ID A8MEB7_ALKOO Unreviewed; 154 AA.
AC A8MEB7;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=tRNA-specific adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_00972};
DE EC=3.5.4.33 {ECO:0000256|HAMAP-Rule:MF_00972};
GN Name=tadA {ECO:0000256|HAMAP-Rule:MF_00972};
GN OrderedLocusNames=Clos_0018 {ECO:0000313|EMBL:ABW17588.1};
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW17588.1, ECO:0000313|Proteomes:UP000000269};
RN [1] {ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the
CC wobble position 34 of tRNA(Arg2). {ECO:0000256|HAMAP-Rule:MF_00972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000256|ARBA:ARBA00001103, ECO:0000256|HAMAP-
CC Rule:MF_00972};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00972};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00972};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00972}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000256|ARBA:ARBA00010669}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000853; ABW17588.1; -; Genomic_DNA.
DR RefSeq; WP_012157903.1; NC_009922.1.
DR AlphaFoldDB; A8MEB7; -.
DR STRING; 350688.Clos_0018; -.
DR KEGG; aoe:Clos_0018; -.
DR eggNOG; COG0590; Bacteria.
DR HOGENOM; CLU_025810_3_2_9; -.
DR OrthoDB; 9802676at2; -.
DR Proteomes; UP000000269; Chromosome.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:UniProtKB-UniRule.
DR CDD; cd01285; nucleoside_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR PANTHER; PTHR11079:SF179; CYTOSINE DEAMINASE; 1.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00972};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00972}; Reference proteome {ECO:0000313|Proteomes:UP000000269};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00972};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00972}.
FT DOMAIN 2..113
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
SQ SEQUENCE 154 AA; 17187 MW; 990F9A21C1BE4E73 CRC64;
MVLEENFMLE AIEEAKKAFN KKEVPIGAVV VKDNEIIGRG HNLRETTKNS ISHAEIMAIQ
EACKFLGGWR LTDCTLYVTI EPCPMCAGAI LQSRIQKVVI GAMDPKAGAC GSLVNLLNDS
RFNHQTEIEQ GVLEEECSLL MKEFFKALRE KRFG
//
