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Protein

5-methylthioadenosine/S-adenosylhomocysteine deaminase

Gene

mtaD

Organism
Bacillus cereus (strain B4264)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.UniRule annotation

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = S-inosyl-L-homocysteine + NH3.UniRule annotation
S-methyl-5'-thioadenosine + H2O = S-methyl-5'-thioinosine + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Zinc; via tele nitrogenUniRule annotation
Metal bindingi67 – 671Zinc; via tele nitrogenUniRule annotation
Binding sitei94 – 941SubstrateUniRule annotation
Binding sitei150 – 1501SubstrateUniRule annotation
Binding sitei189 – 1891SubstrateUniRule annotation
Metal bindingi216 – 2161Zinc; via tele nitrogenUniRule annotation
Binding sitei219 – 2191SubstrateUniRule annotation
Metal bindingi304 – 3041ZincUniRule annotation
Binding sitei304 – 3041SubstrateUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBCER405532:GI1K-1849-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5-methylthioadenosine/S-adenosylhomocysteine deaminaseUniRule annotation (EC:3.5.4.28UniRule annotation, EC:3.5.4.31UniRule annotation)
Short name:
MTA/SAH deaminaseUniRule annotation
Gene namesi
Name:mtaDUniRule annotation
Ordered Locus Names:BCB4264_A1866
OrganismiBacillus cereus (strain B4264)
Taxonomic identifieri405532 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000007096 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4354355-methylthioadenosine/S-adenosylhomocysteine deaminasePRO_1000140347Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7HIQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MTA/SAH deaminase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000250646.
KOiK12960.
OMAiVEYAASC.
OrthoDBiEOG65QWFB.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_01281. MTA_SAH_deamin.
InterProiIPR006680. Amidohydro-rel.
IPR023512. Deaminase_MtaD/DadD.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.

Sequencei

Sequence statusi: Complete.

B7HIQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTTYVNATI VTMNEQNEVI ENGYIIVEND QIIDVKSGKF ANDFEVDEVI
60 70 80 90 100
DMKGKWVLPG LVNTHTHVVM SLLRGIGDDM LLQPWLETRI WPLESQFTPQ
110 120 130 140 150
IAVASTELGL LEMVKSGTTS FSDMFNPIGV DQDAIMETVS RSGMRAAVSR
160 170 180 190 200
TLFSFGTKDD EKKAIEEAEK YVKRYYNESG MLTTMVAPHS PYTCSTELLE
210 220 230 240 250
ECARIAVENQ TMVHIHLSET EREVRDIEAQ YGKRPVEYAA SCGLFKRPTV
260 270 280 290 300
IAHGVVLNDD ERAFLAENDV RVAHNPNSNL KLGSGIANVK AMLEAGIKVG
310 320 330 340 350
IATDSVASNN NLDMFEEMRI ATLLQKGIHQ DATALPVETA LTLATKGAAE
360 370 380 390 400
VIGMKQTGSL EIGKCADFIT IDPSNKPHLQ PADEVLSHLV YAASGKDISD
410 420 430
VIINGKHVVW NGECKTLDEE RIIFEASRYK RGLQR
Length:435
Mass (Da):48,096
Last modified:February 10, 2009 - v1
Checksum:i1AAF873B4CA70678
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK60992.1.
RefSeqiWP_000859299.1. NC_011725.1.

Genome annotation databases

EnsemblBacteriaiACK60992; ACK60992; BCB4264_A1866.
KEGGibcb:BCB4264_A1866.
PATRICi18875665. VBIBacCer117876_1741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK60992.1.
RefSeqiWP_000859299.1. NC_011725.1.

3D structure databases

ProteinModelPortaliB7HIQ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK60992; ACK60992; BCB4264_A1866.
KEGGibcb:BCB4264_A1866.
PATRICi18875665. VBIBacCer117876_1741.

Phylogenomic databases

HOGENOMiHOG000250646.
KOiK12960.
OMAiVEYAASC.
OrthoDBiEOG65QWFB.

Enzyme and pathway databases

BioCyciBCER405532:GI1K-1849-MONOMER.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_01281. MTA_SAH_deamin.
InterProiIPR006680. Amidohydro-rel.
IPR023512. Deaminase_MtaD/DadD.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Bacillus cereus B4264."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B4264.

Entry informationi

Entry nameiMTAD_BACC4
AccessioniPrimary (citable) accession number: B7HIQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: November 11, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.