ID X7F5B0_9RHOB Unreviewed; 564 AA.
AC X7F5B0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=RISW2_14900 {ECO:0000313|EMBL:ETX27286.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27286.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX27286.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27286.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX27286.1}.
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DR EMBL; JAME01000036; ETX27286.1; -; Genomic_DNA.
DR RefSeq; WP_043774060.1; NZ_JAME01000036.1.
DR AlphaFoldDB; X7F5B0; -.
DR STRING; 1449351.RISW2_14900; -.
DR PATRIC; fig|1449351.3.peg.3850; -.
DR eggNOG; COG1001; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000023430; 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:UP000023430}.
FT DOMAIN 65..344
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 394..561
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 564 AA; 60144 MW; 444276BAABAFF93D CRC64;
MTDLASRIAA ARGDAPADLV LRGARVLDLV TGETFEGDVA ILGKTIVGTG HAYEGARVID
ATGLTLVPGF IDTHLHVESS LVTPLEFDRC VTPHGVTTAI CDPHEIANVI GAEGIRYFQR
ASEHTVMDLR VQLSSCVPST HMETAGAALD ADDLAALRGH PSGIGLAEFM NYPGVIHRDP
AALAKLALFE GGHVDGHCPL LSGRDLNAYC AAGIRTEHEA TSAAEAREKL MRGMRVLIRE
GSVSKDLEAL QPVLTERTAP YMCLCTDDRN PLDIAEEGHL DHMIRTLIAR GTPPLAAYRA
ASLSAAEAFG LRDRGLIAPG YRADIVALND VDSCDVAFVI AGGVVADDAA FAARGDLPPV
GRESVRAPRV AAADFRSTGN RQETDVIGVR EGRILTDHLH EDIAIEDGDK RPDPARDLMR
VAVIERHGRN GNIATGFVRG FGMQAGAIAS TLCHDHHNIV AVGADYDDMA VAANRLGEIE
GGFVVVRGGR VRAELALPVA GLMSLESFET VRDRLRDLRA AARDLGVTLH EPFLQLSFLA
LPVIPALKIT DRGMVDVTRF EIIG
//
