ID A9D2F8_HOEPD Unreviewed; 566 AA.
AC A9D2F8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=HPDFL43_14407 {ECO:0000313|EMBL:EDQ34197.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ34197.1, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ34197.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ34197.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ34197.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ34197.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-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:EDQ34197.1}.
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DR EMBL; ABIA03000004; EDQ34197.1; -; Genomic_DNA.
DR RefSeq; WP_007198643.1; NZ_CM002917.1.
DR AlphaFoldDB; A9D2F8; -.
DR STRING; 411684.HPDFL43_14407; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_5; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000004291; 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:EDQ34197.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000004291}.
FT DOMAIN 66..347
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 395..561
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 566 AA; 61077 MW; ED081CD5E2549806 CRC64;
MTSRLGDMID QGQGKAPADI VLKGGKLFDL TTGELRDGDI AICGDRIVGT LESYSGIEEI
DISGRIVVPG FIDTHLHIES SLVTPHEFDR CVLPRGVTTA ICDPHEIANV IGATGIRYFL
DCSEQTIMDI RVQLSSCVPA THLETAGARL DIEDLLPFRD HPQVIGLAEF MNFPGVLFKD
PACMAKLEAF QGGHIDGHAP LLRGLGLNGY LAAGIRTEHE STTAEEALEK MSKGMHVLVR
EGSVSRDLDA LIPIITERNS PFLALCTDDR NPLDIAEHGH LDYMIRHAIA NGVEPLAIYR
AASISAARAF GLRDRGLVAP GWRADLVVLD SLEDCNAQMV FSAGRRVTDA LFATRKQTEL
VGTDSVRAPL VEAGSFTVRK NRSSTPVIGI VPGKIITERR DLDLAIDNGE KQIDLARDIL
KIAVIERHGK NGNIATGFVQ GFGLKRGAIA STIGHDSHNI CVVGATEADM AVAANRLSEI
RGGFVVAEDG KVIAEIALPV AGLMSDQPYE WVRETLIPLR KAAKSLGGTL DEPFLQLAFL
PLPVIPHLKI SDRGMIDVDA FEIIDP
//
