ID Q1R303_ECOUT Unreviewed; 406 AA.
AC Q1R303;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Arginine deiminase {ECO:0000256|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000256|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000256|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000256|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000256|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000256|HAMAP-Rule:MF_00242};
GN OrderedLocusNames=UTI89_C4857 {ECO:0000313|EMBL:ABE10261.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE10261.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE10261.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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:0000256|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:0000256|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000256|ARBA:ARBA00010206, ECO:0000256|HAMAP-Rule:MF_00242}.
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DR EMBL; CP000243; ABE10261.1; -; Genomic_DNA.
DR RefSeq; WP_001346533.1; NZ_CP064825.1.
DR AlphaFoldDB; Q1R303; -.
DR KEGG; eci:UTI89_C4857; -.
DR HOGENOM; CLU_052662_0_0_6; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000001952; 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 {ECO:0000256|HAMAP-Rule:MF_00242};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00242}.
FT ACT_SITE 396
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 406 AA; 45771 MW; 2CC968B5A33CB738 CRC64;
MEKHYVGSEI GQLRSVMLHR PNLSLKRLTP SNCQELLFDD VLSVERAGEE HDIFANTLRQ
QGIEVLLLTD LLTQTLDIPE AKSWLLETQI SDYRLGPTFA TDVRTWLAEM SHRDLARHLS
GGLTYSEIPA SIKNMVVDTH DINDFIMKPL PNHLFTRDTS CWIYNGVSIN PMAKPARQRE
TNNLRAIYRW HPQFAGGEFI KYFGDENINY DHATLEGGDV LVIGRGAVLI GMSERTTPQG
IEFLAQALFK HRQAERVIAV ELPKHRSCMH LDTVMTHIDI DTFSVYPEVV RPDVNCWTLT
PDGHGGLKRT QESTLLHAIE KALGIDQVRL ITTGGDAFEA EREQWNDANN VLTLRPGVVV
GYERNIWTNE KYDKAGITVL PIPGDELGRG RGGARCMSCP LHRDGI
//
