ID A0A0M9Y881_9ACTN Unreviewed; 410 AA.
AC A0A0M9Y881;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ADK54_40750 {ECO:0000313|EMBL:KOU34184.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU34184.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KOU34184.1}.
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DR EMBL; LGDD01000349; KOU34184.1; -; Genomic_DNA.
DR RefSeq; WP_053730894.1; NZ_LGDD01000349.1.
DR AlphaFoldDB; A0A0M9Y881; -.
DR PATRIC; fig|1415557.3.peg.8980; -.
DR OrthoDB; 9807502at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000037774; 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: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 400
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 410 AA; 45720 MW; 0C648CE3B7677CC9 CRC64;
MGFHVDSETG RLRRVILHRP DLELKRLTPS NKDALLFDDV LWVRRARQEH DGFADVLRDR
GVQVHLFGDL LRESLEIPAA RGLVLDRVFD EKEYGPLATG HLRAAFDELP AADLAEALVG
GMTKREFLEG HPEPTSVRFH AMDLDDFLLG PLPNHLFTRD TSAWIYDGVS INAMRWPARQ
RETVHFEAIY RHHPLFKGPE AGPFNIWSRG QSDYPSTIEG GDVLVIGNGA VLIGMSERTT
PQAVEMLARG LFAAGSARTI VALDMPKRRA FMHLDTVMTM VDGETFTQYA GLGMLRSYTI
EPGAGEQELK VTDHPQEHMH RAIAAALGLD RIRVLTATQD VHSAEREQWD DGCNVLAVEP
GVVVAYERNV TTNTHLRKEG IEVIEIRGSE LGRGRGGPRC MSCPVERDAV
//
