ID   W7I7V7_9PEZI            Unreviewed;       469 AA.
AC   W7I7V7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=2,2-dialkylglycine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DRE_02192 {ECO:0000313|EMBL:EWC48423.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC48423.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC48423.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC48423.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-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}.
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DR   EMBL; KI966390; EWC48423.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7I7V7; -.
DR   HOGENOM; CLU_016922_10_0_1; -.
DR   Proteomes; UP000024837; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  49894 MW;  8FA0DA08F4693EAF CRC64;
     MAPCTNPIGT GAGASEPANG IDKPVDQAQL QADAATTLIG IGTPYHRDII VRAQGTSIYT
     AAGHRMQDWT SGQMSCLLGH GNPEIVAVIA HHAATLDHLF SGMLSPPVVN LAKRLTGLAP
     PGLDRAMFLS TGGESNEFAI RIAKLCTGKF EVVGLSASWH GVTAGAIGAQ YHSGRAGYGP
     MVPGNFALPA PNAYRSIFRH PDGSHDWRTE LSYGFSLIDR QSCGSLAAVI VEPILSSGGM
     HPLPPGYLKA LKEHCTARDM LLIIDEAQTA IGRAGDMFAF QHYPEDDGVV PDILTLSKTL
     GNGIALSAVL VSEAIALRAE QRGFMYYTTH MNDPLPAAVG DKVLEIVVRD GLVDRARRLG
     EVLHAGLQRL KTRYACIGDV RGRGLMAGVE IVTDRESKRP AGELGGEIGD RMAELGVWAQ
     LSTHVSFAGV FRIAPPITIT EEELEAGLEV MEEALRITPG TMPLYEVPV
//