ID A0A151UME5_9GAMM Unreviewed; 242 AA.
AC A0A151UME5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|ARBA:ARBA00021164};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
DE Flags: Fragment;
GN ORFNames=BG74_00190 {ECO:0000313|EMBL:KYP97817.1};
OS Sodalis-like endosymbiont of Proechinophthirus fluctus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1462730 {ECO:0000313|EMBL:KYP97817.1, ECO:0000313|Proteomes:UP000217500};
RN [1] {ECO:0000313|EMBL:KYP97817.1, ECO:0000313|Proteomes:UP000217500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPI-1 {ECO:0000313|EMBL:KYP97817.1,
RC ECO:0000313|Proteomes:UP000217500};
RA Boyd B.M., Allen J.M., Koga R., Fukatsu T., Sweet A.D., Johnson K.P.,
RA Reed D.L.;
RT "Two associated bacteria (Sodalis and Rickettsia) associated with the seal
RT louse Proechinophthirus fluctus (Phthirapter: Anoplura).";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001607};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001871};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYP97817.1}.
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DR EMBL; LECR01000002; KYP97817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151UME5; -.
DR PATRIC; fig|1462730.3.peg.1258; -.
DR Proteomes; UP000217500; Unassembled WGS sequence.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KYP97817.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Reference proteome {ECO:0000313|Proteomes:UP000217500};
KW Transferase {ECO:0000313|EMBL:KYP97817.1}.
FT DOMAIN 4..241
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT NON_TER 242
FT /evidence="ECO:0000313|EMBL:KYP97817.1"
SQ SEQUENCE 242 AA; 26420 MW; 9C75E81B0EE53764 CRC64;
MNQVFNFSAG PAMLPAEVLR KAEQELCNWH GLGTSVMEIS HRSKEFLEVA QSSEQDLREL
LAIPDNYKVL FCHGGARAQF AAVPMNLLGD AASADYIDGG YWAHSAIKEA QKYCDPRVID
VTTEVDGLRA IKPMRDWALS TDGAYVHYCP NETIDGLAID ELPDFGDRVV VADFSSTILS
HPLDVSRFGV IYAGAQKNIG LAGLTLVIVR EDLLGRASKA LPSILDYSVL AENDSMFNTP
PT
//
