ID   ARCA_MYCTA              Reviewed;         402 AA.
AC   A5U144;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=MRA_1010;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(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   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00242}.
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DR   EMBL; CP000611; ABQ72744.1; -; Genomic_DNA.
DR   RefSeq; WP_003405169.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U144; -.
DR   SMR; A5U144; -.
DR   STRING; 419947.MRA_1010; -.
DR   EnsemblBacteria; ABQ72744; ABQ72744; MRA_1010.
DR   GeneID; 45424973; -.
DR   KEGG; mra:MRA_1010; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_11; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000001988; 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..402
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000005718"
FT   ACT_SITE        392
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   402 AA;  43089 MW;  16E5B4BEAA1745D2 CRC64;
     MGVELGSNSE VGALRVVILH RPGAELRRLT PRNTDQLLFD GLPWVSRAQD EHDEFAELLA
     SRGAEVLLLS DLLTEALHHS GAARMQGIAA AVDAPRLGLP LAQELSAYLR SLDPGRLAHV
     LTAGMTFNEL PSDTRTDVSL VLRMHHGGDF VIEPLPNLVF TRDSSIWIGP RVVIPSLALR
     ARVREASLTD LIYAHHPRFT GVRRAYESRT APVEGGDVLL LAPGVVAVGV GERTTPAGAE
     ALARSLFDDD LAHTVLAVPI AQQRAQMHLD TVCTMVDTDT MVMYANVVDT LEAFTIQRTP
     DGVTIGDAAP FAEAAAKAMG IDKLRVIHTG MDPVVAEREQ WDDGNNTLAL APGVVVAYER
     NVQTNARLQD AGIEVLTIAG SELGTGRGGP RCMSCPAARD PL