ID A0A0N0NM81_9EURO Unreviewed; 546 AA.
AC A0A0N0NM81;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:KPI40151.1};
GN ORFNames=AB675_11467 {ECO:0000313|EMBL:KPI40151.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI40151.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI40151.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI40151.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) 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:KPI40151.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000013; KPI40151.1; -; Genomic_DNA.
DR RefSeq; XP_018000114.1; XM_018140316.1.
DR AlphaFoldDB; A0A0N0NM81; -.
DR STRING; 1664694.A0A0N0NM81; -.
DR GeneID; 28732197; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000038010; 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:UP000038010}.
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 58381 MW; 2AA1F1C657DCA41A CRC64;
MEAPTSLTQL LMLLHNLVRT QKNLPQELAP GVAGSNSPLP QHDIPGLPIA SSSLSEQPLA
LKSALSPNYY GFVTGGSTPA ALLADWLVSL YDQNVQVHLP RETISTTVEV AALNQLVDLF
RLPRETWGVG SSSSHGGGTF TTGATASNIL GLALGREWVI QQHANDINVS VGNLGLIDAM
RYAGLYSLRV LTTLPHSSIA KAASVVGIGR CQVTSVIKEG TDLDIDLDAV ERYASEPGTG
CILVISAGEV NTGRFATLGS QEGGNQPPVW QQLGEICDRY NVWVHVDGAF GLFGRALLPD
PSSARQNGDG NAGADTDYSH ILNGVTGLEH LADSVTGDAH KLLNVPYDCG FFFTRHKDLS
EQVFVNGGAA YLAAPASAPA AESLDVSEEE GGRGGGAEGG FRVGDAIQSP LNIGLENSRR
FRALPVHATL IAYGREGYVG MLRRQIGLAR HIVRFLWNHP DYDVLPQDAK MEDEAVMRTF
IIVLFRAKDE KVNEVLVERI NASGKIYVSG TRWKGEKAAR IAVSSWMADV EQDGKLVEGV
LGEVVK
//
