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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//