ID A0A0P0CH34_9BACT Unreviewed; 549 AA.
AC A0A0P0CH34;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Adenine deaminase {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000256|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=DC20_04865 {ECO:0000313|EMBL:ALI98436.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI98436.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI98436.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI98436.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000479, ECO:0000256|HAMAP-
CC Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773,
CC ECO:0000256|HAMAP-Rule:MF_01518}.
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DR EMBL; CP012643; ALI98436.1; -; Genomic_DNA.
DR RefSeq; WP_062542804.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0CH34; -.
DR STRING; 512763.DC20_04865; -.
DR KEGG; rti:DC20_04865; -.
DR PATRIC; fig|512763.3.peg.1079; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000061382; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR CDD; cd01295; AdeC; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01518; Adenine_deamin; 1.
DR InterPro; IPR006679; Adenine_deam.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01178; ade; 1.
DR PANTHER; PTHR11113:SF2; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000061382}.
FT DOMAIN 46..326
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 374..539
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 549 AA; 60322 MW; 6C82B0335544048B CRC64;
MATPRFYKVS GNIIDVLHQE IYPGTLEIMD GQIARVVREP VAETHFILPG FIDAHVHVES
SMLVPSEFAR LAVPHGTVAT VSDPHEIGNV LGLKGVEYML ENGKKVPFKF FFGAPSCVPA
TPFETAGAEI TPEDIEELFL RPEVKYLAEM MNWPGVLNGD ELVMQKITLA QKFDKQVDGH
APGLRGEEAQ AYASAGMTTD HECFTAEEAK DKLAAGMKIL IREGSAAKNF EALIELLTDH
PCEIMFCSDD KHPDNLVEGH INELVKRALA KGHDLFHVLQ AACVNAVHHY KLEVGLLQEK
DPADFIVIDN PENFNVLKTY INGQLVAENG KSKIAFTPSE IINNFHAQPK TVEQFQLPAQ
DAVKIRVIEP YDGQLITGML FLDPKIKNGF IVSDPRQDVL KITVVNRYQN TEPAIAFIKN
FGLKRGAIAS SVGHDSHNII AVGCDDESLC RAVNLLIDAK GGISAVDDQR EEVLPLPVAG
IMSPEDGYWV AEQYAKLDQA AKDLGSTLTS PFMTLSFMAL LVIPALKLSD KGLFDGQHFQ
FVDVTSTLL
//
