ID A0A150V6B9_9PEZI Unreviewed; 415 AA.
AC A0A150V6B9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=M433DRAFT_143345 {ECO:0000313|EMBL:KYG46054.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46054.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46054.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46054.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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 -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC {ECO:0000256|ARBA:ARBA00006904}.
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:KYG46054.1}.
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DR EMBL; JPDO01000132; KYG46054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V6B9; -.
DR STRING; 766039.A0A150V6B9; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000075602; 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:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 10..92
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 175..404
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 415 AA; 45133 MW; E65911E7A8D6C4E5 CRC64;
MPSRSEIDYF GAGPAPLPTP VLESAAEVLL NYNNTGIGIT EISHRSAEAT AILNQTQTNL
RKLLDIPTSD GPDGYQILFL QGGGSGEFSA AVYHMVGIWL GALAKRKQQG LDRDVGNLRL
DYYVTGSWSL KASQEAARLV GSEHVNIVTD ARKYHKDGKF GVIPPSDTWT QTKNQDEVAL
TYYCDNETVD GVEFPSPPSG ENLVADMSSN FLSRPVDVRR HAAIFGGAQK NVGTTGITLA
IVSNAILPPH AEMADPALLR KFGLPVGPVV LDWPTIAKNN SLYNTLPIFD VWIAGQVMQR
LLEQSPEGKS PRIATQEAEA DKKAKMLYEA LDANEDVYQV VPVKSVRSRM NLCFRVKGGN
AEAEKSFLKG AESRGLLGLK GHRSVGGIRI SNYNAVQMAA VEKLTQYLND FANEK
//