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Database: UniProt
Entry: M3A590_PSEFD
LinkDB: M3A590_PSEFD
Original site: M3A590_PSEFD 
ID   M3A590_PSEFD            Unreviewed;       514 AA.
AC   M3A590;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MYCFIDRAFT_59453 {ECO:0000313|EMBL:EME86279.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME86279.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME86279.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME86279.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; KB446556; EME86279.1; -; Genomic_DNA.
DR   RefSeq; XP_007922635.1; XM_007924444.1.
DR   AlphaFoldDB; M3A590; -.
DR   STRING; 383855.M3A590; -.
DR   GeneID; 19340523; -.
DR   KEGG; pfj:MYCFIDRAFT_59453; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_4_0_1; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
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   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932}.
SQ   SEQUENCE   514 AA;  55672 MW;  B9FCF1CC14BAE3D5 CRC64;
     MSPSVLNDGN VVDQEIDTTT NGIDVKASKS AVLHRSLHHD PLQVVGAQGH YLFLSNGQEI
     FDATGGAAVA CLGHGDVRVQ DALIKQMQEV SYCHSLFYAT RPAEELAKLL VDSTDGEMAR
     AFFISSGSEA MEAALKMARQ YHLEKPCPEP TRAHFISRHQ SYHGTTLGAL AAGGHVARRA
     IFEPILSVNT SQVSPCYAYR GVSSWTSNGP NDTDAAFVKR LEAELDAEFQ RIGPKNVAAF
     IAEPVVGAAL GCVPPVPGYF KTIRRVCDKY GALLIFDEVM SGTGRCGPEA SERFPKPLHA
     WQDPLIGVVP DIMTMGKSLG GGYMPIAAMM ASRDVVGALQ EGTGSFSHGQ TYQGHPLACK
     AALTVQKIIQ KDDLVANVRR QGALLGRLLR ERLASNPLVG DIRGKGLFWG IEFVRNKASK
     EPFDPSTGVA MGIHELGMQK PYNISLYPGT GSADGRRGDH IIVAPAYNIT AEEVRFVIDT
     VVAVINRYFK HHHSSDWIGS KVGDRETGLR KPRR
//
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