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Database: UniProt
Entry: H3KFM2_9BURK
LinkDB: H3KFM2_9BURK
Original site: H3KFM2_9BURK 
ID   H3KFM2_9BURK            Unreviewed;       606 AA.
AC   H3KFM2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-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   ORFNames=HMPREF9440_01541 {ECO:0000313|EMBL:EHY31089.1};
OS   Sutterella parvirubra YIT 11816.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31089.1, ECO:0000313|Proteomes:UP000004956};
RN   [1] {ECO:0000313|EMBL:EHY31089.1, ECO:0000313|Proteomes:UP000004956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31089.1,
RC   ECO:0000313|Proteomes:UP000004956};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-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:EHY31089.1}.
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DR   EMBL; AFBQ01000227; EHY31089.1; -; Genomic_DNA.
DR   RefSeq; WP_008542559.1; NZ_JH604981.1.
DR   AlphaFoldDB; H3KFM2; -.
DR   STRING; 762967.HMPREF9440_01541; -.
DR   PATRIC; fig|762967.3.peg.1213; -.
DR   HOGENOM; CLU_027935_0_0_4; -.
DR   OrthoDB; 9782972at2; -.
DR   Proteomes; UP000004956; 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:UP000004956}.
FT   DOMAIN          89..371
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          423..594
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   606 AA;  63688 MW;  FC75953EDB76B21A CRC64;
     MSASSHSNAS SPVTVTLTPA NFDALRRRID ASNLAVPADT RFTGGVVADV YTGEFVKGVD
     VLVKDGLVAA VVPEGIGEAR ETVDLQGKTL LPAFIDAHVH IESAMLVPER FAELVVPHGT
     GAVVADPHEI ANVLGTVGLD FMLEASEGLP LDIRFQLPSC VPATPFEHAG AVLDAAALEP
     YWEKKRVLGL GEVMNIPGVL GHDSDLAAKL LHAQKRSRPI DGHAPGILHE ARSATAAAGI
     TTDHESSSLE EMRESLARGM KVIIREGSAA KNLRTLIQGV TPRNSRRCMF CSDDVNPADV
     ERLGHMEKHL RMAVEAGVDP MTAVQMATLN AAEHFGLPGG AIAPGKPADF AVVEDVTTFR
     VAETWHRGEL VAKDGKLTKP IRTPIQPEAV LSRVKLQPVG LETFRLPVPS GEANVIGIVP
     HEIVTKAEVR TVKTDAEGNF DAQLNPGLVK LAVLERHHAL GTVGLGILSG YVAAGALMEG
     AVATTIAHDS HNIVCAGGSD ADMLAAVRAL EALGGGMVVV KRGEVVASLA LPAGGLMSFE
     PADAVARGVA AVHRAAEEAF RLGEGLEPVM TLAFLALPVI PELRLTDLGL FDVRAWTHVG
     TDRGAK
//
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