ID D6YUS7_WADCW Unreviewed; 542 AA.
AC D6YUS7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=adeC {ECO:0000313|EMBL:ADI37888.1};
GN Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN OrderedLocusNames=wcw_0517 {ECO:0000313|EMBL:ADI37888.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37888.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI37888.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(2010).
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; CP001928; ADI37888.1; -; Genomic_DNA.
DR RefSeq; WP_013181614.1; NZ_LVEB01000020.1.
DR AlphaFoldDB; D6YUS7; -.
DR STRING; 716544.wcw_0517; -.
DR KEGG; wch:wcw_0517; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_0; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000001505; 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; 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, ECO:0000313|EMBL:ADI37888.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505}.
FT DOMAIN 43..320
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 371..535
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 542 AA; 58863 MW; E39BDB4332068541 CRC64;
MTNLSISGQI VDLFAKRIFP GEITLADGRI ASISEKEKAP DQYILPGFID AHIHIESSML
IPSEFARIAV LHGTVGTISD PHEIANVAGM EGIRFMLENG SKVPFHFHFG APSCVPATSF
ETAGASITAD DIHTLFEKDR LKYLSEMMNF PGVLHQDPEV MQKIAVAQSF GFPIDGHSPG
LKKDQAKAYI NAGISTDHEC FTLEEALGKI LYGMKILIRE GSAAKNFQAL HPLIKSHPDR
IMFCSDDKHP DELIEGHINL IVKRSIELGY DLMDVLRAAC IHPVEHYRMN VGLLRLNDSA
DFIVLEDLET FNVKSTFIQG IQVASEGKSL IDSVAVSPIN RFACSLKKEN AFKIAAKGEN
IHVIQAVQGE LVTGKLILPA CIEKGEYISD VDKDVLKLVV VNRYQDAPPA IAFVQGLGLK
SGALASSIAH DSHNIVAVGV DDQSLCRAIN AVIESKGGVA AANDQIECVP LPVAGLMSDK
DGWQVAADYA RIKKLSHSLG SKLHDPLMTL SFLALLVIPS LKLSDLGLFD AETFQFIPLE
AS
//
