ID A0A0T5ZP84_9CHLR Unreviewed; 524 AA.
AC A0A0T5ZP84;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:KRT64554.1};
GN ORFNames=XU10_C0001G0002 {ECO:0000313|EMBL:KRT64554.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT64554.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT64554.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT64554.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT64554.1}.
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DR EMBL; LDXM01000001; KRT64554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZP84; -.
DR STRING; 1640513.XU10_C0001G0002; -.
DR PATRIC; fig|1640513.3.peg.2; -.
DR Proteomes; UP000051896; 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:0006520; P:amino 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; 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 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.
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 REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 524 AA; 57541 MW; B6E19F6A934733CB CRC64;
MTDRPDAPSS GRPSDLERFG WHPEPELLGY TDAAESREAL ERLGEAAWRA ALDYLYGEGL
RRPVGPDDHP ALRRGFFGPD GSPSPAPPLP APSAELLEEF RRRLAPHQFN AQHPRAFSYF
TPPPLPISIV GELLAQWTNQ GVDIGPSSPT ATLVEEEVVA WLRELVGYGP ESFGVLTSGG
VMANLMALTV ARDIGLARLL GRSEPPRGSA LEGVRAYVSD QAHFSIARGL DVLGFPAETL
RVLPSDERFR LRGGPVAAAI ADDRAAGLTP WLIAAVTGST NTGSVDLTDE LADVAERDGL
WLHVDAAYGG AVRLAAREAG RVPALERADS VTLDPHKWFF QPYDIGGLLV KRRDDLRQTF
HRSPEYYRTS RPEDEPLHWY QYSLEGTRRF RALKLWLTWK SLGTEGFGRL VEANLALAAH
LARRCRESDD FDATPEEPEL SVVCFRHLPG GRAAAARLDP AALEALDRHQ DRLQRALEVS
GDGWVSTTRL RGATWLRAGI VNYLATEADV DRLLATLRRL AAGL
//
