ID A0A0B9A131_BRELN Unreviewed; 576 AA.
AC A0A0B9A131;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Diaminobutyrate decarboxylase {ECO:0000313|EMBL:KHS52492.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:KHS52492.1};
GN ORFNames=AE0388_2142 {ECO:0000313|EMBL:KHS52492.1};
OS Brevibacterium linens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS52492.1, ECO:0000313|Proteomes:UP000031488};
RN [1] {ECO:0000313|EMBL:KHS52492.1, ECO:0000313|Proteomes:UP000031488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS52492.1,
RC ECO:0000313|Proteomes:UP000031488};
RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, 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:KHS52492.1}.
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DR EMBL; JTJZ01000019; KHS52492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B9A131; -.
DR PATRIC; fig|1703.6.peg.2038; -.
DR Proteomes; UP000031488; Unassembled WGS sequence.
DR GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000031488}.
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 375
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 576 AA; 61065 MW; 8FB8C08A6F582EA7 CRC64;
MTTSLLYDTE ATPTSAPLQT PEIPHTNSDL NAPTAAPEVA NPTLADVQNP TRTDALLGAH
SADEYTSLMH NVVDALGERF RTTERAASAK DRSGLQAAVD AVDLDTAGVG NAEALREVDA
LYADNAVWFH HPSYVAHLNC PVAVTAVAAE AMLAAINTSV DTYDQSEVAT LMERRLIDWT
CGHLGFAGGD GIFTSGGTQS NLHALFLARE NVLAGLAERA DESDRDGSDD AKPRRGGSDL
GEPTRRDQLS RLRILATDQA HFSVSRAAFL LGLDPEAVVT VPTDGTGRMD AEALNASLLA
IEANDQVPMA VVATAGTTDL GVIDPLKTIA EVCDSANVWL HVDAAYGGGL LWAPQRAHLL
DGISGATSVT IDFHKTFFQP VSSSALLIRD ASLFAPTIHH HDYLNPEAEA QAADAEPNQV
DKSLQTTRRF DALKLWTTLR ARGAGEIGVM IDAVCDLATD VRALLDDQAD FEVLGASDLS
TVLFRFTPSN ADRATCDELV PLIRRVLFRS GRAAIARTVI DGTPWLKLTL LNPDTSIDDI
TAVLDLVRAT GHGILAGRDL EGTADIQGAV TEGGAS
//
