ID E0STV5_IGNAA Unreviewed; 613 AA.
AC E0STV5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 OrderedLocusNames=Igag_0905 {ECO:0000313|EMBL:ADM27721.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27721.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM27721.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(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, 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}.
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DR EMBL; CP002098; ADM27721.1; -; Genomic_DNA.
DR AlphaFoldDB; E0STV5; -.
DR STRING; 583356.Igag_0905; -.
DR KEGG; iag:Igag_0905; -.
DR HOGENOM; CLU_027935_0_0_2; -.
DR Proteomes; UP000001304; Chromosome.
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 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:ADM27721.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304}.
FT DOMAIN 82..371
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 434..602
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 613 AA; 67641 MW; AAF63E41FB56075B CRC64;
MGIGYRQLFR KSIDAIKRVI DVAFGRESAD LVLENATLVN VVTGEILDRV SIAIADRYIA
IVSEERVGGI RALNSVDLRG MYIVPGFIDA HVHIESSFLS PEEFSRVAEL HGTTLAVIDP
HELANIGGRR FLELLLEFIT GCGDRCIKLL VQIPSCVPPS KDSYVLDTPG SILSMDDIAI
LIEKGFHSLG EVMDFESIVN GDEDTLNRVI YSLDHGLRVY GHMPVNDIGA LNIYFSTGIS
SDHEISTYGE FVERVRRGVY AMVRGGGAWD DVSRIIPGIA KSGIDTRRLI LVTDDISVID
LVEKGYMDRV VREAIEYGLD PVRAIQAVTI NPAEYLRIDD YVGIIAPGRF ADMVILRDLR
SVDVFGVIRD GVMRVWNGDR VRDIDTRKID DSLAKQFRVM NVNPMASWRD LVISAPDNVS
RAIVRVIVIR PGETISRAEI AELPIYNGYI ASDPSRGILH IAVVDRYRAS RDIGKGFIKI
VPMARRGAIA QSYAHDTHNI VVIGSDPINM YIALNEVVRI GGGIAVVADE KPVAVLDLGI
GGVMSVKPLE TVYRFMKSIE NSVIELFSGA PPRDFLISLS LISLTVIPEV RLTTKGLVDV
SSRRVIDVVV RYM
//
