ID   ARCA1_STAES             Reviewed;         411 AA.
AC   Q8CQG5;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Arginine deiminase 1;
DE            Short=ADI 1;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase 1;
DE            Short=AD 1;
GN   Name=arcA1; OrderedLocusNames=SE_0106;
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; AAO03703.1; -; Genomic_DNA.
DR   RefSeq; NP_763661.1; NC_004461.1.
DR   RefSeq; WP_002485355.1; NZ_WBME01000039.1.
DR   AlphaFoldDB; Q8CQG5; -.
DR   SMR; Q8CQG5; -.
DR   STRING; 176280.SE_0106; -.
DR   EnsemblBacteria; AAO03703; AAO03703; SE_0106.
DR   KEGG; sep:SE_0106; -.
DR   PATRIC; fig|176280.10.peg.100; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; SAWIYDG; -.
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 1"
FT                   /id="PRO_0000182240"
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  47285 MW;  55E986D43995A53A CRC64;
     MVQGPIQVNS EIGKLKTVLL KRPGKELENL VPDHLSGLLF DDIPYLKVAQ EEHDKFAQTL
     RDEGIEVVYL EKLAAESITE PEVRENFIND ILTESKKTIL GHETEIKEFF SKLSDQELVN
     KIMAGIRKEE IQLETTHLVE YMDDRYPFYL DPMPNLYFTR DPQASIGRGM TINRMYWRAR
     RRESIFMTYI LKHHPRFKDK DVPVWLDRNS PFNIEGGDEL VLSKDVLAIG ISERTSAQAI
     EKLARNIFKD ANTSFKKIVA IEIPNTRTFM HLDTVLTMID YDKFTVHAAI FKEENNMNIF
     TIEQNDGKDD IKITRSSKLR ETLAEVLEVE KVDFIPTGNG DVIDGAREQW NDGSNTLCIR
     PGVVVTYDRN YVSNQLLRDK GIKVIEITGS ELVRGRGGPR CMSQPLFRED I