ID A0A0D1D5E0_9RHOB Unreviewed; 457 AA.
AC A0A0D1D5E0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Ddc_2 protein {ECO:0000313|EMBL:KIT15198.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:KIT15198.1};
GN Name=ddc_2 {ECO:0000313|EMBL:KIT15198.1};
GN ORFNames=jaqu_30210 {ECO:0000313|EMBL:KIT15198.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT15198.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT15198.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT15198.1,
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|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:KIT15198.1}.
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DR EMBL; JYFE01000055; KIT15198.1; -; Genomic_DNA.
DR RefSeq; WP_043919807.1; NZ_JYFE01000055.1.
DR AlphaFoldDB; A0A0D1D5E0; -.
DR STRING; 935700.jaqu_30210; -.
DR PATRIC; fig|935700.4.peg.3123; -.
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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
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 PRINTS; PR00800; YHDCRBOXLASE.
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 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 457 AA; 49700 MW; 64E82EB440268D54 CRC64;
MDHDDLNLWA KRAADWVRDY HAGLRDRPVR AQVAPGDLLA QLPGVAPEAA EPVEEIFADF
ERLIPGATTH WQHPRFFAYF PANASPASML AEQLANGIAA QGMLWQTSPA ATELEQAMVG
WLRDALGLPD DVTGTIHDTA TTATLCAVLT MRERALDYAG LTEGLSGGPR LRVYASAQTH
SSVDKAVRLA GIGQDNLVKV PVRDDLSMDP DALAAAIAAD REAGHLPCGV VFCAGGTGVG
AFDDIAACLP ACAGLPTHVD AAWAGSAMVC EEFRPLWAGA ERCDSIVFNP HKWMGAQFDC
CVQFLRDPVA QVNTLGLRPD YLRTLEGEDV TNFNEWTVPL GRRFRALKLW FVLRAYGLDG
IRGRIRDHVA WAEALAGRLR AMEGVEITSE PRLALFSFAL ESDAATEALL TAINAEGRVY
LTQTRHRGRF VIRVSVGSWD CTEADVMEVA QAVERLR
//
