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 27-MAR-2024, 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=MRA_1010;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 GeneID; 45424973; -.
DR KEGG; mra:MRA_1010; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_11; -.
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 Gene3D; 1.10.3930.10; Arginine deiminase; 1.
DR HAMAP; MF_00242; Arg_deiminase; 1.
DR InterPro; IPR003876; Arg_deiminase.
DR NCBIfam; TIGR01078; arcA; 1.
DR PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR Pfam; PF02274; ADI; 1.
DR PIRSF; PIRSF006356; Arg_deiminase; 1.
DR PRINTS; PR01466; ARGDEIMINASE.
DR SUPFAM; SSF55909; Pentein; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase; Reference proteome.
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
//
