ID J8I059_BACCE Unreviewed; 490 AA.
AC J8I059;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:EJR38677.1};
GN ORFNames=IIG_00910 {ECO:0000313|EMBL:EJR38677.1};
OS Bacillus cereus VD048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053226 {ECO:0000313|EMBL:EJR38677.1, ECO:0000313|Proteomes:UP000006960};
RN [1] {ECO:0000313|EMBL:EJR38677.1, ECO:0000313|Proteomes:UP000006960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD048 {ECO:0000313|EMBL:EJR38677.1,
RC ECO:0000313|Proteomes:UP000006960};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD048.";
RL Submitted (APR-2012) 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:EJR38677.1}.
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DR EMBL; AHEU01000004; EJR38677.1; -; Genomic_DNA.
DR RefSeq; WP_002128878.1; NZ_JH792310.1.
DR AlphaFoldDB; J8I059; -.
DR GeneID; 66266472; -.
DR PATRIC; fig|1053226.3.peg.920; -.
DR HOGENOM; CLU_025925_2_1_9; -.
DR Proteomes; UP000006960; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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 InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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}.
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 490 AA; 53676 MW; 0285FD4AFDD4E0CB CRC64;
MSQYETPLFT ALVEHSKRNP VQFHIPGHKK GQGMDPTFRE FIGHNALAID LINIAPLDDL
HHPKGMIKEA QDLAAAAFGA DHTFFSIQGT SGAIMTMVMS VCGPGDKILV PRNVHKSVMS
AIIFSGAKPI FMHPEIDPKL GISHGITIQS VKKALEEHSD AKGLLVINPT YFGFAADLEQ
IVELAHSYDI PVLVDEAHGV HIHFHDELPI SAMQAGADMA ATSVHKLGGS LTQSSILNVK
EGLVNVKHVQ SIISMLTTTS TSYILLASLD VARKRLATEG TALIEQTIQL AEHVRDAINA
IEHLYCPGKE MLGTDATFNY DPTKIIVSVK DLGITGHQAE VWLREHYNIE VELSDLYNIL
CLITFGDTES ETDTLITALQ DLAATYRNRA DKGVQVQVEI PEIPVLALSP RDAFYSETEV
IPFENAAGRI IADFVMVYPP GIPIFTPGEI ITQDNLEYIL KNLEAGLPVQ GPEDMTLQTL
RVIKEYKPIS
//
