ID E3FMZ4_STIAD Unreviewed; 831 AA.
AC E3FMZ4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN OrderedLocusNames=STAUR_5338 {ECO:0000313|EMBL:ADO73109.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO73109.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO73109.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO73109.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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; CP002271; ADO73109.1; -; Genomic_DNA.
DR RefSeq; WP_013376742.1; NZ_AAMD01000016.1.
DR AlphaFoldDB; E3FMZ4; -.
DR STRING; 378806.STAUR_5338; -.
DR KEGG; sur:STAUR_5338; -.
DR eggNOG; COG1051; Bacteria.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_341281_0_0_7; -.
DR OrthoDB; 21342at2; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProt.
DR CDD; cd02883; Nudix_Hydrolase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADO73109.1}.
FT DOMAIN 678..827
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 831 AA; 89185 MW; 7A66987EF1C09565 CRC64;
MTHPSGLGLA PGHRVKWIDG RIAVEADDDR SRLRAALERN LVAGDGGHTL ILGGQIRAHL
RPPAHVEPLT AFEARFLADN NVPLSLPTGT PAFSPRTDLH THFAGALPGR LLVELAAATE
GVTVPRGVLA EAGIDARQDV PAAALTALAR DRLARSLDVP LDQQITFQDM ERLYARRSPL
TKHPRLFVPQ LWAIARGFAA TGVHYAELSL STAVEPEILA ALHASLDSIE ADSGVRLRFL
VAMSRHDDLE WDLDVLDRLE QCLPSRAIAG VDIMGHETCS TRAFVPVLER AGALGRARPG
FVVRVHAGEN PAFPENVREA VRALLPFPGI EIRIGHGLYG VDGETLASMA RNSDRVIVEF
NLTSNLALNN IQTTLQVPLR RYVDAGVSAV LGSDGAGLYG TSAADEARAA LACGLDEPRL
AWLRHTEDLL LKRRQENERP QPALRDWLPP LPLPRRHFTP ARAAELAARR GSVRAAQEQR
LSQLGATVTN EAPVLTGRPL LWLAGAWRHA FAAWSPEEIR TTSGILTDVL RGLASRGGLL
LTGGTCHGME GLSHGLAAQV GVDVLGAIVE ETLAEDLDAR VQTFWRCARS LYEKAAPVVR
LVRDANGLGL FLGGGLIVAD EQQAAHNLRA RHVLLSGLRG AAVDAARASQ HVRFVDDAAS
ILAALDDTRP WGQLRYPGPN DAADVVLIRR GPLGDDELLL IRRHDDSDAA AGRMSLPGGF
VHPGEAPRDA AVRELLEETG LRMPASALSP VAIVEGGGRD PRDTEERWVR SHVFAVRMDG
EDATPHGASG NLVLGGSDAA AALFVSIAHR PRLAFDHDSL VTQALAVLSR G
//
