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Database: UniProt
Entry: A0A1R0TWA3_9MYCO
LinkDB: A0A1R0TWA3_9MYCO
Original site: A0A1R0TWA3_9MYCO 
ID   A0A1R0TWA3_9MYCO        Unreviewed;       960 AA.
AC   A0A1R0TWA3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:OMC07140.1};
GN   ORFNames=A5736_08680 {ECO:0000313|EMBL:OMC07140.1};
OS   Mycobacterium sp. SP-6446.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834162 {ECO:0000313|EMBL:OMC07140.1, ECO:0000313|Proteomes:UP000187139};
RN   [1] {ECO:0000313|Proteomes:UP000187139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP-6446 {ECO:0000313|Proteomes:UP000187139};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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   -!- 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:OMC07140.1}.
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DR   EMBL; MBEM01000269; OMC07140.1; -; Genomic_DNA.
DR   RefSeq; WP_076125090.1; NZ_MBEM01000269.1.
DR   AlphaFoldDB; A0A1R0TWA3; -.
DR   Proteomes; UP000187139; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF4; BLR3474 PROTEIN; 1.
DR   Pfam; PF01276; OKR_DC_1; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
FT   DOMAIN          293..516
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          564..750
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   REGION          933..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  107049 MW;  B952E1F96139B12E CRC64;
     MTRDSAHPRR LRVSALAAVA NPSYTRVDTW NLLDDACRHL AEVDLAGLDI AHDMARVKRL
     MDRIGAYERY WLYPGAENLA TFRAHLESKS TVRLSEEVSL AARLLCEYGD RAGLFDTSAP
     LADQELVARA KQQQFYTVLL ADDAPMTAPD SLAECLRALR SASDDVQFEL LVVPSVEDAI
     TAVALNGEIQ AAIIRHDLPL RSRDRVPLMN TLLGPNDSAA GGVVPDCPDD WVECGEWIRE
     LRPHIDLYLL TDESIAAGNI DEPDVYDRTF YRLNDVTDLH STVLAGLRNR FATPFFDALR
     AYAAAPVGQF HALPVARGAS IFNSKSLQDM GEFYGRNIFM AETSTTSGGL DSLLDPHGNI
     KKAMDKAAKT WNADHTYFVT NGTSTANKIV VQSLTRPGDI VLIDRNCHKS HHYGLVLAGA
     YPLYLDAYPL PQFAIYGAVS LETIKKTLLD LEAAGQLHRV RMLLLTNCTF DGVVYNPRRV
     MEEVLAIKPD ICFLWDEAWY AFATAVPWAR QRTAMVSADR LYQMLSSPEY AEEYRNWAAS
     MQGVDRSEWL HRRLLPDPAA ARVRVYATHS THKSLSALRQ ASMIHVRDQD FNARARDAFG
     EAFLTHTSTS PNQQLLASLD LARRQVDIEG FQLVRLVYNM ALTFRGRVRK DRLISKWFRI
     LDESDLVPDE FRASHVSSFR QVVQGAQAEW NEAWRSDEFV LDPTRVTLFV GKTGMNGYDF
     REKILMERFG IQINKTSINS VLLIFTIGVT WSSVHYLLDV LRRIATDFDH IQNAASAADW
     SLHDRHVEEI TQDLPHLPDF SEFDIAFRPV DACAFGDTRS AFYAGYEESD REYVLIGTAG
     RRLAEGKTLV STTFVVPYPP GFPVLVPGQV VSKEIVYFLA QLDVKEIHGY NPELGLSVFT
     PEALARMEAQ RNAAMAAVGS AFPVFELPSD AKAINGATTS PNGGSTHGDR KGGVSSEVAQ
//
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