ID   ARCA_ALIFM              Reviewed;         406 AA.
AC   B5F9Q1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=VFMJ11_0398;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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; CP001139; ACH65298.1; -; Genomic_DNA.
DR   RefSeq; WP_012532958.1; NC_011184.1.
DR   AlphaFoldDB; B5F9Q1; -.
DR   SMR; B5F9Q1; -.
DR   PRIDE; B5F9Q1; -.
DR   EnsemblBacteria; ACH65298; ACH65298; VFMJ11_0398.
DR   KEGG; vfm:VFMJ11_0398; -.
DR   HOGENOM; CLU_052662_0_0_6; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001857; 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..406
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000100753"
FT   ACT_SITE        396
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   406 AA;  46231 MW;  86DDBA7EE6D09F25 CRC64;
     MNKLFVGSEI GQLRRVILHR PERALSHLTP TNCHNLLFDD VLSVEKALLE HDQFVKTLEN
     QGVDVLLLQD LLEQTLENPE AKEWLLKHQI SHYRFGPTFA NQIRSFLLEH SNKELASILL
     GGLAFIELPF KAPSMLQQLS DPFDFVIDPL PNHLFTRDTS CWIYGGVSIN PMAKAARKRE
     SNHLRAIYRW HPLFSNQDFA RYFEDENRYY DNATIEGGDV LVIGKGNVLV GISERTTPQG
     IENLAKQLFR THQAKQVIAI KLPEDRSCMH LDTVMTHMDH NVFSVYPRVI DKNMGCWSIT
     PCGEQHLDIK EMPNFQNVLM SALELDNLNI ITTGGDSYEA EREQWHDANN VLTIKPGVVV
     AYERNTYTNE KYDKAGIHVL PITGDELGRG RGGARCMSCP IERDGI