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Database: UniProt
Entry: D4N1L7_ANAHA
LinkDB: D4N1L7_ANAHA
Original site: D4N1L7_ANAHA 
ID   D4N1L7_ANAHA            Unreviewed;       440 AA.
AC   D4N1L7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Arginine/lysine/ornithine decarboxylases {ECO:0000313|EMBL:CBL38762.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:CBL38762.1};
GN   ORFNames=CL2_18600 {ECO:0000313|EMBL:CBL38762.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38762.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL38762.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38762.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL38762.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38762.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929061; CBL38762.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4N1L7; -.
DR   STRING; 649756.ERS852387_01839; -.
DR   KEGG; bprl:CL2_18600; -.
DR   PATRIC; fig|245018.3.peg.2144; -.
DR   Proteomes; UP000008960; Chromosome.
DR   GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
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:CBL38762.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          15..274
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          361..429
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   440 AA;  50451 MW;  34D23926191E3682 CRC64;
     MPGHKRNLKI DSLLDAISKI DITEITGFDD LHHPEEMIRE LMDDLKQIYG TKESYLLVNS
     STAGNLAAIA ALCNIGDKIL VARNCHKSVY HAIELLGLDP IYIYPEIDEY GICKGITKEQ
     IENIITKETS IKAMVLVSPT YEGRVSDIEG ISDVLHRNNI PLIVDEAHGA HFIYHEAFPE
     SAANSGADIV IQSLHKTLPA FTQTGLLHLC TDCVTREMMQ KKLSIFQSSS PSYVLIASIE
     QCIHICNENR GYFQQYYEKL WILREKLEEL KYIKLVPTDD IGKLVFSVKD TTISGEELFE
     ILRDNYHLEM EMSELYYVIA MTSVCDTQEG YDRLYQALKE IDSEITKKNT EYLFLENDFH
     QNKKMLKPEE AATKDRIQID YDDAKDEIAA EFIFLYPPGI PLVVPGEVID KYVIDKIRQY
     EQYNMKVIGL NDHKIYIINR
//
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