ID   ARCA_STRGC              Reviewed;         409 AA.
AC   A8AYL1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SGO_1593;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
RN   [2]
RP   INDUCTION, TRANSCRIPTIONAL REGULATION, AND OPERON STRUCTURE.
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=18552185; DOI=10.1128/aem.00556-08;
RA   Liu Y., Dong Y., Chen Y.Y., Burne R.A.;
RT   "Environmental and growth phase regulation of the Streptococcus gordonii
RT   arginine deiminase genes.";
RL   Appl. Environ. Microbiol. 74:5023-5030(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   -!- INDUCTION: Expression of arcA is significantly higher in cells that
CC       have entered stationary phase than in exponential-phase cells. Up-
CC       regulated by low pH and by arginine. Repressed by the CcpA protein.
CC       Part of the arc operon, that consists of the arcABCDT genes.
CC       {ECO:0000269|PubMed:18552185}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00242}.
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DR   EMBL; CP000725; ABV10149.1; -; Genomic_DNA.
DR   RefSeq; WP_012130657.1; NC_009785.1.
DR   AlphaFoldDB; A8AYL1; -.
DR   SMR; A8AYL1; -.
DR   STRING; 467705.SGO_1593; -.
DR   PRIDE; A8AYL1; -.
DR   EnsemblBacteria; ABV10149; ABV10149; SGO_1593.
DR   KEGG; sgo:SGO_1593; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OMA; ERATMHL; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001131; 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   2: Evidence at transcript level;
KW   Arginine metabolism; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..409
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000078368"
FT   ACT_SITE        399
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   409 AA;  46479 MW;  74352CDE288F32BF CRC64;
     MSTHPIHVFS EIGKLKKVML HRPGKELENL MPDYLERLLF DDIPFLEDAQ KEHDNFAQAL
     RNEGIEVLYL EKLAAESLTS PEIRDQFIEE YLDEANIRGR QTKVAIRELL QGIKDNQELV
     EKTMAGVQKA ELPEIPEAAK GLTDLVESDY PFAIDPMPNL YFTRDPFATI GNAVSLNHMY
     ADTRNRETLY GKYIFKYHPV YGGNVELVYN REEDTRIEGG DELVLSKDVL AVGISQRTDA
     ASIEKLLVNI FKKNVGFKKV LAFEFANNRK FMHLDTVFTM VDYDKFTIHP EIQGNLRVFS
     VTYENEQLKI VEEKGDLAEL LAENLGVEKV TLIPCGDGNA VAAAREQWND GSNTLTIAPG
     VVVVYDRNTV TNKKLEEYGL RLIKIRGSEL VRGRGGPRCM SMPFEREEI