ID C6JQ32_FUSVA Unreviewed; 570 AA.
AC C6JQ32;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, 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 ORFNames=FVAG_00113 {ECO:0000313|EMBL:EES62424.1};
OS Fusobacterium varium ATCC 27725.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469618 {ECO:0000313|EMBL:EES62424.1, ECO:0000313|Proteomes:UP000004505};
RN [1] {ECO:0000313|EMBL:EES62424.1, ECO:0000313|Proteomes:UP000004505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES62424.1,
RC ECO:0000313|Proteomes:UP000004505};
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., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium varium ATCC 27725.";
RL Submitted (MAY-2011) 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:EES62424.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACIE02000001; EES62424.1; -; Genomic_DNA.
DR RefSeq; WP_005946824.1; NZ_GL987995.1.
DR AlphaFoldDB; C6JQ32; -.
DR STRING; 469618.FVAG_00113; -.
DR GeneID; 77467881; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_0; -.
DR Proteomes; UP000004505; 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 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:UP000004505}.
FT DOMAIN 55..341
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 399..563
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 570 AA; 64363 MW; 7D8D93B96DC06D65 CRC64;
MKIDLLIKNV KVYNSYLKKF REANVAILDK KIFHVDIKKE VEFHAEKVID GKNQYMIPGL
IDIHMHIESS MMTPAPFCHQ LAKNGVTTIV AEPHEIANVF GDRGIYAMIE AENNIDTSIF
YGIPSSVPST SEELETTGAI IDCEGMKKIA ENPKVICVGE VMNYRKVIVD NTLEICKFIE
YVKKEKPTYA IEGHCPKLLD LELSKFLYLG INGDHTEHTM EEFKQRFENG MFVEIQAKSI
EKELIDYIKE NNLYEHFSFV TDDVMADTFL NEGHLNAVMK KAVKEGLRIE DAIYSATYTP
ARRMHLLDRG VLAPGKKADF LFVEDLENFE IKNTFIDGKE VYNSLEEKKY IPTSYKFPSD
FYKSVHVKNI KKEDLNIPVQ SREKEVMCRV IEVSDGSTRT KELIKPVPVK DGYLDWENSE
YCLIAVFERH GKNGNVGFGL VTGDSIKEGA IATTYAHDHH NLMVIGKNAE DIVAAANRII
EIQGGICAVK DGNILSEVRL PVAGILSEKS VEELGKEVEE LRNAMKTLGY KHYNPIMSFC
TLSLPVSPAL KITDKGLIDV TESKVVNLIV
//
