4-361.
DR STRING; 208964.PA3167; -.
DR DNASU; 882700; -.
DR GeneID; 882700; -.
DR KEGG; pae:PA3167; -.
DR PATRIC; 19840899; VBIPseAer58763_3310.
DR PseudoCAP; PA3167; -.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
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; 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; FALSE_NEG.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1 361 Phosphoserine aminotransferase.
FT /FTId=PRO_0000150198.
FT REGION 77 78 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 238 239 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 43 43 L-glutamate (By similarity).
FT BINDING 103 103 Pyridoxal phosphate (By similarity).
FT BINDING 153 153 Pyridoxal phosphate (By similarity).
FT BINDING 173 173 Pyridoxal phosphate (By similarity).
FT BINDING 196 196 Pyridoxal phosphate (By similarity).
FT MOD_RES 197 197 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 361 AA; 39949 MW; 9D787E60951018DF CRC64;
MSKRAFNFCA GPAALPDAVL QRAQAELLDW RGKGLSVMEM SHRSDDYVAI ASKAEQDLRD
LLDIPSDYKV LFLQGGASQQ FAEIPLNLLP EDGVADYIDT GIWSKKAIEE ARRYGTVNVA
ASAKEYDYFA IPGQNEWTLT KDAAYVHYAS NETIGGLEFD WIPETGDVPL VTDMSSDILS
RPLDVSRFGL IYAGAQKNIG PSGLVVVIVR EDLLGRARSV CPTMLNYKTA ADNGSMYNTP
ATYSWYLSGL VFEWLKEQGG VTAMEQRNRA KKDLLYKTID ASDFYTNPIQ PSARSWMNVP
FRLADERLDK PFLEGAEARG LLNLKGHRSV GGMRASIYNA LGLDAVEALV AYMAEFEKEH
G
//
