ID   ARCA_ECO81              Reviewed;         407 AA.
AC   B7MSY5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=ECED1_5105;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR11060.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7MSY5; -.
DR   SMR; B7MSY5; -.
DR   EnsemblBacteria; CAR11060; CAR11060; ECED1_5105.
DR   KEGG; ecq:ECED1_5105; -.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000748; 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_1000119037"
FT   ACT_SITE        397
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   407 AA;  45888 MW;  310D4C47106B8CD8 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
     GVEFLAQALF KHRQAERVIA VELPKHRSCM HLDTVMTHID IDTFSVYPEV VRPDVNCWTL
     TPDGHGGLKR TQESTLLHAI EKALGIDQVR LITTGGDAFE AEREQWNDAN NVLTLRPGVV
     VGYERNIWTN EKYDKAGITV LPIPGDELGR GRGGARCMSC PLHRDGI