ID A0A058ZP31_9RHOB Unreviewed; 564 AA.
AC A0A058ZP31;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ATO10_01295 {ECO:0000313|EMBL:KCV83354.1};
OS Actibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1461693 {ECO:0000313|EMBL:KCV83354.1, ECO:0000313|Proteomes:UP000024836};
RN [1] {ECO:0000313|EMBL:KCV83354.1, ECO:0000313|Proteomes:UP000024836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-Z10 {ECO:0000313|Proteomes:UP000024836};
RA Lai Q., Li G., Shao Z.;
RT "Shimia sp. 22II-S11-Z10 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:KCV83354.1}.
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DR EMBL; AQQY01000001; KCV83354.1; -; Genomic_DNA.
DR RefSeq; WP_035246998.1; NZ_AQQY01000001.1.
DR AlphaFoldDB; A0A058ZP31; -.
DR STRING; 1461693.ATO10_01295; -.
DR PATRIC; fig|1461693.3.peg.271; -.
DR eggNOG; COG1001; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000024836; 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:UP000024836}.
FT DOMAIN 65..343
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 394..561
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 564 AA; 59907 MW; 69C31A207891A961 CRC64;
MADLAAKIDQ AAGRVPADLV LRGGQVFDLV TGALIPGDVA ICGDTIVGIG AGYEGARVVD
VSGMTLVPGF IDTHLHVESS LVTPFEFDRC VGPRGVTTAI CDPHEIANVI GVPGIEYFLE
ASARTLMDIR VQLSSCVPST DMETAGAAIG ADELAALKDH PRSCGLAEFM NYPGVIYKDP
GVMAKLEAFE GRHIDGHAPL LGGRDLNAYV SAGIRTEHEA TSAEEAREKL QKGLRVLIRE
GSVSKDMLAL QPLLTDITAP YMCLCTDDRN PLDIAEHGHL DFMIRSLIAL GCSPLAVYRA
ASLSAAEAFG LKDRGQIAPG KRADIVVLPD LADCRAERVF CGGVEMTDAA FAARDLIDPI
GRHSVKAPTV QASDFRSIGN RDTRDVIGIL PGKIITEHLH EEIAVVDGDQ RPDVTRDLIK
IAVIERHGKN GNIATGFVKG FGLQRGAIAS TVCHDHHNIA VVGADYEDMA LAANRLGEIE
GGFVVVEGGK VLAELALPVA GLMSLNPFEQ VEADLRVLRD AALGLGVVLE EPFLQLAFLA
LPVIPALKIT DRGLVDVTKF EIIP
//
