ID   ARCA_STAA8              Reviewed;         411 AA.
AC   Q2FUX7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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};
GN   OrderedLocusNames=SAOUHSC_02969;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD31958.1; -; Genomic_DNA.
DR   RefSeq; WP_000129411.1; NZ_LS483365.1.
DR   RefSeq; YP_501419.1; NC_007795.1.
DR   AlphaFoldDB; Q2FUX7; -.
DR   SMR; Q2FUX7; -.
DR   STRING; 1280.SAXN108_2906; -.
DR   EnsemblBacteria; ABD31958; ABD31958; SAOUHSC_02969.
DR   GeneID; 3921670; -.
DR   KEGG; sao:SAOUHSC_02969; -.
DR   PATRIC; fig|93061.5.peg.2678; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   PRO; PR:Q2FUX7; -.
DR   Proteomes; UP000008816; 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.
DR   TIGRFAMs; TIGR01078; arcA; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..411
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000005721"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   411 AA;  46915 MW;  1F45C9C2FB7FF1C0 CRC64;
     MTDGPIKVNS EIGALKTVLL KRPGKELENL VPDYLDGLLF DDIPYLEVAQ KEHDHFAQVL
     REEGVEVLYL EKLAAESIEN PQVRSEFIDD VLAESKKTIL GHEEEIKALF ATLSNQELVD
     KIMSGVRKEE INPKCTHLVE YMDDKYPFYL DPMPNLYFTR DPQASIGHGI TINRMFWRAR
     RRESIFIQYI VKHHPRFKDA NIPIWLDRDC PFNIEGGDEL VLSKDVLAIG VSERTSAQAI
     EKLARRIFEN PQATFKKVVA IEIPTSRTFM HLDTVFTMID YDKFTMHSAI LKAEGNMNIF
     IIEYDDVNKD IAIKQSSHLK DTLEDVLGID DIQFIPTGNG DVIDGAREQW NDGSNTLCIR
     PGVVVTYDRN YVSNDLLRQK GIKVIEISGS ELVRGRGGPR CMSQPLFRED I