ID   ARCA_DICNV              Reviewed;         415 AA.
AC   A5EXR1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=DNO_1075;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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}.
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DR   EMBL; CP000513; ABQ13883.1; -; Genomic_DNA.
DR   RefSeq; WP_012031382.1; NC_009446.1.
DR   AlphaFoldDB; A5EXR1; -.
DR   SMR; A5EXR1; -.
DR   STRING; 246195.DNO_1075; -.
DR   PRIDE; A5EXR1; -.
DR   EnsemblBacteria; ABQ13883; ABQ13883; DNO_1075.
DR   KEGG; dno:DNO_1075; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; SAWIYDG; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000248; 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; Reference proteome.
FT   CHAIN           1..415
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000336662"
FT   ACT_SITE        404
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   415 AA;  46407 MW;  877C17391AEA2361 CRC64;
     MSQYPLGVNS EVGKLRTVMV CQPGLAHERL TPDNCDELLF DDVLWVEQAQ RDHQDFVEKM
     RARDIEVLEM HESLAETVKN PEALKWILDR KITPNLVGLP IMNELRSWFE GLDARQQADF
     LIGGVSVLDI TPDKFSADVI SLVRATQGDL GFVFPPLPNT QFTRDTTNWI YGGVTLNPMY
     WPARQQETLL AAAIYKFHPR FAGKVKVWWG DPDKDYGNAT LEGGDVFPVG KGLVLVGMGE
     RSSIQAITQL AQVLFAEKAA ERIIVAAMPK TRSAMHLDTI FTFCDRDLIN YFPKMVDQIK
     PYSIRPDESK PNGLDIREER KSFVDVVQEA LGLKELRKVA TGGNSYAADR EQWDDANNVF
     ALEPGVVVSY DRNLLTNKLL KAAGVEIVSI RSSELGRGRG GGRCMTCPIA RDAAY