ID G4D411_9FIRM Unreviewed; 563 AA.
AC G4D411;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:EGY79737.1};
GN ORFNames=HMPREF9129_1141 {ECO:0000313|EMBL:EGY79737.1};
OS Peptoniphilus indolicus ATCC 29427.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY79737.1, ECO:0000313|Proteomes:UP000003422};
RN [1] {ECO:0000313|EMBL:EGY79737.1, ECO:0000313|Proteomes:UP000003422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY79737.1,
RC ECO:0000313|Proteomes:UP000003422};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-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:EGY79737.1}.
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DR EMBL; AGBB01000111; EGY79737.1; -; Genomic_DNA.
DR RefSeq; WP_004821181.1; NZ_JH165061.1.
DR AlphaFoldDB; G4D411; -.
DR STRING; 997350.HMPREF9129_1141; -.
DR PATRIC; fig|997350.3.peg.1095; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000003422; 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000003422}.
FT DOMAIN 56..339
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 390..557
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 563 AA; 61801 MW; 22A4C4B12DF73DC8 CRC64;
MLKSDMKADL IIKDARVIDV FQNEIYKGNV AVKNGKIIGI GDYEDADEIV DAKGAYLSPT
MTDGHVHIES SMVSPAEFLK CLVARGVSTI IADPHEIANV CGLDGLEYII DETKDLPAHV
YVMLPSCVPC TPFETSGAIL KACDYKEMIN DPRVLGLGEM MDFVGTVNRA EDILEKIDLA
KNSNKVIDGH APLLSGKALD DYVLAGILTD HECSAVDEMK EKIRRGMYIQ LREGTAAKNL
EALIKGVTKD NISRCFFCTD DRHPEDLLKD GNVDNNVRKA IKLGMEPLDA IKMATLNPAQ
CYKMENSGAI APGYVADFFL FDDLNNINAK AVFIGGKKVA EDGKVIVDFS PKLSPKVLSK
MKIKDFKLED LKLKLNSNRV HVIEMEKESL LTKKVVCDVD VKDGYFEYSD DGIRKIVVIE
RHTGNSTIAI GLIKGYDIKN AAVGTTIAHD SHNLVVIGDN DEDMLNVIKR IDEMSGGMAI
SSNGKLEGSL RLDIAGIMSS KSMTEVHEDI KKLLKKAKEL GVGDGIDPFM TLGFMALPVI
PDIKMTDKGL FDVNEFKHIP LEV
//
