ID   ARCA_LIMRD              Reviewed;         410 AA.
AC   A5VIN9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Lreu_0445;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(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; CP000705; ABQ82713.1; -; Genomic_DNA.
DR   RefSeq; WP_003667540.1; NZ_AZDD01000022.1.
DR   AlphaFoldDB; A5VIN9; -.
DR   SMR; A5VIN9; -.
DR   STRING; 557436.Lreu_0445; -.
DR   PRIDE; A5VIN9; -.
DR   EnsemblBacteria; ABQ82713; ABQ82713; Lreu_0445.
DR   GeneID; 66470564; -.
DR   KEGG; lre:Lreu_0445; -.
DR   PATRIC; fig|557436.17.peg.864; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001991; 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_0000336666"
FT   ACT_SITE        398
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   410 AA;  46243 MW;  698EA5C46B76EE05 CRC64;
     MQSPIHVTSE IGKLKTVMLH RPGKEIENVY PEILHRMLVD DIPYLPIAQE EHDLFAQTLR
     DNGAEVLYLE DLLTDALADD NIKDEFLEKI IAESGYAAGA IHDGLKEFLL SFSTKDMVNK
     IIAGVRKDEI KTKYASLAEL AEDKDYPFYM DPMPNAYFTR DQQACIGDGI TINHMTFKAR
     QRESLFTEYI IKHNKRFADK GVEVWRNRYP EGRIEGGDEL VLSDHVLAIG ISQRTSAKAI
     TELAESLFEK SDYDTVIAIH IPHNHAMMHL DTVFTMINYD QFTVHPAILR DGGHVDAYIM
     HPGNNGEISI THETNLKEIL KKALDKPEID LIPTGGGDPI IAPREQWNDG SNTLAIAPGV
     VVTYDRNYVS NDLLRKHGIL VHEVRSSELS RGRGGPRCMS CPIVREDLKK