ID D8F9A0_9DELT Unreviewed; 585 AA.
AC D8F9A0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=NPH_1704 {ECO:0000313|EMBL:EFK07676.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK07676.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK07676.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK07676.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
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};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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:EFK07676.1}.
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DR EMBL; ADZZ01000482; EFK07676.1; -; Genomic_DNA.
DR AlphaFoldDB; D8F9A0; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 549..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..356
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 420..577
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 585 AA; 63458 MW; D28E1FA8D38E9CF1 CRC64;
MENGKNLRQL ADVALGKTPA DVVIKNGVLM DVYTGRMVPG RSVAMAGEWI SYVGPDADYA
IGPETHVIDA GGRVICPGYI DAHTHLANYA DFSDSLAYAV PSGVTAVLTE IDSYAFALGK
EGVNAFLTQT ESCPIKVYVA VPSMVSLSPA TEPIRITNEQ LSELFTHPRV IALGESYWQE
AILTDDDSVL DLMAEARKMR KSIQGHAAGA FDRKLAAYVA TGVESCHEAI STEDVINRLE
MGLYAMIREG DIRRDLEIIL PLRDKVDFRR MILVTDGTNP DFLLEKGYLQ DVVQKAVDLG
VAPMDAVRMV TLNPAEHLGL DNLIGGVAPG RYADLLLLGD FKNMKPEMVI SKGRIVAEKG
HMCISIPDAD PPEIFLNTVN VEPISPADLQ IPESLSDEAG QIRSIDIQPG GLVAREGRGV
PVVSGKYLMA DPEKDLLKIV FVERISGKGE KFAGFVRGWG QRRGGIATST CWDAGGIVGI
GENDEDLAAA VNRVIEMQGG MTLVVEGRLE AEIPFPSGGY VSDLKIPQLA LRLKEFQNVM
VSLGFIHDYA LLALSVMTGA AIPFIRMTEK GYYRFRENDF VGLAL
//
