ID A0A0D1CTB0_9RHOB Unreviewed; 465 AA.
AC A0A0D1CTB0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Ddc_1 protein {ECO:0000313|EMBL:KIT18007.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:KIT18007.1};
GN Name=ddc_1 {ECO:0000313|EMBL:KIT18007.1};
GN ORFNames=jaqu_02340 {ECO:0000313|EMBL:KIT18007.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT18007.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT18007.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT18007.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
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|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:KIT18007.1}.
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DR EMBL; JYFE01000006; KIT18007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1CTB0; -.
DR STRING; 935700.jaqu_02340; -.
DR PATRIC; fig|935700.4.peg.256; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000032232; 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; 3.90.1150.170; -; 1.
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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
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:UP000032232}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 465 AA; 49669 MW; 23565E22C37E9EF6 CRC64;
MMEGHRLDPA DWDAFSEALE DAARACADRL RHARDLPWQP PPPDMADRVA LDEVAAGDPG
VIDAILRDIV PYSTGNTHPR FFGWVHGTGT PLGVAAEMIA AAMNANMGGR DQGGAHVERA
VLSWLHRVAG WPPDASGLLT TGTSQATILA LSCARMRAFP KVREQGIGAL PPLRVYAAEG
AHSCVKKALE VMGHGSVALR GISAPGGRMD VDALSQAIAE DRAEGWSPLA VVGTVGSVNL
GTFDDLSALA DLCAAEDLWL HADAAFGFWT RLADLPWRDL SVGIERADSL ATDFHKWMSV
PYDCGAVLIR DHDLHLSTFR ERPAYLSEGQ ALAGGEWWAT DYGFDLSRGF RALKVWATIR
GLGTDALGAQ ITDNCRQAAY MGELAEASDV LDLAAPVVSN LCVIRPRRGE AAAIAAELQL
SGDAVFSTTL VDGVSCLRAA IVNHRTTRAD VERAVRAVEQ VIRSA
//
