ID   ARCA_VIBCM              Reviewed;         407 AA.
AC   C3LRF4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=VCM66_0408;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP04734.1; -; Genomic_DNA.
DR   RefSeq; WP_001081182.1; NC_012578.1.
DR   AlphaFoldDB; C3LRF4; -.
DR   SMR; C3LRF4; -.
DR   EnsemblBacteria; ACP04734; ACP04734; VCM66_0408.
DR   GeneID; 57739162; -.
DR   KEGG; vcm:VCM66_0408; -.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; WPARHDE; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001217; Chromosome I.
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..407
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000125329"
FT   ACT_SITE        397
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   407 AA;  45904 MW;  B07EF67C3CED54EF CRC64;
     MNRLYVGSEV GQLRRVLLNR PERALTHLTP SNCHELLFDD VLAVEAAGVE HDAFANTLRT
     QDVEVLLLHD LLEETLAIPE ARQWLLNTQI SDFRFGPTFA RELRHALNHL DDHHLTTLLL
     GGLAFSELHL ESDSMLPKMR QPLDFVIEPL PNHLFTRDTS CWVYGGVSLN PMMKPARQRE
     TNHLRAIYRW HPIFAQHPFI HYFGIDDLHY DNANIEGGDV LVIGKGAVLI GMSERTSPQG
     VENLAAALFK HGQASKVIAI NLPKHRSCMH LDTVMTHMDV DTFSVYPEVM RKDLPTWRLT
     PKGNNGDMRV EQVPSYLHAI EQALGVDYLK IITTGGNSYE AEREQWNDAN NVLTVKPGVV
     IGYERNVYTN EKYDKAGIKV LTIPGNELGR GRGGARCMSC PIERDGI