ID   ARCA2_STAES             Reviewed;         411 AA.
AC   Q8CMW1;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Arginine deiminase 2;
DE            Short=ADI 2;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase 2;
DE            Short=AD 2;
GN   Name=arcA2; OrderedLocusNames=SE_2217;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05859.1; -; Genomic_DNA.
DR   RefSeq; NP_765772.1; NC_004461.1.
DR   RefSeq; WP_002437936.1; NZ_WBME01000025.1.
DR   AlphaFoldDB; Q8CMW1; -.
DR   SMR; Q8CMW1; -.
DR   STRING; 176280.SE_2217; -.
DR   EnsemblBacteria; AAO05859; AAO05859; SE_2217.
DR   GeneID; 50017714; -.
DR   KEGG; sep:SE_2217; -.
DR   PATRIC; fig|176280.10.peg.2164; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001411; 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.
FT   CHAIN           1..411
FT                   /note="Arginine deiminase 2"
FT                   /id="PRO_0000182241"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  47112 MW;  34019B46C18EDFC2 CRC64;
     MTNGPIQVNS EIGKLKTVLL KRPGKELENL VPDYLDGLLF DDIPFLKVAQ QEHDHFAQVL
     QDEGIEVLYL EKLAAQSIED SNVREQFIDD VLAESRKTIL GHEKEIKKLF STLSNQALIN
     KIMAGVRKEE IQLESTHLVE YMDDKYPFYL DPMPNLYFTR DPQASIGRGM TVNRMFWRAR
     RRESIFISYI LKHHPRFKDE NIPLWVDRDC PFNIEGGDEL VLSKDVLAIG ISERTSAQAI
     ERLARRIFKD PLSTFKKVVA IEIPTSRTFM HLDTVCTMID YDKFTTHSAI LKSEGNMNIF
     IIEYDDKAED IKIQHSSHLK QTLEEVLDVD EITLIPTGNG DIIDGAREQW NDGSNTLCIR
     PGVVVTYDRN YVSNQLLREH GIKVIEIPGS ELVRGRGGPR CMSQPLIRED L