ID   ARCA_PSEMY              Reviewed;         416 AA.
AC   A4XRA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Pmen_1108;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP83875.1; -; Genomic_DNA.
DR   RefSeq; WP_012017788.1; NC_009439.1.
DR   AlphaFoldDB; A4XRA9; -.
DR   SMR; A4XRA9; -.
DR   STRING; 399739.Pmen_1108; -.
DR   PRIDE; A4XRA9; -.
DR   EnsemblBacteria; ABP83875; ABP83875; Pmen_1108.
DR   KEGG; pmy:Pmen_1108; -.
DR   PATRIC; fig|399739.8.peg.1120; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; SAWIYDG; -.
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..416
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000336672"
FT   ACT_SITE        404
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   416 AA;  45964 MW;  2ED8C13A85758102 CRC64;
     MSKKALGVHS EAGKLHKVMV CSPGLAHLRL TPNNCDELLF DDVIWVSQAK RDHFDFMTKM
     RERGIEVVEM HNLLEETVRD PQALKWILDR KITPNSVGLG LQGEVRSFIE GLEPRRIAEF
     LIGGVSGADL AKHKDSEAAK MFNAYLGESS FIFPPLPNTQ FTRDTTCWIY GGVTLNPMYW
     PARRQETLLT SAIYKFHPDF AGEQFEIWYG DPDQDHGAAT LEGGDVMPIG NGTVLIGMGE
     RTSHQAIGQV ARALFAKGAA QRVVVAGLGK SRAAMHLDTV FSFCDRDLVT IFPEVANSIV
     PFSLRPDESR PGGIDVRRED KSFLDVVAES LNLPKLRVVE TGGDAYEAER EQWDDGNNVV
     CLEPGVVVGY DRNTYTNTLL RKAGVEVITI SASELGRGRG GGHCMTCPII RDPIDY