ID   ARCA_STRP3              Reviewed;         411 AA.
AC   P0CZ64; Q8K5F0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
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};
DE   AltName: Full=Streptococcal acid glycoprotein;
GN   Name=arcA {ECO:0000255|HAMAP-Rule:MF_00242}; Synonyms=sagP;
GN   OrderedLocusNames=SpyM3_1196;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP 268 / Serotype M3;
RX   PubMed=12901845; DOI=10.1016/s0882-4010(03)00094-9;
RA   Marouni M.J., Ziomek E., Sela S.;
RT   "Influence of group A streptococcal acid glycoprotein on expression of
RT   major virulence factors and internalization by epithelial cells.";
RL   Microb. Pathog. 35:63-72(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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         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   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00242}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF468045; AAM22954.1; -; Genomic_DNA.
DR   EMBL; AE014074; AAM79803.1; -; Genomic_DNA.
DR   RefSeq; WP_011054721.1; NC_004070.1.
DR   AlphaFoldDB; P0CZ64; -.
DR   SMR; P0CZ64; -.
DR   EnsemblBacteria; AAM79803; AAM79803; SpyM3_1196.
DR   KEGG; spg:SpyM3_1196; -.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000564; 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; Glycoprotein; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..411
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182249"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   411 AA;  46256 MW;  8B3D026B229A4972 CRC64;
     MTAQTPIHVY SEIGKLKKVL LHRPGKEIEN LMPDYLERLL FDDIPFLEDA QKEHDAFAQA
     LRDEGIEVLY LETLAAESLV TPEIREAFID EYLSEANIRG RATKKAIREL LMAIEDNQEL
     IEKTMAGVQK SELPEIPASE KGLTDLVESS YPFAIDPMPN LYFTRDPFAT IGTGVSLNHM
     FSETRNRETL YGKYIFTHHP IYGGGKVPMV YDRNETTRIE GGDELVLSKD VLAVGISQRT
     DAASIEKLLV NIFKQNLGFK KVLAFEFANN RKFMHLDTVF TMVDYDKFTI HPEIEGDLRV
     YSVTYDNEEL HIVEEKGDLA DLLAANLGVE KVDLIRCGGD NLVAAGREQW NDGSNTLTIA
     PGVVVVYNRN TITNAILESK GLKLIKIHGS ELVRGRGGPR CMSMPFERED I