ID A0A177H9U5_9RHOB Unreviewed; 599 AA.
AC A0A177H9U5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=adeC {ECO:0000313|EMBL:OAH06954.1};
GN Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=pfor_22c2490 {ECO:0000313|EMBL:OAH06954.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH06954.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH06954.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH06954.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) 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:OAH06954.1}.
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DR EMBL; LGRT01000023; OAH06954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H9U5; -.
DR STRING; 1689867.pfor_22c2490; -.
DR PATRIC; fig|1689867.3.peg.1963; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000077333; 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 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:OAH06954.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT DOMAIN 80..365
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 426..590
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 599 AA; 64065 MW; 8316B0DAEFA4AA55 CRC64;
MAKGEFASWA DCAADLVAVA AGRSSADLVV QNSRLVNVQS REVLENWQIA VVRGRFAYVG
PDARHCIGPK TQIIDAGRRY LIPGLCDGHM HIESGMLIPA EFAAAVIPYG TTTMFTDPHE
IANVLGLAGV RMMHDEALLQ PINIFTQMPS CAPSAPGLET TGFEITPQDV AEAMRWPGII
GLGEMMNYPG VIAGDEKMLA EMAATQAAGK VIGGHYASPD LGTPFHAYAA GGAADDHEGT
HEADAVLRAR MGMRAMLRLG SAWYDVERQI TAITERDLDP RNFILCTDDC HSETLVNEGH
MDRVVRHAID CGCEPLIALQ MATINTATHF GLERELGSIA PGRRADFILS SDLVSLPIEV
VFARGQKLAE HGQILTECPH YEWPEGAKNT VNLGKTMGAT DFEIAAAPNM AEAHVKVIGV
IENQAPTQAL SAKLPVIDGL VEANKGVCQI ALVERHHATG RISNGFVQGF AYQGEMAIAS
SVAHDSHHII VVGTNREMMA QAVNRLGEIG GGATIWQDGA EIGQVHLPIA GLMSDRPAAD
VATEVQTILS GMQRCGCALN NAFMQHSLLA LVVIPALRIS DLGLVDVDQF ALTDLFISE
//
