ID   ARCA_CUTAK              Reviewed;         414 AA.
AC   Q6AA78;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PPA0583;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT82338.1; -; Genomic_DNA.
DR   RefSeq; WP_002515158.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6AA78; -.
DR   SMR; Q6AA78; -.
DR   STRING; 267747.PPA0583; -.
DR   EnsemblBacteria; AAT82338; AAT82338; PPA0583.
DR   KEGG; pac:PPA0583; -.
DR   PATRIC; fig|267747.3.peg.611; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_11; -.
DR   OMA; WPARHDE; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000603; 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.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; Hydrolase.
FT   CHAIN           1..414
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182224"
FT   ACT_SITE        402
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   414 AA;  45754 MW;  2C409A69D71E612D CRC64;
     MTTPIGAWSE VGKLREVMVC EPRLAHRRLT PSNCRELLFD DVLWVEKAQE DHRDFVAKMR
     ERGIVVHEMH QLLSEVLDIS EGRSWVLDRK LSPNAVGLGV DEDVRDWLND MPSDTLAEYL
     IGGVAYGEVP ADRRKHVLGA LIKAHSENEF LIPPLPNTQF TRDTTAWIFG GVTFNPMRWP
     ARQQETVLAS AIYTHHPIFA ERDFKIWYGC AEADHGMSTL EGGDIMPVGN GTVLIGMGER
     SSWQAITQVA RSLFAQNAAR RMVVAAMAPD RASMHLDTVF SFCDVDLVTL YKPVVDTITP
     LVLEPSSEAA GFSVRVDDRH FTDVVASSLG LDGLRTVETG GDCWEAQREQ WDDGNNVVAL
     EPGVVVGYDR NTATNALLAK AGVEVVEIKA AELGRGRGGG HCMTCPITRD PVDY