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Database: UniProt
Entry: A0A1I2WH19_9FIRM
LinkDB: A0A1I2WH19_9FIRM
Original site: A0A1I2WH19_9FIRM 
ID   A0A1I2WH19_9FIRM        Unreviewed;       486 AA.
AC   A0A1I2WH19;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SFG98871.1};
GN   ORFNames=SAMN05660649_03415 {ECO:0000313|EMBL:SFG98871.1};
OS   Desulfotruncus arcticus DSM 17038.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfotruncus.
OX   NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFG98871.1, ECO:0000313|Proteomes:UP000199337};
RN   [1] {ECO:0000313|Proteomes:UP000199337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
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   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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DR   EMBL; FOOX01000013; SFG98871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2WH19; -.
DR   STRING; 341036.SAMN05660649_03415; -.
DR   Proteomes; UP000199337; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 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; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199337}.
FT   DOMAIN          221..235
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   486 AA;  51435 MW;  BFC81DD23A48F093 CRC64;
     MSGDHTEMPI VAALDNFSQK KPLRFHVPGH GGGQALHPAM RKANLPSWDV TELDGLDDLH
     NPSGVIELAQ KKAAGLYGAR HTFFLINGTT VGIQALIAAA CCEPDSAIAL PRNVHRSVLG
     GLVFSGARPV FIEPQLVPGF DFAAGFTGAA LKQVLQAVPE IAAVLAVHPC YYGVVGNLAE
     AAEICHRYNI PLLADEAHGT HLRFSPHLPP DALEQGADAT VQSVHKTGGA LTQASWLHLA
     EGGRVDRKKV AGVLRLLQSS SPSYLLMASL DAARQQLALC GRASLDAALD TALEAARAIK
     AIPGLTVLGP EHLARPGAVD YDPTRLVVSF RELGLSGYEA SRLLAEEYNI YVEMADIYNI
     VAVLPIGVNR EEVGALVHAL AGISGQVRGA ALKGDSPPLT MPQLPPQIMT PRLAWLARKR
     QVRLETSAGL VSAEAVAVQP PGIAVIYPGE EITPAIIEYL MVARDHGLQL HGAADPRLGT
     IEVVDC
//
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