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Database: UniProt
Entry: H1PRT1_9FUSO
LinkDB: H1PRT1_9FUSO
Original site: H1PRT1_9FUSO 
ID   H1PRT1_9FUSO            Unreviewed;       570 AA.
AC   H1PRT1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=HMPREF0402_01124 {ECO:0000313|EMBL:EHO83094.1};
OS   Fusobacterium ulcerans 12-1B.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=457404 {ECO:0000313|EMBL:EHO83094.1, ECO:0000313|Proteomes:UP000003233};
RN   [1] {ECO:0000313|EMBL:EHO83094.1, ECO:0000313|Proteomes:UP000003233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12_1B {ECO:0000313|EMBL:EHO83094.1,
RC   ECO:0000313|Proteomes:UP000003233};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium ulcerans 12_1B.";
RL   Submitted (JUL-2012) 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}.
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:EHO83094.1}.
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DR   EMBL; AGWJ02000002; EHO83094.1; -; Genomic_DNA.
DR   RefSeq; WP_008696563.1; NZ_KE161007.1.
DR   AlphaFoldDB; H1PRT1; -.
DR   PATRIC; fig|457404.5.peg.145; -.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   Proteomes; UP000003233; Unassembled WGS sequence.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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   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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT   DOMAIN          55..341
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          398..563
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   570 AA;  64165 MW;  1B09C2616C6B724E CRC64;
     MKIDLLIKNV KIYNSYLKKF KEANVAILDK KILHVDTKKE IEFDAEKIID GKNQYMVPGL
     IDIHMHIESS MMTPAPFCHQ LAKNGVTTIV AEPHEIANVF GDRGIYAMIK AEDNIDTSIF
     YGIPSSVPST SEELETTGAV IDCEGMKKIA ENPNVICVGE VMNYRKVIVD DTLEICRFIE
     YVKKEKPTYA IEGHCPKLLD LELSKFLYLG INGDHTEHTM EEFKQRFENG MFVEIQAKSI
     EKELIDYIKE NNLYEHFSFV TDDVMADTFL NEGHLNVVMK KAVKEGLRIE DAIYSATYTP
     ARRMHLLDRG VLAPGKKADF LFVEDLEKFE IKNTFIDGKE VYNSSEEKKY IPTTYRFPED
     FYRSVHVKNI KAEDIKIPVE TTEKEVMCRV IEVSDGSTRT KELIRPVPVK DGYLDWESSE
     YCLIAVFERH GKNGNIGFGL VTGDSIKKGA IATTYAHDHH NLMVIGKTAV DIIKAANRII
     EIQGGICAME NGNILAEVEL PVAGILSEKS VEELGKEVEK LRGAMKALGY KHYNPIMSLC
     TLSLPVSPAL KITDKGLIDV AESKVVSLIA
//
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