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Reviewed, UniProtKB/Swiss-Prot Q81DR5 (IOLA_BACCR)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methylmalonate semialdehyde dehydrogenase [acylating]
      Short name=MMSA dehydrogenase
      Short name=MMSDH
      Short name=MSDH
    EC=1.2.1.27
Alternative name(s):
    Malonate semialdehyde dehydrogenase [acetylating]
      Short name=MSA dehydrogenase
    EC=1.2.1.18
Gene names
Name: iolA
Ordered Locus Names: BC_2290
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Converts malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively By similarity.

Catalytic activity

3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. HAMAP MF_01670

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. HAMAP MF_01670

Pathway

Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7. HAMAP MF_01670

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family. IolA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Methylmalonate semialdehyde dehydrogenase [acylating] HAMAP MF_01670
PRO_0000352321

Regions

Nucleotide binding178 – 1825NAD By similarity

Sites

Active site2861Nucleophile By similarity
Binding site3861NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81DR5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 82FC20D727E4B83A

FASTA48652,954
        10         20         30         40         50         60 
MITTEIKRVK NHINGEWVES TGTEVEAVPN PATGKIIAYV PLSPKEDVEK AVEAAKAAFE 

        70         80         90        100        110        120 
TWSKVPVPNR SRNLYKYLQL LQENKDELAK IITLENGKTL TDATGEVQRG IEAVELATST 

       130        140        150        160        170        180 
PNLMMGQALP NIASGIDGSI WRYPIGVVAG ITPFNFPMMI PLWMFPLAIA CGNTFVLKTS 

       190        200        210        220        230        240 
ERTPLLAERL VELFYEAGFP KGVLNLVQGG KDVVNSILEN KDIQAVSFVG SEPVARYVYE 

       250        260        270        280        290        300 
TGTKHGKRVQ ALAGAKNHAI VMPDCNLEKT VQGVIGSAFA SSGERCMACS VVAVVDEIAD 

       310        320        330        340        350        360 
EFIDVLVAET KKLKVGDGFN EDNYVGPLIR ESHKERVLGY INSGVADGAT LLVDGRKINE 

       370        380        390        400        410        420 
EVGEGYFVGA TIFDGVNQEM KIWQDEIFAP VLSIVRVKDL EEGIKLTNQS KFANGAVIYT 

       430        440        450        460        470        480 
SNGKHAQTFR DNIDAGMIGV NVNVPAPMAF FAFAGNKASF FGDLSTNGTD GVQFYTRKKV 


VTERWF 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP09254.1.
RefSeqNP_832053.1.

3D structure databases

HSSPHSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBaseSearch...

Genome annotation databases

GeneID1204639.
GenomeReviewsGene locus BC_2290 in contig AE016877_GR.
KEGGbce:BC2290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ81DR5.
OMAQ81DR5. KVGPGNG.

Enzyme and pathway databases

BioCycBCER226900:BC_2290-MONOMER.

Family and domain databases

HAMAPMF_01670.
[Tree]
InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PTHR11699:SF27. MMSDH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLA_BACCR
AccessionPrimary (citable) accession number: Q81DR5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: June 1, 2003
Last modified: June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents