ID A0A094DEH5_9PEZI Unreviewed; 244 AA.
AC A0A094DEH5;
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:KFY64689.1};
DE Flags: Fragment;
GN ORFNames=V496_03084 {ECO:0000313|EMBL:KFY64689.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY64689.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY64689.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
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:KFY64689.1}.
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DR EMBL; JPJY01000485; KFY64689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DEH5; -.
DR STRING; 1420909.A0A094DEH5; -.
DR HOGENOM; CLU_011856_6_1_1; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000029302; 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:UP000029302}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFY64689.1"
SQ SEQUENCE 244 AA; 26538 MW; A9D8CF9C4B9ACC1C CRC64;
EVNTGRYFGG EEEMEGLKAC LEECAPGAAW IHVDGAFGIF ARSLPETEEF ASLRASSEGL
QYADSITADC HKALNVPYAS AFLLTRSPTD LSNVCNNGAA AYLKTSATDP IPSPLNHGLE
NSRRFSALPI YAVLHAHGRE GMALLFATQV RLARAVARMI GELEAYELLP TAEVGEVGTI
VLFRARNEEL NEGLLGRIND QNRIFLSGTS WEGRGAVRVA VSGWEIDVEK DTRVIREVLE
KVAE
//