ID   ARCA_ALIF1              Reviewed;         406 AA.
AC   Q5E7U3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=VF_0408;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW84903.1; -; Genomic_DNA.
DR   RefSeq; WP_011261199.1; NC_006840.2.
DR   RefSeq; YP_203791.1; NC_006840.2.
DR   AlphaFoldDB; Q5E7U3; -.
DR   SMR; Q5E7U3; -.
DR   STRING; 312309.VF_0408; -.
DR   EnsemblBacteria; AAW84903; AAW84903; VF_0408.
DR   KEGG; vfi:VF_0408; -.
DR   PATRIC; fig|312309.11.peg.398; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000537; 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:0008218; P:bioluminescence; IMP:CACAO.
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..406
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000100752"
FT   ACT_SITE        396
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   406 AA;  46289 MW;  B46FFC3F22E806B0 CRC64;
     MNKLFVGSEI GQLRRVILHR PERALSHLTP TNCHNLLFDD VLSVEKALLE HDQFVKTLEN
     QDVDVLLLQD LLEQTLENPE AKEWLLKHQI SHYRFGPTFA NQIRVFLLEH SNKELASILL
     GGLAFIELPF KAPSMLQQLS DPFDFVIAPL PNHLFTRDTS CWIYGGVSIN PMAKAARKRE
     SNHLRAIYRW HPLFSHHDFA RYFEDENRYY DNATIEGGDV LVIGKGNVLV GISERTTPQG
     IENLAKQLFR THQAKQVIAI KLPEDRSCMH LDTVMTHMDH NVFSVYPRVI DKNMGCWSIT
     PCGEQHLDIK EMPNFQNVLM SALELDNLNI ITTGGDSYEA EREQWHDANN VLTIKPGVVV
     AYERNTYTNE KYDKAGIHVL PITGDELGRG RGGARCMSCP IERDGI