ID W9YHC0_9EURO Unreviewed; 469 AA.
AC W9YHC0;
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:EXJ91923.1};
GN ORFNames=A1O3_00473 {ECO:0000313|EMBL:EXJ91923.1};
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:EXJ91923.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ91923.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ91923.1,
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:EXJ91923.1}.
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DR EMBL; AMGY01000001; EXJ91923.1; -; Genomic_DNA.
DR RefSeq; XP_007728813.1; XM_007730623.1.
DR AlphaFoldDB; W9YHC0; -.
DR STRING; 1182542.W9YHC0; -.
DR GeneID; 19164613; -.
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:EXJ91923.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 469 AA; 51180 MW; 208D82242774D941 CRC64;
MAPMLEENSP STVNINITSK SIDTPTLYSN VDEEQLKVAA EACLANYGTE FEKDIMTGSK
GLYVFTANGH KVLDWTSGQM SCLIGHGHPE IVSTIQDHAA QLDHLFSGML SPPVIRLAQR
LTSVLPPGLD KAFFLSTGGE SNEAAIKLAK VYTGKFEIVG LGASWHGVTA QALGTQYHFG
RKGQGPLMPG MHMLPPPNSY RSIFRKPDGS YDWETELDYG WDMIDRASCG SLAACIVECI
QSSAGMHVLP PGYLRALKKH CEKRGMLLIV DEAQTGVGRC GDLFAINHEG DSVVPDILTL
SKTLGNGLPL SAVVMSSEIE RICAERDYCF YTTHVNDPLP ASVGDKVLEI VLRDNLVENS
RTMGLYLQAG LQRLKSRYGC IGDVRGRGLM AGVEIVRDRE TKAADIDLAR RMAAKMYELG
LWANLSSHSS FSGVFRIAPP IVITREQLDQ GLDIMERAFS ETAGTMPLY
//