ID   ARCA_STRCO              Reviewed;         420 AA.
AC   Q9RJN1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SCO0613; ORFNames=SCF55.37;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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:0000305}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; AL939106; CAB61307.1; -; Genomic_DNA.
DR   RefSeq; NP_624925.1; NC_003888.3.
DR   RefSeq; WP_011027247.1; NZ_VNID01000004.1.
DR   AlphaFoldDB; Q9RJN1; -.
DR   SMR; Q9RJN1; -.
DR   STRING; 100226.SCO0613; -.
DR   PRIDE; Q9RJN1; -.
DR   GeneID; 1096036; -.
DR   KEGG; sco:SCO0613; -.
DR   PATRIC; fig|100226.15.peg.594; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_11; -.
DR   InParanoid; Q9RJN1; -.
DR   OMA; WPARHDE; -.
DR   PhylomeDB; Q9RJN1; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016990; F:arginine deiminase activity; IBA:GO_Central.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019546; P:arginine deiminase pathway; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182245"
FT   ACT_SITE        408
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  46169 MW;  8B86B941129CB5B4 CRC64;
     MTSNESAVSQ ALGVHSEVGR LRKVLVCSPG LAHRRLTPTN SDELLFDDVM WVENAQRDHA
     AFVGELRRRG VEVVELHDLL AQIMALPEAR AWLLDRKITA NQVGIGLIDA ARAYLETLSP
     RELAEYLVGG LATSDLPEDF RSPHLALARE STGAREYLMP PLPNTLYTRD TTCWLYGGLT
     LNPLYWSARH DETLLMKAIY TFHPDFKGSK VWWGDPERDW GQATFEGGDI MPVGNGVVLM
     GMSERTSRQA ITQVAAALFR SGAAEHVVVA GMPKLRSAMH LDTVFTFADR DVVTLYPRIM
     DAVHTFSLRP GDRAPGFDVV DEGSTPFVDV VAKALGLPKL RVVETGGDAY ASERQQWDSG
     NNAVAVEPGV VFTYDRNTLT NALLREARVE VVTIVGAELG RGRGGGHCMT CPLVREPVDF