ID   ARCA_ENTFA              Reviewed;         408 AA.
AC   Q93K67; Q7C3W8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=EF_0104;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29212 / DSM 2570;
RX   PubMed=12399499; DOI=10.1128/jb.184.22.6289-6300.2002;
RA   Barcelona-Andres B., Marina A., Rubio V.;
RT   "Gene structure, organization, expression, and potential regulatory
RT   mechanisms of arginine catabolism in Enterococcus faecalis.";
RL   J. Bacteriol. 184:6289-6300(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AJ312276; CAC41341.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO79979.1; -; Genomic_DNA.
DR   RefSeq; NP_813907.1; NC_004668.1.
DR   RefSeq; WP_002356129.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q93K67; -.
DR   SMR; Q93K67; -.
DR   STRING; 226185.EF_0104; -.
DR   EnsemblBacteria; AAO79979; AAO79979; EF_0104.
DR   GeneID; 60892653; -.
DR   KEGG; efa:EF0104; -.
DR   PATRIC; fig|226185.45.peg.156; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001415; 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..408
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182211"
FT   ACT_SITE        398
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   408 AA;  46735 MW;  42382220D96AD735 CRC64;
     MSHPINVFSE IGKLKTVMLH RPGKELENLM PDYLERLLFD DIPFLEKAQA EHDAFAELLR
     SKDIEVVYLE DLAAEALINE EVRRQFIDQF LEEANIRSES AKEKVRELML EIDDNEELIQ
     KAIAGIQKQE LPKYEQEFLT DMVEADYPFI IDPMPNLYFT RDNFATMGHG ISLNHMYSVT
     RQRETIFGQY IFDYHPRFAG KEVPRVYDRS ESTRIEGGDE LILSKEVVAI GISQRTDAAS
     IEKIARNIFE QKLGFKNILA FDIGEHRKFM HLDTVFTMID YDKFTIHPEI EGGLVVYSIT
     EKADGDIQIT KEKDTLDNIL CKYLHLDNVQ LIRCGAGNLT AAAREQWNDG SNTLAIAPGE
     VVVYDRNTIT NKALEEAGVK LNYIPGSELV RGRGGPRCMS MPLYREDL