ADEC_BACP2
ID ADEC_BACP2 Reviewed; 576 AA.
AC A8FCR4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=BPUM_1348;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR EMBL; CP000813; ABV62031.1; -; Genomic_DNA.
DR RefSeq; WP_012009817.1; NC_009848.4.
DR AlphaFoldDB; A8FCR4; -.
DR SMR; A8FCR4; -.
DR STRING; 315750.BPUM_1348; -.
DR EnsemblBacteria; ABV62031; ABV62031; BPUM_1348.
DR KEGG; bpu:BPUM_1348; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; TDHECFT; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000001355; Chromosome.
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; 2.30.40.10; -; 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; PTHR11113:SF2; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01178; ade; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..576
FT /note="Adenine deaminase"
FT /id="PRO_1000068608"
SQ SEQUENCE 576 AA; 62999 MW; 97E4AA8F69AC280C CRC64;
MDKELFRHQI EVAAKRKKAA LVIKHAKVMD VFNQEWIDAD VAVENGQIVG IGEYEGEQEL
DAVGQMLVPG FIDGHVHIES SMVTPAEFSK AVVPHGVTTV VTDPHEIANV SGITGIRFML
EEAKKAALHI YFMLPSCVPA VSFERSGATL KAKDLKPLYQ EKEVLGLAEV MDYVGVEQAE
EDMLQKLLDA QHENKLIDGH LAGLTDRLIN VYRTASVQTD HEVTTAQEAL ERVKRGMYVM
LREGSVAKNV KNVLPAVNEK NARRFFFCTD DKHLDDLMAQ GSIDEQVRMS IKEGLDPFLA
YQMGSLNAAE CFGLKTKGAI APGYDADFML VSDFHHVDIT SVFIAGELVA QNGEYKPSVE
KIAPSPALLQ SVHAIDVQEE DIALPITGDQ HMNVIRIIPN QLETKLEQVS PSEMNGQFTS
DTGRDVLKMV LVERHQGLSE MGVGIVSGFG IKQGAIATTV AHDSHNLIAV GTNDADIIKA
IEALKEAGGG LTVVKEGQSL HTLPLPISGL LSDQPAHLVN ESLHSLHEAL KETGFSLDFN
PFLTLSFLAL PVIPDVKMTT KGLFDVRNFQ HLPIQS