ID L5N658_9BACI Unreviewed; 502 AA.
AC L5N658;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase RhbB {ECO:0000313|EMBL:ELK46087.1};
GN ORFNames=D479_12628 {ECO:0000313|EMBL:ELK46087.1};
OS Halobacillus sp. BAB-2008.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK46087.1, ECO:0000313|Proteomes:UP000010769};
RN [1] {ECO:0000313|EMBL:ELK46087.1, ECO:0000313|Proteomes:UP000010769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK46087.1,
RC ECO:0000313|Proteomes:UP000010769};
RX PubMed=23469348;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BAB-2008.";
RL Genome Announc. 1:E00222-12(2013).
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:ELK46087.1}.
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DR EMBL; ANPF01000051; ELK46087.1; -; Genomic_DNA.
DR AlphaFoldDB; L5N658; -.
DR PATRIC; fig|1246484.3.peg.2578; -.
DR eggNOG; COG0076; Bacteria.
DR Proteomes; UP000010769; Unassembled WGS sequence.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1650.10; PLP-dependent transferases; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000010769}.
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 502 AA; 55377 MW; 566C71C9CBF84F99 CRC64;
MTTACKQTNT AFDHLFLHGE AGLTAFRKQM ELVTEAVLDV YEEVDQPFIG KSHQQVRAEI
QAMDTDSVNG RALEDVWNEL KDPVLKNSLH VSHPQSMAHL HCPPLVAGIA AEVMIGAWNQ
SMDSWDQSPA ATYVEEMLVK YWADLVRFPE EADGVFTSGG TQSNYMGMLL ARDAYCLKRF
GHDVQKKGLP ENFRKLRVLC SEEAHFSVRK SLAQLGLGED AVIPVAVNEH HRMDPAALKD
TLDEMEQTGL HPFAVAATCG TTDFGSIDPL EEIADICQER GIWFHVDAAY GGGLLFSRAH
KGKLAGLERA DSVTLDFHKW LYQPISCGLF LLKDGGHMRL LSHHADYLNP KADEEDGILN
LVNKSVQTTR RFDALKVLVT LKTVGTEVLG DMVDQTMATA RFAADRLAGH PDFLVENAEP
EMSAVVFQYK GSGDVDRGAL NRQIQQDLFT SGKPIIAKTV VRGETYLKCT ILNPRTTEAD
VKAVIEAVLD AADKRTTGGD SH
//
