ID   ARCA_BORAF              Reviewed;         409 AA.
AC   O51896;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
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;
OS   Borreliella afzelii (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=29518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R-IP3;
RX   PubMed=9402027; DOI=10.1046/j.1365-2958.1997.6051963.x;
RA   Casjens S., Murphy M., DeLange M., Sampson L., van Vugt R., Huang W.M.;
RT   "Telomeres of the linear chromosomes of Lyme disease spirochaetes:
RT   nucleotide sequence and possible exchange with linear plasmid telomeres.";
RL   Mol. Microbiol. 26:581-596(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; AF008219; AAB93998.1; -; Genomic_DNA.
DR   AlphaFoldDB; O51896; -.
DR   SMR; O51896; -.
DR   UniPathway; UPA00254; UER00364.
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..409
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182202"
FT   ACT_SITE        399
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  46812 MW;  0524047ECA16649C CRC64;
     MEEYLNPINI FSEIGRLKKV LLHRPGEELE NLTPFIMKNF LFDDIPYLEV ARQEHEVFAS
     ILKNNLVEIE YIEDLISEVL VSSVALENKF ISQFILEAEI KTDFTINLLK DYFSSLTIDN
     MISKMISGVV TEELKNYTSS LDDLVNGANL FIIDPMPNVL FTRDPFASIG NGVTINKMFT
     KVRQRETIFA EYIFKYHPVY KENVPIWLNR WEEASLEGGD ELVLNKGLLV IGISERTEAK
     SVEKLAISLF KNKTSFDTIL AFQIPKNRSY MHLDTVFTQI DYSVFTSFTS DDMYFSIYVL
     TYNPSSSKIH IKKEKARIKD VLSFYLGRKI DIIKCAGGDL IHGAREQWND GANVLAIAPG
     EIIAYSRNHV TNKLFEENGI KVHRIPSSEL SRGRGGPRCM SMPLIREDI