ID A0A174J1U1_9CLOT Unreviewed; 508 AA.
AC A0A174J1U1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Orn/Lys/Arg decarboxylase major region {ECO:0000313|EMBL:CUO91070.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:CUO91070.1};
GN Name=speA {ECO:0000313|EMBL:CUO91070.1};
GN ORFNames=ERS852407_04360 {ECO:0000313|EMBL:CUO91070.1};
OS Hungatella hathewayi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=154046 {ECO:0000313|EMBL:CUO91070.1, ECO:0000313|Proteomes:UP000095651};
RN [1] {ECO:0000313|EMBL:CUO91070.1, ECO:0000313|Proteomes:UP000095651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608850 {ECO:0000313|EMBL:CUO91070.1,
RC ECO:0000313|Proteomes:UP000095651};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYZE01000014; CUO91070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A174J1U1; -.
DR Proteomes; UP000095651; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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: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:CUO91070.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000095651}.
FT DOMAIN 6..296
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 428..477
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 508 AA; 55438 MW; 5E29D6E75B918EB3 CRC64;
MEKYLLDRLM EYGESDAYPF HMPGHKRQAG AGFAGDFPNP FSVDITEIGG FDNLHHPEGI
LKESMEWAGN VYGADQTYYL VNGSSCGILS AVCGSVSHGG TILMSRNCHK SAYHGVYLGH
LRAEYIYPQT IPEFGIQGGL SPEDVRRLLI THPETEAVLV VSPTYDGIVS DIGAIAKIVH
EWGIPLIVDE AHGAHFPFGG EARFPVSALE LGADVVIQSL HKTLPSLTQT AVMHVNAGFA
DISRIDRYVH MFQSSSPSYV LMAAIENCIR WMDEAGRDEM KAFSGRLDRI RRRMGEMECL
ALLGGVKGRC QVFDVDKSKI VVSVGSSSLT GPELTELLRN RYHLEMEMCG PDYVTAITTV
ADTDEGLDRL CRAFLEIDHE RRRDTGDCGT AASGFTGING DNTGERDCGI VDNRMEKERG
CGWPEIAMTI AQAMDSPGRS VPLDACEGMV SGEFIYIYPP GIPIVAPGEV LKPELVEMIR
QYKRKGLPVQ GTADPEVEAV LTAAGAEN
//