ID A0A0T5ZMA7_9CHLR Unreviewed; 533 AA.
AC A0A0T5ZMA7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=XU10_C0006G0086 {ECO:0000313|EMBL:KRT63939.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63939.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT63939.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63939.1};
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:KRT63939.1}.
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DR EMBL; LDXM01000006; KRT63939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZMA7; -.
DR STRING; 1640513.XU10_C0006G0086; -.
DR PATRIC; fig|1640513.3.peg.780; -.
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; 3.90.1150.10; 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 REGION 510..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 533 AA; 58387 MW; 5EFF7A3213427804 CRC64;
MPDAAAPTEL EALFATLDHA QREGVRDMDP ETFRRAGHAV VDVMADYLAG VERYPVLPRV
APGELRARFP ATPPESPEPL GAILADYRAL VEPNVTHWQH PGFFAYFAST ASGPGILGEM
LMATLVANAM LWRSSPVATE LEEVTVGWLR DGLGLPPAFD GLFTDTASTS SLIALAAARQ
AAAGDASATG LADARPLRVY ASAEAHSSIE KACMTLGIGR AGLHRVPVDA DYRMDVAALE
TAIAGDRAAG WRPCAIVATL GTTGSTSVDP VGAIADVAER EGMWLHVDAA YAGVVALIRE
RRAPFAGWER ADSIVVNPHK WLFTPLDCSL LLSRRMDVLR AAFSLVPEYL RTLDQERPVH
DYNEYQPQLG RRFRALKIWF IVRYFGLEGL RRRIEAHIEM AERLATWVDD EPDAELLAPV
PFSTVCFRWR PRRFRGREGE MEVEAALDAL NAQLLERLNA TGEVFLSHTR LGGRFTIRLA
LGNLRTEPRH VERAWALVRE IGAELDRTMV SESSDRKEAG HGGDQDRGGD LGG
//
