ARCA_BORGP
ID ARCA_BORGP Reviewed; 409 AA.
AC Q65ZT1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; OrderedLocusNames=BG0868;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000013; AAU07690.1; -; Genomic_DNA.
DR RefSeq; WP_011194134.1; NZ_CP028872.1.
DR AlphaFoldDB; Q65ZT1; -.
DR SMR; Q65ZT1; -.
DR STRING; 290434.BG0868; -.
DR EnsemblBacteria; AAU07690; AAU07690; BG0868.
DR KEGG; bga:BG0868; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_12; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000002276; 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_0000182204"
FT ACT_SITE 399
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 409 AA; 46690 MW; C36F23CACC67DEA8 CRC64;
MEGYLNPINI FSEIGRLKKV LLHRPGEELE NLTPFIMKKF LFDDIPYLEV ARQEHEVFAS
TLKNNSVEIE YVEDLVSEVL ASSVALKDKF ISQFILEAEI KTDSTINILK DYFSNLTIDN
MVSKMISGIV SKELKNYVSS LDDLVNSASL FIIDPMPNVL FTRDPFASIG NGITINKMSN
KVRHRETIFA EYIFKYHPIY KKNVPIWFNR WEESSLEGGD EFVLSKDILV IGISERTEAE
SVEKLAISLF KNKTSFNTIL AFKIPKNRAY MHLDTVFTQI DYSVFTSFTS DDMYFSIYAL
TYNSSSSKIH VKEEKARLRD VLSFYLGRKI DIIKCAGGDL IHGAREQWND GANILAIAPG
EVIAYSRNHV TNKLFEENGI KVYRIPSSEL SRGRGGPRCM SMPLVREDI