ID   ARCA_LACLM              Reviewed;         410 AA.
AC   Q9K576; A2RNI7;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=llmg_2313;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Aungpraphapornchai P., Mulholland F., Griffin H.G., Gasson M.J.;
RT   "Cloning, sequencing and analysis of the genes involved in the arginine
RT   deiminase pathway of Lactococus lactis.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AJ250129; CAB93579.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98877.1; -; Genomic_DNA.
DR   RefSeq; WP_011835985.1; NZ_WJVF01000005.1.
DR   AlphaFoldDB; Q9K576; -.
DR   SMR; Q9K576; -.
DR   STRING; 416870.llmg_2313; -.
DR   EnsemblBacteria; CAL98877; CAL98877; llmg_2313.
DR   GeneID; 61110358; -.
DR   KEGG; llm:llmg_2313; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   PhylomeDB; Q9K576; -.
DR   BioCyc; LLAC416870:LLMG_RS11595-MON; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000000364; Chromosome.
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..410
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182214"
FT   ACT_SITE        400
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   410 AA;  45981 MW;  52B274A1E3959C06 CRC64;
     MNNGINVNSE IGKLKSVLLH RPGAEVENIT PDTMKQLLFD DIPYLKIAQK EHDFFAQTLR
     DNGAETVYIE NLATEVFEKS SETKEEFLSH LLHEAGYRPG RTYDGLTEYL TSMPTKDMVE
     KVYAGVRKNE LDIKRTALSD MAGSDAENYF YLNPLPNAYF TRDPQASMGV GMTINKMTFP
     ARQPESLITE YVMANHPRFK DTPIWRDRNH TTRIEGGDEL ILNKTTVAIG VSERTSSKTI
     QNLAKELFAN PLSTFDTVLA VEIPHNHAMM HLDTVFTMIN HDQFTVFPGI MDGAGNINVF
     ILRPGQDGEV EIEHLTDLKA ALKKVLNLSE LDLIECGAGD PIAAPREQWN DGSNTLAIAP
     GEIVTYDRNY VTVELLKEHG IKVHEILSSE LGRGRGGARC MSQPLWREDL