ID   ARCA_CLOP1              Reviewed;         413 AA.
AC   Q0TUR5; Q46168; Q46254;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Arginine deiminase;
DE            Short=ADI;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase;
DE            Short=AD;
GN   Name=arcA; OrderedLocusNames=CPF_0161;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9053381; DOI=10.1111/j.1574-6968.1997.tb10186.x;
RA   Ohtani K., Bando M., Swe T., Banu S., Oe M., Hayashi H., Shimizu T.;
RT   "Collagenase gene (colA) is located in the 3'-flanking region of the
RT   perfringolysin O (pfoA) locus in Clostridium perfringens.";
RL   FEMS Microbiol. Lett. 146:155-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; X97684; CAA66275.1; -; Genomic_DNA.
DR   EMBL; CP000246; ABG84531.1; -; Genomic_DNA.
DR   RefSeq; WP_003462829.1; NC_008261.1.
DR   AlphaFoldDB; Q0TUR5; -.
DR   SMR; Q0TUR5; -.
DR   STRING; 195103.CPF_0161; -.
DR   PRIDE; Q0TUR5; -.
DR   EnsemblBacteria; ABG84531; ABG84531; CPF_0161.
DR   GeneID; 29572717; -.
DR   KEGG; cpf:CPF_0161; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; SAWIYDG; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001823; 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..413
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000273582"
FT   ACT_SITE        403
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        165
FT                   /note="D -> E (in Ref. 1; CAA66275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  47203 MW;  35754EDCAFE95064 CRC64;
     MRDDRALNVT SEIGRLKTVL LHRPGEEIEN LTPDLLDRLL FDDIPYLKVA REEHDAFAQT
     LREAGVEVLY LEVLAAEAIE TSDEVKQQFI SEFIDEAGVE SERLKEALIE YFNSFSDNKA
     MVDKMMAGVR KEELKDYHRE SLYDQVNNVY PFVCDPMPNL YFTRDPFATI GHGITLNHMR
     TDTRNRETIF AKYIFRHHPR FEGKDIPFWF NRNDKTSLEG GDELILSKEI LAVGISQRTD
     SASVEKLAKK LLYYPDTSFK TVLAFKIPVS RAFMHLDTVF TQVDYDKFTV HPGIVGPLEV
     YALTKDPEND GQLLVTEEVD TLENILKKYL DRDIKLIKCG GGDEIIAARE QWNDGSNTLA
     IAPGEVVVYS RNYVTNEILE KEGIKLHVIP SSELSRGRGG PRCMSMPLIR EDL