ID   ARCA_CLOPE              Reviewed;         413 AA.
AC   P0C2E1; Q46168; Q46254;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=CPE0168;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-413.
RC   STRAIN=13 / Type A;
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).
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; BA000016; BAB79874.1; -; Genomic_DNA.
DR   EMBL; X97768; CAA66364.1; -; Genomic_DNA.
DR   RefSeq; WP_003474161.1; NC_003366.1.
DR   AlphaFoldDB; P0C2E1; -.
DR   SMR; P0C2E1; -.
DR   STRING; 195102.gene:10489412; -.
DR   PRIDE; P0C2E1; -.
DR   EnsemblBacteria; BAB79874; BAB79874; BAB79874.
DR   KEGG; cpe:CPE0168; -.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; SAWIYDG; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000818; 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..413
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182209"
FT   ACT_SITE        403
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  47217 MW;  D8D49EDCAFE9494C 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
     IAPGEVIVYS RNYVTNEILE KEGIKLHVIP SSELSRGRGG PRCMSMPLIR EDL