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Database: UniProt
Entry: A0A0H3GSQ0_KLEPH
LinkDB: A0A0H3GSQ0_KLEPH
Original site: A0A0H3GSQ0_KLEPH 
ID   A0A0H3GSQ0_KLEPH        Unreviewed;       603 AA.
AC   A0A0H3GSQ0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   OrderedLocusNames=KPHS_36150 {ECO:0000313|EMBL:AEW62313.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW62313.1, ECO:0000313|Proteomes:UP000007841};
RN   [1] {ECO:0000313|EMBL:AEW62313.1, ECO:0000313|Proteomes:UP000007841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS11286 {ECO:0000313|EMBL:AEW62313.1,
RC   ECO:0000313|Proteomes:UP000007841};
RX   PubMed=22408243; DOI=10.1128/JB.00043-12;
RA   Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA   Ou H.Y.;
RT   "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT   HS11286, a multidrug-resistant strain isolated from human sputum.";
RL   J. Bacteriol. 194:1841-1842(2012).
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}.
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DR   EMBL; CP003200; AEW62313.1; -; Genomic_DNA.
DR   RefSeq; WP_014343336.1; NC_016845.1.
DR   RefSeq; YP_005227915.1; NC_016845.1.
DR   AlphaFoldDB; A0A0H3GSQ0; -.
DR   SMR; A0A0H3GSQ0; -.
DR   STRING; 1125630.KPHS_36150; -.
DR   GeneID; 11848646; -.
DR   KEGG; kpm:KPHS_36150; -.
DR   PATRIC; fig|1125630.4.peg.3522; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   Proteomes; UP000007841; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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   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:UP000007841}.
FT   DOMAIN          72..356
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          412..576
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   603 AA;  64334 MW;  19F6E3F00C323FA5 CRC64;
     MSSNAQVRRR AVQAARGESP FDLLLIDAQI VDMATGEIRP ADVGIVGEMI ASVHPRGSRE
     DAHEVRSLAG GYLSPGLMDT HVHLESSHLP PERYAEIVLT QGTTAVFWDP HELANVLGVA
     GVRYAVDASR HLPLQVMVAA PSSVPSTPGL EMSGADFAGA EMETMLGWPE VRGVAEVMDM
     HGVLHGSERM QEIVQAGLNS GKLIEGHARG LSGADLQAYL AAGVTSDHEL TSADDALEKL
     RAGLTIEIRG SHPYLLPGIV AALKTLPHLS SQITVCTDDV PPDILLEKGG IIALLNLLIE
     HGLPAVDALR FATLNAAIRL QRHDLGLIAA GRRADLVVFD SLEKLVAREV YVGGKLLARA
     GNLLTPIAPA AGVTPPRDTL QIAPLRADDF ILRVQGIRHG TARLRHIRGA RFTQWGEVEV
     QVRDGIVQLP AGFSLIWVKH RHGRHQATPQ IALLEGWGEL RGAIATSYSH DSHNLVVLGR
     DANDMALAAN QLIASGGGMA LAQQGEILAH VAMPIAGMLS DLPAAELARQ FRELRDLSSQ
     VADWEPPYRV FKAIEGTCLA CNAGPHLTDL GLTDGGSRQI VDPLIACRET PAPTPHNNNP
     QGA
//
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