ID A0A031LRQ5_9GAMM Unreviewed; 510 AA.
AC A0A031LRQ5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:EZQ10154.1};
GN ORFNames=CL42_08575 {ECO:0000313|EMBL:EZQ10154.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ10154.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ10154.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ10154.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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:EZQ10154.1}.
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DR EMBL; JFYL01000025; EZQ10154.1; -; Genomic_DNA.
DR RefSeq; WP_035267116.1; NZ_JFYL01000025.1.
DR AlphaFoldDB; A0A031LRQ5; -.
DR eggNOG; COG0076; Bacteria.
DR Proteomes; UP000023816; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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; 3.90.1150.170; -; 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; 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}.
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 510 AA; 55993 MW; 0C01411FF8A3AD6C CRC64;
MVDFAEHRKA LLCNDAASIA DYTSAMDQAT QAVAAWLQND KMYTGGSIKE LRSAIAFNPS
KEGLGVEKSL ERMVELFLNK SLKVHHPHSL AHLHCPTMVT SQIAEVLINA TNQSMDSWDQ
SPAGSLMEVQ LIDWLRQKVG YGAGQAGVFT SGGTQSNLMG VLLARDACIA KNWKDENGNP
WSVQRDGVPA EAMRNVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVDEN ARMDMDALEK
TMAHLQNEGK IVACVVATAG TTDAGAIDPL KKVREITNKY GAWMHIDAAW GGALILSNNH
RDMLDGIELS DSITLDFHKH YFQTISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN
LVSKSLQTTR RFDALKLWMT IEALGEELYG SMIDHGVTLT RDVADYIKAT DGLELLVEPQ
FASVLFRVIP EGYPTELLDT LNQNVADELF ARGEANIGVT KVGQVQSLKM TTLSPVATLD
NVKNLLALVL AESDRIKASI ADGTYTPPID
//
