ID   ARCA_CHESB              Reviewed;         408 AA.
AC   Q11G43;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Meso_2241;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG63632.1; -; Genomic_DNA.
DR   RefSeq; WP_011581574.1; NC_008254.1.
DR   AlphaFoldDB; Q11G43; -.
DR   SMR; Q11G43; -.
DR   STRING; 266779.Meso_2241; -.
DR   EnsemblBacteria; ABG63632; ABG63632; Meso_2241.
DR   KEGG; mes:Meso_2241; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_5; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
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..408
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000058987"
FT   ACT_SITE        398
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   408 AA;  45004 MW;  FA2E4A7B8E7945C6 CRC64;
     MSLVYGVHSE VGKLRRVMVH RPGTALARLT PSNCHELLFD DVIWVKQARV EHMTFVDAMR
     YRGVEVVFLR EMLTETMRIQ EARRWLLDRR VNDNTVGVGL ADDLHAHLME IDADALSSIL
     VGGLSKAELP VKTNSVVASV LTPEDFILPP LPNHIFTRDT TCWIYEGVTL NPMRWNARQL
     ETVNIAAIYR FHPDFRDAGF PVWFGDPERS FGAATAEGGD VMPIGNRAVL IGMGERTTAH
     AVGQIARSLF AHGTAERVIA CKLPKERASM HLDTVFTFCD RDLVTIFADV VNAIDAYSLR
     PGEKPGTVDV RAEEQPLTEV VAGALGLPKL RVVETGGDAY VQEREQWDDG NNVVALEPGV
     VVGYDRNVYT NTLLRKAGVE VITVPGAELG RGRGGGHCMT CPLIRDAL