ID   ARCA2_ECOL6             Reviewed;         407 AA.
AC   Q8FAD9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=c5350;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
CC   -!- CAUTION: There are two genes termed arcA in strain O6 of E.coli, one
CC       refers to an arginine deiminase and the other to a two-component
CC       regulator. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83772.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FAD9; -.
DR   SMR; Q8FAD9; -.
DR   STRING; 199310.c5350; -.
DR   EnsemblBacteria; AAN83772; AAN83772; c5350.
DR   KEGG; ecc:c5350; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; ERATMHL; -.
DR   BioCyc; ECOL199310:C5350-MON; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001410; 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..407
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182210"
FT   ACT_SITE        397
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  45902 MW;  CB7FDF5E38C38F52 CRC64;
     MMEKHYVGSE IGQLRSVMLH RPNLSLKRLT PSNCQELLFD DVLSVERAGE EHDIFANTLR
     QQGIEVLLLT DLLTQTLDIP EAKSWLLETQ ISDYRLGPTF ATDVRTWLAE MSHRDLARHL
     SGGLTYSEIP ASIKNMVVDT HDINDFIMKP LPNHLFTRDT SCWIYNGVSI NPMAKPARQR
     ETNNLRAIYR WHPQFAGGEF IKYFGDENIN YDHATLEGGD VLVIGRGAVL IGMSERTTPQ
     GIEFLAQALF KHRQAERVIA VELPKHRSCM HLDTVMTHID IDTFSVYPEV VRPDVNCWTL
     TPDGHGGLKR TQESTLLHAI EKALGIDQVR LITTGGDAFE AEREQWNDAN NVLTLRPGVV
     VGYERNIWTN EKYDKAGITV LPIPGDELGR GRGGARCMSC PLHRDGI