ARCA_BORAP
ID ARCA_BORAP Reviewed; 409 AA.
AC Q0SM08; G0IQN3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BAPKO_0896, BafPKo_0869;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH02120.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL70058.1; -; Genomic_DNA.
DR RefSeq; WP_011601268.1; NC_017238.1.
DR AlphaFoldDB; Q0SM08; -.
DR SMR; Q0SM08; -.
DR STRING; 390236.BafPKo_0869; -.
DR EnsemblBacteria; AEL70058; AEL70058; BafPKo_0869.
DR KEGG; baf:BAPKO_0896; -.
DR KEGG; bafz:BafPKo_0869; -.
DR PATRIC; fig|390236.22.peg.830; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_12; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000005216; 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..409
FT /note="Arginine deiminase"
FT /id="PRO_1000005713"
FT ACT_SITE 399
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 409 AA; 46797 MW; E1A63CE47742834C CRC64;
MEEYLNPINI FSEIGRLKKV LLHRPGEELE NLTPFIMKNF LFDDIPYLEV ARQEHEVFAS
ILKNNLVEIE YIEDLVSEVL VSSVALQNKF 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