ID A0A1I7ADS6_9ACTN Unreviewed; 550 AA.
AC A0A1I7ADS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:SFT73038.1};
GN ORFNames=SAMN05660657_02711 {ECO:0000313|EMBL:SFT73038.1};
OS Geodermatophilus amargosae.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1296565 {ECO:0000313|EMBL:SFT73038.1, ECO:0000313|Proteomes:UP000199546};
RN [1] {ECO:0000313|Proteomes:UP000199546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46136 {ECO:0000313|Proteomes:UP000199546};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FPBA01000008; SFT73038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7ADS6; -.
DR STRING; 1296565.SAMN05660657_02711; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000199546; 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 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 488..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 550 AA; 58955 MW; CF1E0AAA5712FB8C CRC64;
MTPEQFRQHG HEVVDWIADY WSRIESFPVR SRVSPGDVRA ALPPSAPEQG EPFSAVLADL
DRVVLPGVTH WQHPGFLAYF PANTSGPSVL GDLLSAGLGV QGMSWVTSPA ATELEQHVMD
WLAELLGLPA SFRSTGTGGG VVQDSSSGAN LVALLAALHR ASGGATVRHG VLPDEYTVYV
SSETHSSMEK AVRIAGLGTD AVRIVEVDGD LAMRPAALAA RLERDTARGY RPVLVCATVG
TTSTTAIDPL AEIGAICRRY GAWLHVDAAY AGVSAVAPEL RALQAGVEEA DSYTTDAHKW
LLTGFDATLF WVADRAALTG ALAILPEYLR NAATDAGTVV DYRDWQVELG RRFRALKLWA
VVRWYGAEGL RAHARSGVAL AQELAGWADA DDRFDVATPH PLSLVCLRPR WPADVDADVA
TMTLLERLND GGEVYLTHTA VRGSVVLRVA IGAPTTTRAH VERAWALLCE GHDWLAADFA
EQAAERARAE AERKEAERRA AEEEAARRRA EERAAEQAAE QAAAQQVAEE APEEAPADDE
PVAATPPVTG
//