ID J0VA84_9BACT Unreviewed; 416 AA.
AC J0VA84;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:EJF11117.1};
GN ORFNames=O71_05124 {ECO:0000313|EMBL:EJF11117.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF11117.1, ECO:0000313|Proteomes:UP000003746};
RN [1] {ECO:0000313|EMBL:EJF11117.1, ECO:0000313|Proteomes:UP000003746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF11117.1,
RC ECO:0000313|Proteomes:UP000003746};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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|ARBA:ARBA00009533, 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:EJF11117.1}.
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DR EMBL; AKIS01000031; EJF11117.1; -; Genomic_DNA.
DR RefSeq; WP_007653680.1; NZ_AKIS01000031.1.
DR AlphaFoldDB; J0VA84; -.
DR PATRIC; fig|1144253.3.peg.1008; -.
DR Proteomes; UP000003746; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase 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 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 PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF18; HISTIDINE 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}.
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 416 AA; 46585 MW; B8CBB8DFE9484BE3 CRC64;
MQQWTKLNKE TIRTIVFNAL EENVNFYDEN ILGIPGSHLD NKVFYQDAPF LKDAPFLTAL
IHNPNHIGCH TLGASESFFR GTHQIERELI GLCAEQILKA EPGSCDGYVA AGGTEANLQA
IWIYRNYFRN IDGVRNNSIC ILCSRDSHYS MSKAANVFDL DIATVRVDDN TRAIDEKHLQ
EVITAQKAKG KSHFIVVANM MTTMFGSVDN ADIYAAALEA NGCQFMIHVD AAFGGFIYPF
TNPDNTLNFQ NKHITSVTLD AHKMVQAPYG TGIFLIRKGL MQHANTKEAS YVEGEDFTLI
GSRSGANAIA VWMILMTYGR YGWEEKTTTL LNRAAWLAAE LDKAGIAYYR NPYSNIITIR
SEHLNKGIAG KYGLVPDNHQ DANWYKVVVM DHVTIDRLIP LLEDLKAYQH EACLAE
//
