ID   ARCA_RHOE4              Reviewed;         405 AA.
AC   C1A399;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=RER_43760;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
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-2005) 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; AP008957; BAH35084.1; -; Genomic_DNA.
DR   RefSeq; WP_019744713.1; NC_012490.1.
DR   AlphaFoldDB; C1A399; -.
DR   SMR; C1A399; -.
DR   GeneID; 57485728; -.
DR   KEGG; rer:RER_43760; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_11; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002204; 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   Gene3D; 1.10.3930.10; Arginine deiminase; 1.
DR   HAMAP; MF_00242; Arg_deiminase; 1.
DR   InterPro; IPR003876; Arg_deiminase.
DR   NCBIfam; TIGR01078; arcA; 1.
DR   PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR   PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR   Pfam; PF02274; ADI; 1.
DR   PIRSF; PIRSF006356; Arg_deiminase; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; Hydrolase.
FT   CHAIN           1..405
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000204477"
FT   ACT_SITE        395
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   405 AA;  43520 MW;  2ACC41A4D7427F4B CRC64;
     MNASGSVPLG VDSEVGRLRS VILHRPGDEL KRLTPRNNDE LLFDALPWVD RAQEEHDQFA
     TVLRERGVEV LLLSDLLTEA LEVSGAARIQ GIAAAVDARK IGHALGQHLA AYLRKVEPKE
     LSSILTAGMT FDELPIDAGS TSLVRRMHHG GDFVIDPLPN LLFTRDSSFW VGPRVIITSL
     ALSARARESS ITDLVYAHHP RFKGVRRAYE SHTAPVEGGD VLLLAPGVIA IGVGERTSPA
     GAEALARSVF DDGLAHTVLV VPIEQRRASM HLDTVCTMVE ADAVVMYPAI QDTLAAFTLR
     KEDDGVSIRG ATPFLEAAAD AMGIGKLRVI DTGLDTVTAE REQWDDGNNT LAVEPGVVVA
     YERNVETNAR LEASGIEVLR IAGSELGSGR GGPRCMSCPI ARDPL
//