ID Q81JB6_BACCR Unreviewed; 473 AA.
AC Q81JB6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:AAP07133.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:AAP07133.1};
GN OrderedLocusNames=BC_0035 {ECO:0000313|EMBL:AAP07133.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP07133.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP07133.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP07133.1; -; Genomic_DNA.
DR RefSeq; NP_829932.1; NC_004722.1.
DR RefSeq; WP_001075300.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81JB6; -.
DR KEGG; bce:BC0035; -.
DR PATRIC; fig|226900.8.peg.51; -.
DR HOGENOM; CLU_025925_2_0_9; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd00615; Orn_deC_like; 1.
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:AAP07133.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT DOMAIN 7..306
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 397..453
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 473 AA; 53611 MW; 4830F7D21D771906 CRC64;
MNQNRMPLYE ALIEFKERGP LSFHVPGHKN GLNFPQEAIR EFKGILSIDV TELAGLDDLH
SPFECIDEAQ QLLAEVYNTK RSYFLINGST VGNLAMILSC CGEHDIVLVQ RNCHKSIING
LKLAGANPIF LDPWIDEAYN VPVGVRNEII KNAIGKYPNA KALILTHPNY YGMGMDLEAS
IAFAHAHKIP VLVDEAHGAH LCLGEPFPKS ALTYGADIVV HSAHKTLPAM TMGSYLHINS
HLVDEDKVTT YLSMLQSSSP SYPIMASLDI ARFTMARIKE EGHSEIVEFL RRFKEQLRSI
PQIAILEYPL QDELKVTVQT RCQLSGYELQ SVFEKVGIYT EMADPYNVLF ILPLQVNEGY
MKVIEMIRVA LQHYEVKDKR ESIRYTYNGE FSLLPYTYKQ LDGYETKIVS IEEAVGMIAA
EMVIPYPPGI PLIMYGERIT SEHKEQIMYL ERAGARFQGN TKYMKVYDIE SRF
//
