ARCA_BACCN
ID ARCA_BACCN Reviewed; 410 AA.
AC A7GKP8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Arginine deiminase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000255|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000255|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000255|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000255|HAMAP-Rule:MF_00242}; OrderedLocusNames=Bcer98_0348;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-citrulline + NH4(+);
CC Xref=Rhea:RHEA:19597, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:57743; EC=3.5.3.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00242};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000764; ABS20706.1; -; Genomic_DNA.
DR RefSeq; WP_011983464.1; NC_009674.1.
DR AlphaFoldDB; A7GKP8; -.
DR SMR; A7GKP8; -.
DR STRING; 315749.Bcer98_0348; -.
DR EnsemblBacteria; ABS20706; ABS20706; Bcer98_0348.
DR GeneID; 56415904; -.
DR KEGG; bcy:Bcer98_0348; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0018101; P:protein citrullination; IEA:GOC.
DR HAMAP; MF_00242; Arg_deiminase; 1.
DR InterPro; IPR003876; Arg_deiminase.
DR PIRSF; PIRSF006356; Arg_deiminase; 1.
DR PRINTS; PR01466; ARGDEIMINASE.
DR TIGRFAMs; TIGR01078; arcA; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase.
FT CHAIN 1..410
FT /note="Arginine deiminase"
FT /id="PRO_1000078363"
FT ACT_SITE 400
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 410 AA; 46862 MW; 0B250363EC8AE0B0 CRC64;
MKHPIHVTSE IGELQTVLLK RPGKELENLT PDYLQQLLFD DIPYLPIVQK EHDYFAQTLR
NRGVEVLYLE TLAAEALTDK KLREEFVNRI LKEGQADANV AHQTLKEYLL SFSNEELIQK
IMGGVRKNEI DTSQKTHLYE LMEDHYPFYL DPMPNLYFTR DPAATIGEGV TINKMREPAR
RRESLFIEYI MKYHPRFANH NVPVWLNRDY KFPIEGGDEL ILNEETVAIG VSARTSAKAI
ERLAKNLFSR QNKIKKVLAI EIPKCRAFMH LDTVFTMVDY DKFTIHPAIQ GPKGNMNIYI
LEKGLDEETL KITHRTSLME VLKEVLGLQE LVLIPCGGGD VIASAREQWN DGSNTLAIAP
GVVVTYDRNY VSNALLREHG IEVIEVLSSE LSRGRGGPRC MSMPIVRKDI