ARCA_RHOE4
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 03-AUG-2022, entry version 71.
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; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC 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 STRING; 234621.RER_43760; -.
DR PRIDE; C1A399; -.
DR EnsemblBacteria; BAH35084; BAH35084; RER_43760.
DR GeneID; 57485728; -.
DR KEGG; rer:RER_43760; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_11; -.
DR OMA; ERATMHL; -.
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 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_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