ID A9ECH7_9FLAO Unreviewed; 539 AA.
AC A9ECH7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=KAOT1_09966 {ECO:0000313|EMBL:EDP94366.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP94366.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP94366.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP94366.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(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}.
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:EDP94366.1}.
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DR EMBL; ABIB01000019; EDP94366.1; -; Genomic_DNA.
DR RefSeq; WP_007094552.1; NZ_DS544873.1.
DR AlphaFoldDB; A9ECH7; -.
DR STRING; 391587.KAOT1_09966; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_10; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000002945; 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 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};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945}.
FT DOMAIN 40..317
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 368..532
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 539 AA; 58993 MW; 8FB64ED1295C27F3 CRC64;
MIKQGNIVDI FNKRIYKGEI HAEAGKIVNI LEKDHDNETY IIPGFVDAHI HIESSMLVPS
EFARLAVLHG TVATVSDPHE IANVLGKAGV EFMIENGKKV PFKFNFGAPS CVPATSFESA
GAVIDSDDIK ELLAKPEIKY LAEMMNYPGV LFDDAEVLKK IAWAKHFDKP VDGHAPGLRG
DDVSKYIAAG ISTDHECFTY DEALEKLQKG MKVIIREGSA AKNFEALIPL LDEHYAEMMF
CSDDKHPDDL LLGHINQLCA RAVAKGNDIF KVLQVACVNP VEHYKLDVGQ LQKGDAADFV
VLEDLTNFKV LETYINGIRV ASGETSHIDS VPFEILNNFN TSAKNVVDFQ VKATKSKIRV
IEALDGELVT NELILDNLVE DGNLVSNTAE DILKMTVVNR YQDEVPAMAF IKNFGLKEGA
IASSVGHDSH NIIAVGVSDE AICKAVNLLI ENKGGICAVS EKDEKVVSLP VAGIMSDKTG
WEIGEEYAEL DKLAKEMGST LRAPYMSLSF MALLVIPSLK LSDKGLFNGT TFEFTSLEV
//
