ID M7N401_9FLAO Unreviewed; 554 AA.
AC M7N401;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=D778_01450 {ECO:0000313|EMBL:EMQ96469.1};
OS Xanthomarina gelatinilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Xanthomarina.
OX NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ96469.1, ECO:0000313|Proteomes:UP000012024};
RN [1] {ECO:0000313|EMBL:EMQ96469.1, ECO:0000313|Proteomes:UP000012024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK20 {ECO:0000313|EMBL:EMQ96469.1,
RC ECO:0000313|Proteomes:UP000012024};
RA Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT "Genome assembly of Formosa sp. AK20.";
RL Submitted (DEC-2012) 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:EMQ96469.1}.
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DR EMBL; ANLA01000003; EMQ96469.1; -; Genomic_DNA.
DR RefSeq; WP_007646606.1; NZ_ANLA01000003.1.
DR STRING; 1137281.D778_01450; -.
DR PATRIC; fig|1137281.3.peg.86; -.
DR eggNOG; COG1001; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000012024; 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:UP000012024}.
SQ SEQUENCE 554 AA; 61033 MW; 335E0D2E696AE619 CRC64;
MILKGNIVDI PNQRVFKGEI TIKDGKIFSV EEKQHNVNHY ILPGFVDAHI HIESSMLVPS
EFARIAVKHG TIATVSDPHE IANVLGVEGV EFMINNGKET PFKFNFGAPS CVPATSFESA
GAVIDSEGIK TLMANPDIKY LAEMMNYPGV LFKDDEVLKK IAWAKHYNKP IDGHAPGLRG
DDLTKYIQAG ISTDHECFTF EEGLEKLQKG MKVLIREGSA AKNFEALIDL LPEHYENMMF
CSDDKHPDDL LLHHINNLCA RAVAKGMDVF KVLQVACVNP VKHYNLDVGL LNVGDFADCI
VVEDLKDFKT LQTYINGELV FDEDISKIDS VPFEILNNFQ TDKKDVSDFR YESSATLRLR
SGQAKIRVIE ALEGQLVTNE IIVESLLQDG NLVSNVEKDI LKMTVVNRYQ NQKPAIAFIK
NFGLKKGAIA SSVGHDSHNI IAVGVSDEAI CKAVNLLIET KGGICAVSDS ENLSADKAEK
VVALPVAGIM SDQDAKTIGK QYAELDKMAK QLGSTLHAPY MTLSFMALLV IPSLKLSDKG
LFDGNTFQFT NIEV
//
