ID A0A0P7YE47_9RHOB Unreviewed; 409 AA.
AC A0A0P7YE47;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ECO:0000313|EMBL:KPP86824.1};
GN ORFNames=HLUCCO07_13345 {ECO:0000313|EMBL:KPP86824.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP86824.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP86824.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP86824.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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|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:KPP86824.1}.
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DR EMBL; LJSU01000014; KPP86824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YE47; -.
DR STRING; 1666914.HLUCCO07_13345; -.
DR PATRIC; fig|1666914.4.peg.1581; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000050369; 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 399
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 409 AA; 44839 MW; AE230F2612FE123D CRC64;
MSDMELGVHS ETGRLRQVIV CKPGRAHRRL TPENCEHLLF DDVFWVKQAQ KDHDVFADLM
RGEGVEVLDT GLLLGEVLDI PEARGWVLDH RVTPQEIGVG MNDDLRAWMD ELQGPELAEY
LMGGLTVDDL PFEPAGMFGS YLGRLGFVLP PLPNTLFSRD NSAWIYSGVT LNPMYWQARR
PETLLTAAIY RFHPKFAGRA EVLWGDPTHD FGRATLEGGD VMPVGDGLVL IGMGERTSPQ
AVGLLAEALF DQGRATRVLA CQLPKSRAAM HLDTVFTFCG GEVVTSFTEV AAEMTVYDLH
PGEGRAPLDI RRIDRPLFDV LAKAMGLKKL TVVPTGGADT FEASREQWND GNNVLALRPG
VVVGYDRNDD TNAALRTEGI EVLEVPGAEL GRGRGGGRCM SCPTIRDPA
//