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
//