ID B8G779_CHLAD Unreviewed; 471 AA.
AC B8G779;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:ACL24036.1};
DE EC=4.1.1.28 {ECO:0000313|EMBL:ACL24036.1};
GN OrderedLocusNames=Cagg_1126 {ECO:0000313|EMBL:ACL24036.1};
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL24036.1, ECO:0000313|Proteomes:UP000002508};
RN [1] {ECO:0000313|Proteomes:UP000002508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; CP001337; ACL24036.1; -; Genomic_DNA.
DR AlphaFoldDB; B8G779; -.
DR STRING; 326427.Cagg_1126; -.
DR KEGG; cag:Cagg_1126; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_3_1_0; -.
DR Proteomes; UP000002508; Chromosome.
DR GO; GO:0004058; F:aromatic-L-amino-acid 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}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 471 AA; 52131 MW; 0493AC3815A87ED4 CRC64;
MMHPDEFRRI GYQIIDMIAD YRATIANRPV WSQLRPGEFR SQLPATPPEQ PEPPEAILAD
VERLIIPGLS NWQHPRFFGY FPANASLASL LGDFLSGGLG QLGLNWQASP PLTELEELTT
DWMRQLLGLS EAWRGVIQDT ASTSTLVALL CARERASDHS QVRGGLQALP QPLVVYTSIQ
SHSSVEKAAL LAGFGRDNLR LLPVDDTFAL RVDTLADAIA TDRAAGRVPC AVVASIGATA
TTACDPLEPI GELCRREGIW LHVDAAMAGS AMILPECRYL WQGIEQADSL VLNPHKWLGA
AFDCSLYYVR DPQHLIRVMS TNPSYLQTSA DGAVTNYRDW GIPLGRRFRA LKLYFLLRCE
GAEGLRTRLR RDIANARWLA EQIDATPHWR RLAPVPLQTV CVRHEPPGLT GEDLDRHTLR
WVGAINASGA AYLTPAMLDG RWMVRISIGA EPTEHTDVAA LWALMQEVVR G
//
