ID   ARCA_BORBU              Reviewed;         410 AA.
AC   O51781;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Arginine deiminase;
DE            Short=ADI;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase;
DE            Short=AD;
GN   Name=arcA; OrderedLocusNames=BB_0841;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC67191.1; -; Genomic_DNA.
DR   PIR; H70204; H70204.
DR   RefSeq; NP_212975.1; NC_001318.1.
DR   RefSeq; WP_002557431.1; NC_001318.1.
DR   AlphaFoldDB; O51781; -.
DR   SMR; O51781; -.
DR   STRING; 224326.BB_0841; -.
DR   PRIDE; O51781; -.
DR   EnsemblBacteria; AAC67191; AAC67191; BB_0841.
DR   GeneID; 56567419; -.
DR   KEGG; bbu:BB_0841; -.
DR   PATRIC; fig|224326.49.peg.1234; -.
DR   HOGENOM; CLU_052662_0_1_12; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001807; 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; Reference proteome.
FT   CHAIN           1..410
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182203"
FT   ACT_SITE        400
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   410 AA;  46844 MW;  C2DF4F58E5848FAB CRC64;
     MEEEYLNPIN IFSEIGRLKK VLLHRPGEEL ENLTPLIMKN FLFDDIPYLK VARQEHEVFV
     NILKDNSVEI EYVEDLVSEV LASSVALKNK FISQFILEAE IKTDGVINIL KDYFSNLTVD
     NMVSKMISGV AREELKDCEF SLDDWVNGSS LFVIDPMPNV LFTRDPFASI GNGITINKMY
     TKVRRRETIF AEYIFKYHSA YKENVPIWFN RWEETSLEGG DEFVLNKDLL VIGISERTEA
     GSVEKLAASL FKNKAPFSTI LAFKIPKNRA YMHLDTVFTQ IDYSVFTSFT SDDMYFSIYV
     LTYNSNSNKI NIKKEKAKLK DVLSFYLGRK IDIIKCAGGD LIHGAREQWN DGANVLAIAP
     GEVIAYSRNH VTNKLFEENG IKVHRIPSSE LSRGRGGPRC MSMSLVREDI