ID   W9Y1E0_9EURO            Unreviewed;       468 AA.
AC   W9Y1E0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=2,2-dialkylglycine decarboxylase (Pyruvate) {ECO:0000313|EMBL:EXJ86303.1};
GN   ORFNames=A1O3_03254 {ECO:0000313|EMBL:EXJ86303.1};
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:EXJ86303.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ86303.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ86303.1,
RC   ECO:0000313|Proteomes:UP000019478};
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:EXJ86303.1}.
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DR   EMBL; AMGY01000003; EXJ86303.1; -; Genomic_DNA.
DR   RefSeq; XP_007731582.1; XM_007733392.1.
DR   AlphaFoldDB; W9Y1E0; -.
DR   STRING; 1182542.W9Y1E0; -.
DR   GeneID; 19167382; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_10_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; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:EXJ86303.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   468 AA;  50880 MW;  17AC1EF2448DC2F6 CRC64;
     MAPHAQDIVV SGSESTNTNK SQAYVPSLYH DVDEQDLQQS AREYLANYGI PLHTDIITGA
     KDLYVYNSTG HRILDWTSGQ MSCLIGHGHP EIVSVIHDYA SNLDHLFSAM VSPPVINLAK
     RLASVLPKPL SKTVFLSTGG ESNEAAIKMA KIYTGKFEIV GLGASWHGMT AQALSSQYFY
     GRRGQGPLVP GSHQLPAPNA YRSIFRHPDG SYDWETELNY GWEMVDRASC GSLAACIVEI
     IQSTGGMHVL PPGYLTALKK HCEKRGMLLI IDEAQTGVGR TGDLFAFNHE NVVPDILTLS
     KTLGNGIPLS AVVTSPEIDR VCTERGFMFI TTHVNDPMPA AVGDKVLEIV QRDNLVENSR
     LMGLHLEAGL KKLQSRYGCV GDVRGRGLMM GMEIVADRDS KAPSPELAQK LADKIYELGL
     WANLSSHPVS GGSFRIAPPI TTTRAQIDEG IEILERALAA TKGSQPLY
//