ID   W9YK56_9EURO            Unreviewed;       448 AA.
AC   W9YK56;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A1O3_01474 {ECO:0000313|EMBL:EXJ92918.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ92918.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ92918.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ92918.1};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:EXJ92918.1}.
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DR   EMBL; AMGY01000001; EXJ92918.1; -; Genomic_DNA.
DR   RefSeq; XP_007729808.1; XM_007731618.1.
DR   AlphaFoldDB; W9YK56; -.
DR   STRING; 1182542.W9YK56; -.
DR   GeneID; 19165608; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_4_0_1; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:UP000019478}.
SQ   SEQUENCE   448 AA;  48001 MW;  F1996D0E0016C946 CRC64;
     MIAPTLSSIP ATSAILHRSF SKEYPTAASG QGVYIQDHTG RLVLDGSSGA AVSCLGHGHK
     KVIEAIVEQA QQMSFAHTSF FTSDPAENLA SVLISTCPDV FSKVMFVSSG SEAVESALKL
     ARQYHLCNGQ PDRHIFISRR FAYHGNTLGA LSAGFNPPRR DPFQPMLSQA FRHVSPCFFT
     RDGLPGEDEE SYVDRLVAEY ETTISSLGSE KIAAIIVEPV SGATLGAVPA ARGYLGRLRE
     LCDRYGCLLI FDEVMCGMGR VGTMHAWQSL GGIAPDLQTI GKGLGAGYQP ISAILIANKV
     HAVLERNHEQ RPFVSGHTYQ GHSIGCAAAL ATQRAIAEDK LLDNVRRMGE RLSRRLKKET
     PMLKEVRGLG LFQAVEFATA TATPPGSSIA AAVASTCLEN GVAVYLCSSA VDAVLFAPPF
     IISESEIDKL VDVFVQSVKQ TIEKAKGS
//