ID   ARCA_VIBPA              Reviewed;         407 AA.
AC   Q87LG0;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=VP2652;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC60915.1; -; Genomic_DNA.
DR   RefSeq; NP_799031.1; NC_004603.1.
DR   RefSeq; WP_005455102.1; NC_004603.1.
DR   AlphaFoldDB; Q87LG0; -.
DR   SMR; Q87LG0; -.
DR   STRING; 223926.28807662; -.
DR   EnsemblBacteria; BAC60915; BAC60915; BAC60915.
DR   GeneID; 1190197; -.
DR   KEGG; vpa:VP2652; -.
DR   PATRIC; fig|223926.6.peg.2547; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; WPARHDE; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..407
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182254"
FT   ACT_SITE        397
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   407 AA;  45762 MW;  914AEF1311986656 CRC64;
     MSKLYVGSEV GQLRRVLLNR PERALTHLTP SNCHELLFDD VLAVEAAGEE HDAFARTLRE
     QDVEVLLLHD LLVETLAVPE AKQWLLNTQI SDFRYGPTFA RDLRQYLLEM DDEHLATILL
     GGLAYSELPI QSSSMLPKMK RPLDFVIEPL PNHLFTRDTS CWVYGGVSLN PMMMPARQRE
     TNHLRAIYRW HPIFAGQDFI KYFGDDDLHY DNANVEGGDV LVIGKGAVLI GMSERTTPQG
     VENLAASLFK AGQASEVIAI DLPKHRSCMH LDTVMTHMDV DTFSVYPEIM RKDLDTWRLT
     PKGTDGEMHV EASHNYLHAI ESALGLDQLK IITTGGDSYE AEREQWNDAN NVLTVKPGVV
     IGYERNVYTN EKYDKAGIQV LTVPGNELGR GRGGARCMSC PIERDDI