ID   A0A093X1H7_9PEZI        Unreviewed;       154 AA.
AC   A0A093X1H7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFX86585.1};
DE   Flags: Fragment;
GN   ORFNames=O988_09489 {ECO:0000313|EMBL:KFX86585.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX86585.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFX86585.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX86585.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:KFX86585.1}.
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DR   EMBL; JPJR01002835; KFX86585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093X1H7; -.
DR   STRING; 1391699.A0A093X1H7; -.
DR   HOGENOM; CLU_1708592_0_0_1; -.
DR   Proteomes; UP000029329; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11999:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029329}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFX86585.1"
SQ   SEQUENCE   154 AA;  16359 MW;  BAD99827248C9998 CRC64;
     AGGRAWVHVD GAFGIFARSL PDTDEFASLR ASSEGLQYAD SITGDCHKSL NVPYASAFLL
     TRSQTDLSNV CTNGSAAYLK TSGTDTTPSP LNHGLENSRR FTALPIYAVL HAHGREGLAL
     LFATQVRLAR AVADMISGLD GYELLPTSDV GAWD
//