ID A0A136KZE0_9CHLR Unreviewed; 596 AA.
AC A0A136KZE0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KXK14815.1};
GN ORFNames=UZ14_CFX002000992 {ECO:0000313|EMBL:KXK14815.1};
OS Chloroflexi bacterium OLB14.
OC Bacteria; Chloroflexota; Tepidiformia.
OX NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK14815.1, ECO:0000313|Proteomes:UP000070321};
RN [1] {ECO:0000313|EMBL:KXK14815.1, ECO:0000313|Proteomes:UP000070321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB14 {ECO:0000313|EMBL:KXK14815.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK14815.1}.
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DR EMBL; LMZR01000020; KXK14815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KZE0; -.
DR STRING; 1617415.UZ14_CFX002000992; -.
DR PATRIC; fig|1617415.3.peg.1003; -.
DR Proteomes; UP000070321; 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, ECO:0000313|EMBL:KXK14815.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 75..362
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 422..588
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 596 AA; 64603 MW; C8A35540A9297031 CRC64;
MTSSTKLTKS LIDVAMGREP ADLVIKNGKW VSVQSGEIIP NTDIAIINER IAFVGRDASH
TIGKKTRVID ANGKYLVPGL LDGHMHVESG MVTVTEFVRA VAVRGTTGMF IDPHEIANVF
GLKGVKLMVD EALKQPIHVW VQMPSCVPSA PGLETPGSSI GPKEVEQAMK WKGIIGLGEM
MNFPGVFMSD KKMLDEMSAT HAAGKTIGGH YASPDLGIPF HGYVAGGAED DHEGTRMDDA
IARVRQGMKA MLRYGSAWFD VAAQVKAITE KRLDSRHFIL CTDDSHAATL TDEGHMDRVL
RHAVSEGLNP MTAIQMMTIN TAEHFGVSKE MGMIAPGRYA DILLVNDLMN FKAETVIAKG
VVIAENNEWQ IKLPVVKYPK WVTNSVKVKR KFVSQDFVLR SRASNGSEIE AHVIGVIENQ
APTRHLKMKV TVEENQVKSD IKNDLAKIAL VERHKGTGKV VVGLTSGFGF TRKCAIASTV
AHDSHHMLVV GTDDECMALA ANELAKCGGG QVVVLNGKVI GLVELQIAGL MSNEHADVVA
KKTATVLDGF KMCGSELNNP NMQLSLLALV VIPELRISDK GLVDVTKFDF IDVLDD
//
