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Database: UniProt
Entry: A0A084A0L6_9GAMM
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ID   A0A084A0L6_9GAMM        Unreviewed;       582 AA.
AC   A0A084A0L6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:KEY58845.1};
GN   ORFNames=SRDD_22350 {ECO:0000313|EMBL:KEY58845.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY58845.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY58845.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY58845.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(2014).
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   -!- SUBUNIT: Homodimer. {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:KEY58845.1}.
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DR   EMBL; AYKS02000063; KEY58845.1; -; Genomic_DNA.
DR   RefSeq; WP_023491735.1; NZ_AYKS02000063.1.
DR   AlphaFoldDB; A0A084A0L6; -.
DR   STRING; 1410619.SRDD_22350; -.
DR   eggNOG; COG1001; Bacteria.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000017810; 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:UP000017810}.
FT   DOMAIN          77..359
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          431..575
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   582 AA;  63540 MW;  AFD0D44C5EB63F94 CRC64;
     MAKQTQSLTR EQTGRLLAVS RGEAVADMMI ENVRILDLIN GGEIAGPIVI SGNTIAGIGP
     AYQGAAALQR IDAHNAIAVP GFIDAHLHIE SSMMTPVTFE SATLPLGVTT IVCDPHEIIN
     VMGQAGLAWF LRSAEQARQN QFIQISSCVP ALAGCDVNGA EFPVEQMQAY HDHPHVLGLA
     EMMDYPGVIA GNSAILDKLD TFRDLTLDGH CPLLTGKDLN GYIAAGIENC HETLLRAEGR
     EKLSLGMALM IREGSVARNL DTLAPLINEF NSPQCMLCTD DRNPWEITHE GHINSLIHRL
     INQHHIPAHV AYRVASWSAA RHFGLKRLGL LAPGKQADIV LLDDLNQVSI RQVIIRGERL
     NNEELQSTRQ QRQQLTQPPL QNTIDRQPVT AAALTLPLTT GHRYRVIQVV PNELITHQQQ
     AEWLGDRFSL PDICRIAVLE RYGKNHPPAL GLLQGFELQQ GALAASVSHD SHNLVVIGHR
     PEEMALAINQ LIEYGGGLCV VNNHQVQSHL ALPIAGLMSD LSTTEIAQSI TELKAACLAC
     GIKLNEPFIQ MAFLSLPVIP ALKLTSMGLF DVTQFRFVET PL
//
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