ID   ARCA_RHILO              Reviewed;         412 AA.
AC   Q988I1;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=mll6733;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52969.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q988I1; -.
DR   SMR; Q988I1; -.
DR   STRING; 266835.14026372; -.
DR   EnsemblBacteria; BAB52969; BAB52969; BAB52969.
DR   KEGG; mlo:mll6733; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_5; -.
DR   OMA; SAWIYDG; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000552; 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.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; Hydrolase.
FT   CHAIN           1..412
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182229"
FT   ACT_SITE        400
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   412 AA;  45661 MW;  3E9750B0C3238673 CRC64;
     METKFGVHSE VGQLRKVMVC APGRAHQRLT PSNCDALLFD DVLWVDNAKR DHFDFMTKMR
     DRGVEVVEMH NLLAETVAVP EGKKWILDNQ VVPNQIGLGL VDEVRSYLEG LSNRDLAETL
     IGGLSTHEFP ESIGGEQLEL IRDAAGVNEY LLPPLPNTLY TRDTTCWIYG GVTQNPLYWP
     ARHEETILTT SIYKFHPDFA GKVNVWWGDP TKDWGLATLE GGDVMPIGKG NVLIGMSERT
     SRQAISQLAA TLFEKGAAER VIVAAMPKLR AAMHLDTVFT FADRDCVLLY PDIVNGIEAF
     SYRPDGKGGV ELHKDKGTFV ETVRDALGLK KMRVVETGGN AYMRERTQWD SGANLVCASP
     GVVYAYDRNT YTNTLLRKEG IEVITIIGAE LGRGRGGGHC MTCPIIRDAV DY