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Database: UniProt
Entry: A0A161X781_9CLOT
LinkDB: A0A161X781_9CLOT
Original site: A0A161X781_9CLOT 
ID   A0A161X781_9CLOT        Unreviewed;       505 AA.
AC   A0A161X781;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:KZL89966.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:KZL89966.1};
GN   Name=speA_2 {ECO:0000313|EMBL:KZL89966.1};
GN   ORFNames=CLMAG_44500 {ECO:0000313|EMBL:KZL89966.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL89966.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL89966.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL89966.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-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}.
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:KZL89966.1}.
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DR   EMBL; LWAE01000006; KZL89966.1; -; Genomic_DNA.
DR   RefSeq; WP_066627154.1; NZ_LWAE01000006.1.
DR   AlphaFoldDB; A0A161X781; -.
DR   STRING; 1121326.CLMAG_44500; -.
DR   PATRIC; fig|1121326.3.peg.4513; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000076603; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd00615; Orn_deC_like; 1.
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; 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:SF3; LYSINE 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KZL89966.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076603}.
FT   DOMAIN          5..383
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          390..466
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   505 AA;  57254 MW;  C792966108417592 CRC64;
     MSELPILEGI LKYVKEENIS FCMPGHKGGR GFANTPIGKE FIESFLKCDV TEVDGLDNLH
     NSEGIIKEAQ QLLSDFYGSK KSYFLVNGST SGNLAMIFSC FNEGDKIIVE RNCHRSIFNA
     IIMRKLRPVY VKNIIIERLN APLSMDLEHF SQVLDNNRDA KGIVVTYPNY YGICGNLKYI
     IEQGNKHGIR VLVDSAHGSH FGIHENLPES AVRLGADMIV TSTHKTLPSL TQTSYLHINN
     GQDIKKTDFY VSALLSTSPS YLFLCAMDYA RFYLNKYGKE QYGRILDICS YYRNKINEIE
     GIYILGKEDI NSFNQYINKT RQINDYTYGI DTILDIDTTR YVINLRSGYS GHLLLKYLKK
     HGIQGEMSDN SNVVLIFSPF NDETEFKKLY TVLKKCNLDE LKDKDVSIVN FDIPKIELLP
     YEVMEKEKEY ETLQESLGRI SGSNIVPYPP GVPILVMGEV IDKNCLDAIF YCKNNGLDIL
     GIKNDKIEVM KCKLESDGVS NSPDS
//
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