ID   ARCA_STRP6              Reviewed;         411 AA.
AC   Q5XAY2; P16962;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Arginine deiminase;
DE            Short=ADI;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase;
DE            Short=AD;
DE   AltName: Full=Streptococcal acid glycoprotein;
GN   Name=arcA; OrderedLocusNames=M6_Spy1296;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=JRS4 / Serotype M6;
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; CP000003; AAT87431.1; -; Genomic_DNA.
DR   RefSeq; WP_002983803.1; NC_006086.1.
DR   AlphaFoldDB; Q5XAY2; -.
DR   SMR; Q5XAY2; -.
DR   EnsemblBacteria; AAT87431; AAT87431; M6_Spy1296.
DR   GeneID; 57852966; -.
DR   GeneID; 66901284; -.
DR   KEGG; spa:M6_Spy1296; -.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001167; 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   1: Evidence at protein level;
KW   Arginine metabolism; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..411
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182251"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46297 MW;  9182F04A238E7243 CRC64;
     MTAQTPIHVY SEIGKLKKVL LHRPGKEIEN LMPDYLERLL FDDIPFLEDA QKEHDAFAQA
     LRDEGIEVLY LETLAAESLV TPEIREAFID EYLSEANIRG RATKKAIREL LMAIEDNQEL
     IEKTMAGVQK SELPEIPASE KGLTDLVESN YPFAIDPMPN LYFTRDPFAT IGTGVSLNHM
     FSETRNRETL YGKYIFTHHP IYGGGKVPMV YDRNETTRIE GGDELVLSKD VLAVGISQRT
     DAASIEKLLV NIFKQNLGFK KVLAFEFANN RKFMHLDTVF TMVDYDKFTI HPEIEGDLRV
     YSVTYDNEEL HIVEEKGDLA ELLAANLGVE KVDLIRCGGD NLVAAGREQW NDGSNTLTIA
     PGVVVVYNRN TITNAILESK GLKLIKIHGS ELVRGRGGPR CMSMPFERED I