ID A0A1A7KNK6_9FLAO Unreviewed; 455 AA.
AC A0A1A7KNK6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:OBW43346.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:OBW43346.1};
GN Name=ddc_1 {ECO:0000313|EMBL:OBW43346.1};
GN ORFNames=AB670_00263 {ECO:0000313|EMBL:OBW43346.1};
OS Chryseobacterium sp. MOF25P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1664318 {ECO:0000313|EMBL:OBW43346.1, ECO:0000313|Proteomes:UP000092708};
RN [1] {ECO:0000313|EMBL:OBW43346.1, ECO:0000313|Proteomes:UP000092708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOF25P {ECO:0000313|EMBL:OBW43346.1,
RC ECO:0000313|Proteomes:UP000092708};
RA David V.-J., Thomas B., Ramon P.Y., Thao N., David R., Richard E.,
RA Roderick C., Nikki M., Timothy W.J., Alexander A.E., Kimberley T.;
RT "A floR containing integrative conjugative element found in multidrug
RT resistant Chryseobacterium spp. isolates: exception to the general rule?";
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|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:OBW43346.1}.
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DR EMBL; LFEG01000006; OBW43346.1; -; Genomic_DNA.
DR RefSeq; WP_066674908.1; NZ_LFEG01000006.1.
DR AlphaFoldDB; A0A1A7KNK6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000092708; 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:UP000092708}.
FT MOD_RES 290
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 455 AA; 51226 MW; 55A4D7ADFFF8A9C3 CRC64;
MKNELIAIAN RSEQLFDAFS KKDAILDISV EDIRGKLSKY DFNEPKDLSE IIDDVEFALE
NWNLQTNHPL HFGLFQPSVT SSGVVADALA AIYNPQMATW WFSPAANEIE KHTLSFLISK
FGYDPEKTFA SFTSGGSESN YTAVITALTT RFPEYRNEGA FSLKKQPIIY VSQDAHDSIV
RAAHQSGIGR NAVVRIPVDD NRKMDVGQLV LQIESDKKQN KEPFMIVTTL GTTSYGVIDP
IEKILEINKD QKLWMHLDAA WGGGFVISRE AGPYLKGIDK VDSITWDPHK TLPIPTGAGF
FLTVHKEAMK KTFSVDASYV PDEIDGNVDS YKVSFAWSRR FIGLKIFMLL AESGSRNIGE
LLTHQIKMGN EFRKLLIENG WEIVGNSPLP VICFTHPYHR QNIENVLLNA LNRKKVWFSK
VDNNGTSVLR VCISSFKTDM SHLKILMDEL ELAIQ
//
