ID H8GX20_DEIGI Unreviewed; 418 AA.
AC H8GX20;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:AFD24560.1};
GN Name=argE {ECO:0000313|EMBL:AFD24560.1};
GN OrderedLocusNames=DGo_CA0633 {ECO:0000313|EMBL:AFD24560.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD24560.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD24560.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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DR EMBL; CP002191; AFD24560.1; -; Genomic_DNA.
DR RefSeq; WP_014684043.1; NC_017790.1.
DR AlphaFoldDB; H8GX20; -.
DR STRING; 745776.DGo_CA0633; -.
DR KEGG; dgo:DGo_CA0633; -.
DR PATRIC; fig|745776.4.peg.647; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_0; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 418 AA; 45026 MW; A95D153A789DDAE3 CRC64;
MTALPSPAVD PARTLAELKD LRALTGDENG AQRVAFTPRW LAARQFLKDR LAELPAEVHQ
DAAGNLWATL RGDSERELLI GGHLDSVPGG GWLDGCLNVL AGLEVLRRVS AQYGGRPPVT
LRLVDWADEE GARFGRSLYG SSAASGFFDV TELAKLRDRD GVALGDALRE VGVTLEDAPQ
ARAELAKAAA YLELHIEQGP VLEGLGLPLG AVLGTVGVER HTLTFRGQAA HSGSTPMNVR
RDAFLAAGRF GQEIYAIAER HGGVCTVGSV KTWPGIVTSV VETCELTLDQ RHLDAGKLAA
MWQDAQDAAR RFAEEGGCTV DFGYLWNIEP IPFHPELIDA AEASILEVTP ATHRLPSGPL
HDAAEVARAG VPTVMLFVQS LRGISHNKIE DTREDHIALS VQALDRLTTR AMAWVQER
//
