ID H0F6X3_9BURK Unreviewed; 383 AA.
AC H0F6X3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=KYC_12918 {ECO:0000313|EMBL:EHK66031.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK66031.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK66031.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK66031.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
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|ARBA:ARBA00001190, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00005213, ECO:0000256|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK66031.1}.
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DR EMBL; AGUF01000046; EHK66031.1; -; Genomic_DNA.
DR AlphaFoldDB; H0F6X3; -.
DR STRING; 477184.KYC_12918; -.
DR PATRIC; fig|477184.5.peg.2554; -.
DR eggNOG; COG2235; Bacteria.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000003113; Unassembled WGS sequence.
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 PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR PANTHER; PTHR47271:SF3; 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 373
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 383 AA; 42055 MW; A8984C207C7E1FD1 CRC64;
MTPSNCDALL FDDVLWVDNA KRDHFDFMTK MRDRGVDVVE MHNLLAETLE VPEAKKWILD
NQVVANQVGL GLLDEIRSYL DGLPARQLAE TLIGGLSTEE FPESVGGEQL MLIKEAAGVT
EYLLPPLPNT LYTRDTTCWI YGGVTLNPLY WPARHEETIL TSSIYKFHPR FAGKVNVWWG
DPTADHGLAT LEGGDVMPIG NRTVLIGMSE RTSRQAISQL AATLFAKDAA DRVIVAAMPK
LRAAMHLDTV LTFADRDCVL MYPDIVNNIQ AFSYRPADGT GKLELHKDKG SLVDVIGGAL
GIKKMRVVET GGNAYMRERT QWDSGANLVC VSPGTVLAYD RNVYTNTLLR KAGIEVITFA
GAELGRGRGG GHCMTCPISR DPA
//
