ID   ARCA_STRSV              Reviewed;         409 AA.
AC   A3CLW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=SSA_0737;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44171.1; -; Genomic_DNA.
DR   RefSeq; WP_011836692.1; NC_009009.1.
DR   RefSeq; YP_001034721.1; NC_009009.1.
DR   AlphaFoldDB; A3CLW6; -.
DR   SMR; A3CLW6; -.
DR   STRING; 388919.SSA_0737; -.
DR   PRIDE; A3CLW6; -.
DR   EnsemblBacteria; ABN44171; ABN44171; SSA_0737.
DR   KEGG; ssa:SSA_0737; -.
DR   PATRIC; fig|388919.9.peg.707; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002148; 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..409
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000005730"
FT   ACT_SITE        399
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   409 AA;  46694 MW;  B13F672A6E45E58A CRC64;
     MSTHPIRVFS EIGKLKKVML HRPGKELENL QPDYLERLLF DDIPFLEDAQ KEHDNFAQAL
     RNEGVEVLYL EQLAAESLTS PEIREQFIEE YLEEANIRGR ETKKAIRELL RGIKDNRELV
     EKTMAGVQKV ELPEIPEEAK GLTDLVESDY PFAIDPMPNL YFTRDPFATI GNAVSLNHMY
     ADTRNRETLY GKYIFKHHPV YGGKVDLVYN REEDTRIEGG DELVLSKDVL AVGISQRTDA
     ASIEKLLVNI FKKNVGFKKV LAFEFANNRK FMHLDTVFTM VDYDKFTIHP EIEGDLRVYS
     VTYVDDKLKI VEEKGDLAEI LAENLGVEKV HLIRCGGGNI VAAAREQWND GSNTLTIAPG
     VVVVYDRNTV TNKILEEYGL RLIKIRGSEL VRGRGGPRCM SMPFEREEI