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Database: UniProt
Entry: A0A1L9N9X4_ASPTC
LinkDB: A0A1L9N9X4_ASPTC
Original site: A0A1L9N9X4_ASPTC 
ID   A0A1L9N9X4_ASPTC        Unreviewed;      1053 AA.
AC   A0A1L9N9X4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN   ORFNames=ASPTUDRAFT_53329 {ECO:0000313|EMBL:OJI86029.1};
OS   Aspergillus tubingensis (strain CBS 134.48).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI86029.1, ECO:0000313|Proteomes:UP000184304};
RN   [1] {ECO:0000313|Proteomes:UP000184304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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}.
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DR   EMBL; KV878187; OJI86029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9N9X4; -.
DR   STRING; 767770.A0A1L9N9X4; -.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_53329; -.
DR   OMA; ANKETDF; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000184304; Unassembled WGS sequence.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:InterPro.
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; IPR027796; OTT_1508_deam-like.
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   Pfam; PF14441; OTT_1508_deam; 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:UP000184304};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          9..122
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          167..414
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          474..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  119107 MW;  DCA8AA23099AF7C4 CRC64;
     MKREDITYLG AGPASLPTDV LATAAQALQN YQDTGLGVAE HSHRSEIATN ILNGAKADLA
     NFLDIPDTYE ILFLQGGGSG QFDATVYNLV SIWAEKQRQQ IIKEKAGISE DEVISELRKK
     VESELKLDYL VTGSWSLKAS QEAVRLLGSE YVNIVSDSRT VNDGKFGKIA DESTWKLSRK
     AALVYKCENE TVDGVEFPSF PKVLEPKGTD EDPIVVGDFS STILSRRIPV QNYSIIFFGA
     QKNLGVAGIT GVIIKKDLLP PVSSPCSPAI LRKLGLPVAP TILDYSVAAK NNSLYNTLPI
     FDVYIAGQVL KKLLASFPDK VDGQQAVADR KAKLIYETLD AYPEVYKVVP AKEVRSRMNA
     CFRVIKGGNV DDAEKAFLKG AVERGITGLK GHRSVGGIRA SNYNAIPESG IEKLAAYLKE
     FYAGLVVHNR MSHVKKLHLL RPTAGIKTDV WNLPNEIESQ ITTLAAVLQV QQQQRTPIAR
     EEEEGEEETD DEETSNEQLH NHELGSSAVV APLASENTKN LRRCFLDQLA ELLCYKKDAH
     YVTCTYLREE VDEVTILASR NAAWEDKDIR LLESLAGTLE QLAVRDPFNL DFKPDLEREF
     SEYYTPRLKY HVKQLVNFLE AVKGETGLVD FLRNFFSRRI SSQRIWANID FRYRIEVLPK
     ANKIVRELGY ILRPIVAADT FDKAAREISN FQRVKIELLP GYKAESVTPS LSLVSRTPQY
     LGISKKTCFM CGHFLQSLSQ FQARNNHGKV YSQWRLPKSL IMPPKYCETL DNAARNLRDV
     MQCEFAPQHM RIWSPFSRHV PDPKLQARES EWLSYRSPRE IAVRSNNDVA KAFGILYFTS
     AADQHRLFEL YCSLVNDWGV GEEELREAWQ QNKLKEFILF RSSQIPSTWI HNESHWISQQ
     DGFAANKETD FNIVLESQKH VLKPEDQQVP YQLWKPREKL EAFVFLCQIR NGYIPQADEY
     NWISLGFCTA RDGSETQKVA ELYKELLDTC VFEEFWKAMV ESKMVDLFRK YGLGDAIAEL
     RNFETLLSAV GTTHQSCYRG LWILQLSNTT GAE
//
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