ID   ARCA_RHOOB              Reviewed;         405 AA.
AC   C1AXW8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=ROP_57160;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH53963.1; -; Genomic_DNA.
DR   RefSeq; WP_015889457.1; NC_012522.1.
DR   AlphaFoldDB; C1AXW8; -.
DR   SMR; C1AXW8; -.
DR   STRING; 632772.ROP_57160; -.
DR   EnsemblBacteria; BAH53963; BAH53963; ROP_57160.
DR   KEGG; rop:ROP_57160; -.
DR   PATRIC; fig|632772.20.peg.5970; -.
DR   HOGENOM; CLU_052662_0_1_11; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002212; 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..405
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000125320"
FT   ACT_SITE        395
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   405 AA;  43117 MW;  FF1E4B2D89AEB54C CRC64;
     MNASGSAPLG ANSEVGQLRA VLLHRPGDEL KRLTPRNNDQ LLFDGLPWVD RAQEEHDAFA
     DLLRSRGVEV LLLSDLLAET LGASGAARIQ GIGAAVDPRK LGHTLAQELA AHLRGVPAPE
     LSTILTAGMT FDELPVAANT ASLVRRMHHG GDFVIDPLPN LLFTRDSSFW IGPRVAITSL
     ALPARVRETS LTDIIYAHHP RFRGARRAYE SHTAPVEGGD VLLLAPGVVA VGVGERTTPA
     GAEALARSVF EDELAHTVLV VPIAQARASM HLDTVCTMVD HDAVVMYPII QDTLSAFTIH
     REDNGVSIRG ADPFLSAAAE AMGIGKLRVI DTGLDNVTAE REQWDDGNNT LALAPGVVVA
     YERNVETNAR LEASGIEVLR IAGSELGSGR GGPRCMSCPV ARDPL