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Database: UniProt
Entry: A0A0S1S9G5_9FLAO
LinkDB: A0A0S1S9G5_9FLAO
Original site: A0A0S1S9G5_9FLAO 
ID   A0A0S1S9G5_9FLAO        Unreviewed;       354 AA.
AC   A0A0S1S9G5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   07-NOV-2018, entry version 14.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
GN   Name=serC {ECO:0000256|HAMAP-Rule:MF_00160};
GN   ORFNames=SB49_04650 {ECO:0000313|EMBL:ALM07169.1};
OS   Sediminicola sp. YIK13.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sediminicola.
OX   NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM07169.1, ECO:0000313|Proteomes:UP000063759};
RN   [1] {ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA   Kwon Y.M., Kim S.-J.;
RT   "Genome sequence of Sediminicola sp. YIK13.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALM07169.1, ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|EMBL:ALM07169.1,
RC   ECO:0000313|Proteomes:UP000063759};
RX   PubMed=26823585;
RA   Kwon Y.M., Kim S.J.;
RT   "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT   Bacterium Sediminicola sp. YIK13.";
RL   Genome Announc. 4:e01635-15(2016).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine.
CC       {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00347518}.
CC   -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC       (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00347441}.
CC   -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC       phosphonooxypyruvate + L-glutamate. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00347461}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00347488}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00347515}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|SAAS:SAAS00542307}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
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DR   EMBL; CP010535; ALM07169.1; -; Genomic_DNA.
DR   RefSeq; WP_062054309.1; NZ_CP010535.1.
DR   EnsemblBacteria; ALM07169; ALM07169; SB49_04650.
DR   KEGG; syi:SB49_04650; -.
DR   PATRIC; fig|1453352.4.peg.975; -.
DR   KO; K00831; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000063759; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00425538};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00425559};
KW   Complete proteome {ECO:0000313|Proteomes:UP000063759};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00023586};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063759};
KW   Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00425644};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00425627}.
FT   DOMAIN        5    340       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION       76     77       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   REGION      232    233       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   BINDING      41     41       L-glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00160}.
FT   BINDING     100    100       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     148    148       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     167    167       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     190    190       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   MOD_RES     191    191       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
SQ   SEQUENCE   354 AA;  39187 MW;  9163893C77A2DAA1 CRC64;
     MKKHNFSAGP CVLPQEVILK SAEAIQDFNG SGLSLIEISH RSKDFVAVMD KAQALALELL
     GLENKGYKAL FLHGGASLQF LMTAYNLLEK KAGYLNTGTW SDKAIKEAKL FGEVLEVGSS
     KSEGYNHIPK MYGVPNDLDY LHLTSNNTIY GTQIKNFPNV NVPLVCDMSS DIFSRQLDFS
     KFDLIYAGAQ KNMGPAGTTL VVVKESILGK VSRKIPSMMD YQVHISKESM FNTPAVFPVY
     VSMLTLEWLK NLGGIQAIEE INNKKAQLLY SEIDLNPLFK GYSVKEDRST MNATFNLTDE
     KLQTTFDAMW KEAGINGLSG HRSVGGYRAS MYNALTLESV GVLVDIMSEM ERKA
//
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