ID A0A0F4RHL1_9RHOB Unreviewed; 599 AA.
AC A0A0F4RHL1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=TW80_11840 {ECO:0000313|EMBL:KJZ19441.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ19441.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ19441.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ19441.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJZ19441.1}.
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DR EMBL; JXYE01000003; KJZ19441.1; -; Genomic_DNA.
DR RefSeq; WP_045997581.1; NZ_JXYE01000003.1.
DR AlphaFoldDB; A0A0F4RHL1; -.
DR STRING; 579483.TW80_11840; -.
DR PATRIC; fig|579483.3.peg.2424; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000033741; Unassembled WGS sequence.
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:UP000033741}.
FT DOMAIN 79..367
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 425..590
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 599 AA; 63418 MW; 7C6DDF1C91A33B51 CRC64;
MEHHIKSWAE VAPRLVAVAA GRAHADLVIR GGKLVNVQSR EILDGWQVAV ADGRFAYVGP
DTSHCIGPDT QVIEAEGRYL IPGLCDGHMH IESGMLTPAE FAAAVIPHGT TTMFTDPHEI
ANVLGLRGVR MMHDEALMQP VNIYTQMPSC APSAPGLETT GFKISADDVA EAMSWPGIIG
LGEMMNFPGV INGDPQMLAE MAATMNAGKT VGGHYASPDK GNAFAAYVAG GAADDHEGTA
EADAIARVRL GMKSMMRLGS AWYDVESQIT AITEKGLDPR NFILCTDDCH SGTLVNDGHM
NRVVRHAIDC GCDPLIALQM ATINTATHFG LERELGSIAP GRRADVILTS DLKTLPIEHV
IARGQTVAME GKITVDCPHY DWPADARQTV NMGKALGDAD FAISAPEGAN SVKVKVIGVV
ENQAPTEALT AELPVVDGLV EGEGDTYQIA LVERHQGTGK VVNGFVSGFG YTGKMAMAST
VAHDSHHMIV VGTDRENMAA AANRLGEVGG GVTVWKDGKE IALVELPIAG LMSDSPAAVV
AAKADEMVAA MQDCGCTLNN AYMQHSLLAL VVIPSLRISD LGLVDVEKFE LTELFEDDL
//
