ID   ARCA_VIBVU              Reviewed;         406 AA.
AC   Q8DCF4;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=VV1_1467;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016795; AAO09906.1; -; Genomic_DNA.
DR   RefSeq; WP_011079424.1; NC_004459.3.
DR   AlphaFoldDB; Q8DCF4; -.
DR   SMR; Q8DCF4; -.
DR   EnsemblBacteria; AAO09906; AAO09906; VV1_1467.
DR   KEGG; vvu:VV1_1467; -.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; WPARHDE; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002275; 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.
FT   CHAIN           1..406
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182255"
FT   ACT_SITE        396
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   406 AA;  45862 MW;  2741DC0AAFFFD418 CRC64;
     MSKLYVGSEV GQLRRVLLNR PERALTHLTP SNCHELLFDD VLLVEAAGKE HDAFADTLRQ
     QGVEVLLLHD LMVDTLAVPE AKQWLLDVQI SDFRYGPIFA RDLRRYLSEM DNEHLATILL
     GGLAYSELPI QSASMLPRMK QPLDFVIEPL PNHLFTRDTS CWVYGGVSLN PMMKPARQRE
     TNHLRAIYQW HPIFAGQDFI KYFGNEDLHY DNANIEGGDV LVIGKGAVLI GMSERTTPQG
     VENLAANLFK HGQAKEVIAI ELPKHRSCMH LDTVMTHMDV DTFSVYPEIM RKDLHTWRLT
     PKGNGEMQVE ALHNYLHAIE RALGLNHLNI ITTGGDSYEA EREQWNDANN VLTVKPGVVI
     GYERNVYTNE KYDKAGIEVL TIPGNELGRG RGGARCMSCP IERDDI