ID A0A0M2GZ73_9MICO Unreviewed; 484 AA.
AC A0A0M2GZ73;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:KJL39138.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:KJL39138.1};
GN Name=ddc_3 {ECO:0000313|EMBL:KJL39138.1};
GN ORFNames=RS81_02232 {ECO:0000313|EMBL:KJL39138.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL39138.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL39138.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL39138.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC 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:KJL39138.1}.
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DR EMBL; JYIZ01000052; KJL39138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2GZ73; -.
DR STRING; 92835.RS81_02232; -.
DR PATRIC; fig|92835.4.peg.2267; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000033956; 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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 484 AA; 49697 MW; FC07E345177B9962 CRC64;
MEDQTGATHP NNEDEIPAEG LPTRAGAELH RALDAAHRHA VAWLDSVAER PIRLETDVDG
ILGALDTTLH DESRSAAAVV DELAAIAEPG LMAMGSPRFY GFVIGGSHPA ALAADWLVSA
WDQNTGSRQP TPATAGLEEV AGAWLLELLG LPAGSGVGFA TGASSANFAC LVTARDAVLR
DRGYDASTGG LQAGPRLRFL AGDAVHTSVV LAGRLAGLGA PETVGADAQG RIDVPGLERA
LAADPDAATV VALQAGDVHS GAFDDFAIAI AVARDAGAWV HVDGAFGLWA AASSRYTDLT
DGVAEADSWA TDAHKTLNVP YDCGVAIVRD EAAMTSSLGA HAAYLPAVAA VSDPYDRVPE
LSRRARGVTV WAALRALGRR GVADLVDGLA DAASALADGF AEIPGLEVLN DVAFTQVCLA
SGDDAQTLAL GEWLRAEGTV WASSSNWQGR AVVRFAVSNR GTDAEAVART VDAVARGAEA
LGIR
//
