ID   ARCA_PSEPU              Reviewed;         420 AA.
AC   P41142;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Arginine deiminase;
DE            Short=ADI;
DE            EC=3.5.3.6;
DE   AltName: Full=Arginine dihydrolase;
DE            Short=AD;
GN   Name=arcA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4359 / IAM 1506 / JCM 20188;
RA   Wilson S.D., Wang M., Filpula D.;
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CHARACTERIZATION, AND CRYSTALLIZATION.
RX   PubMed=237904; DOI=10.1016/s0021-9258(19)41341-0;
RA   Shibatani T., Kakimoto T., Chibat I.;
RT   "Crystallization and properties of L-arginine deiminase of Pseudomonas
RT   putida.";
RL   J. Biol. Chem. 250:4580-4583(1975).
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   -!- ACTIVITY REGULATION: Activated by Mg(2+) or Mn(2+) and strongly
CC       inhibited by Zn(2+). {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR   EMBL; U07185; AAA16964.1; -; Unassigned_DNA.
DR   RefSeq; WP_016485080.1; NZ_CP022560.1.
DR   AlphaFoldDB; P41142; -.
DR   SMR; P41142; -.
DR   STRING; 1240350.AMZE01000025_gene1683; -.
DR   PRIDE; P41142; -.
DR   eggNOG; COG2235; Bacteria.
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   1: Evidence at protein level;
KW   Arginine metabolism; Cytoplasm; Hydrolase.
FT   CHAIN           1..420
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182227"
FT   ACT_SITE        408
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  46620 MW;  4EE3BF5DD504AF2F CRC64;
     MSAEKQKYGV HSEAGKLRKV MVCSPGLAHK RLTPSNCDEL LFDDVIWVDQ AKRDHFDFVT
     KMRERGVDVL EMHNLLTDIV QQPEALKWIL DRKITSDTVG VGLTNEVRSW LEGLEPRHLA
     EFLIGGVAGQ DLPVSEGAEV IKMYNKYLGH SSFILPPLPN TQFTRDTTCW IYGGVTLNPM
     YWPARRQETL LTTAIYKFHK EFTGADFQVW YGDPDKDHGN ATLEGGDVMP VGKGIVLIGM
     GERTSRHAIG QLAQNLFEKG AAEKIIVAGL PKSRAAMHLD TVFSFCDRDL VTVFPEVVKE
     IKPFIITPDS SKPYGMNIAP QDASFLEVVS EQLLGKKDKL RVVETGGNSF AAEREQWDDG
     NNVVALEPGV VIGYDRNTYT NTLLRKAGIE VITISAGELG RGRGGGHCMT CPIVRDPIDY