ID D7DBK3_STAHD Unreviewed; 605 AA.
AC D7DBK3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=Shell_0419 {ECO:0000313|EMBL:ADI31550.1};
OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS P8).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI31550.1, ECO:0000313|Proteomes:UP000002573};
RN [1] {ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI31550.1, ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RX PubMed=22180806; DOI=10.4056/sigs.2054696;
RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Staphylothermus hellenicus P8.";
RL Stand. Genomic Sci. 5:12-20(2011).
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; CP002051; ADI31550.1; -; Genomic_DNA.
DR RefSeq; WP_013142748.1; NC_014205.1.
DR AlphaFoldDB; D7DBK3; -.
DR STRING; 591019.Shell_0419; -.
DR GeneID; 9233708; -.
DR KEGG; shc:Shell_0419; -.
DR eggNOG; arCOG00693; Archaea.
DR HOGENOM; CLU_027935_0_0_2; -.
DR OrthoDB; 24954at2157; -.
DR Proteomes; UP000002573; 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 Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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, ECO:0000313|EMBL:ADI31550.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 83..372
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 430..596
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 605 AA; 66403 MW; 3EB38C0F67FCA568 CRC64;
MVLPRIFHYD VDERISLIQT ITGKKPADIV ISNVNLVLAP TGEILDNASI IISGKRIAGA
GKYSELHRFI GKNTLVIDGE NNYAMPGFID PHIHIESSLL TPHGFAKLAL KHGTTTVVAD
PHEIGNVLGS RGVEIFIDEA RNLPLKILID IPSCVPATDP SYGLETTANI IGVDEVEKLA
ALEGTIGLGE VMDFISILNA NKAVLEKIRV AHRYGLIVNG HAPLLRGAEL DAYIDAGIWS
DHESTIYEEA LEKARKGMYV FIREGSAWKD LKALLPLIKD HSIDHRFLSF ASDDINVVDL
MEKGHMDRII NIAIEYGVDP VKAIQLATIG PATRIHLEDH VGVVGPARLA DIVLSKNIEY
IKPHTVIASG EIIYYKGESR KTFNNYKYPE EALNTVKLAK TPGPQEFIPR INNREGIVEV
NIIGVTPGSA LTKHVVEELA VKDYKVLADP SRDIIYAAVI DRHKASGSMG KGFIKGLGFK
AGAIAQTIAH DTHNLIVAGN NPEDMSRAVK RIVEIQGGIV VVDKGKIIGE LPLRLAGLMS
IEEPETVYEK YKKITKELME RYGLEFESFF MTLALVALPV IPEIRLTDKG LVNVREAKLM
PLINK
//
