ID A0A0C5X296_9GAMM Unreviewed; 590 AA.
AC A0A0C5X296;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=H744_2c2812 {ECO:0000313|EMBL:AJR09465.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR09465.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR09465.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR09465.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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}.
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DR EMBL; CP005974; AJR09465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5X296; -.
DR STRING; 658445.H744_2c2812; -.
DR KEGG; pgb:H744_2c2812; -.
DR PATRIC; fig|658445.3.peg.4856; -.
DR HOGENOM; CLU_027935_0_0_6; -.
DR Proteomes; UP000032303; Chromosome 2.
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:UP000032303}.
FT DOMAIN 83..365
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 434..580
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 590 AA; 64105 MW; AC4A043B7319118C CRC64;
MMSNLKHKHT QQLGREQLQH LLTVLRGEKK AELKLTNLSV LDLVNGEVLP GPVVIDQGYI
AAVGPEAEVL QAKRSVDCNG QVAVPGFIDG HMHVETSTMT PFEFERTTLP LGTTSIVCDP
HELVNVMGKQ GIEWFLRCSE LMVQNMFVQI SSCVPAVADL DINGSDFTLK EMEAYLEHPH
VLGLAEVMDY PAVIGGNPAM LNKLAAFGEL NIDGHCPLLS GLELSAYRAS GIQNCHETTN
YQEGKEKLAK GMAVIIREGS VAKNLDALAP LITDYSSPLC LLCTDDRNPH EIAKEGHINY
MVKRLIQQHK IKPHLAYRVA SWSAARHFGL DRLGLIAPGY KADINLLTDL EQVDIQRVVI
GGQFVDELKL DELVSDKLDS SAPPLQATMR HNVVASDELA IPLTPGNYHV IEIIKDELLT
NLLVSYYNGR KFDQPGINRL AVVERYGHQL PPAVGLVKGF GLNRGAIATS VGHDSHNIVA
IGADEQSMAQ AINHLLAIGG GYCVVEDGTV TADLKLPLGG IMSLDSSEAI TSHIIALKVA
AKNIGVTVAE PFVQMSFLAL PVIPSLKMTV KGLVDVEKFQ LIELQVEAPL
//
