Q81QB6 (IOLA2_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methylmalonate semialdehyde dehydrogenase [acylating] 2 Short name=MMSA dehydrogenase 2 Short name=MMSDH 2 Short name=MSDH 2 EC=1.2.1.27 Alternative name(s): Malonate semialdehyde dehydrogenase [acetylating] 2 Short name=MSA dehydrogenase 2 EC=1.2.1.18 | ||||
| Gene names |
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| Organism | Bacillus anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 487 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Converts malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively By similarity. HAMAP MF_01670 |
| 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. HAMAP MF_01670 |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. IolA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Molecular function | malonate-semialdehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC methylmalonate-semialdehyde dehydrogenase (acylating) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 487 | 487 | Methylmalonate semialdehyde dehydrogenase [acylating] 2 HAMAP MF_01670 | PRO_0000352319 | |||||
Regions | |||||||||
| Nucleotide binding | 178 – 182 | 5 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 286 | 1 | Nucleophile By similarity | ||||||
| Binding site | 386 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
| [3] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP26371.1. AE017334 Genomic DNA. Translation: AAT31624.1. AE017225 Genomic DNA. Translation: AAT54646.1. |
| RefSeq | NP_844885.1. NC_003997.3. YP_019149.1. NC_007530.2. YP_028595.1. NC_005945.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1T90 based on UniProtKB P42412. |
| ProteinModelPortal | Q81QB6. |
| SMR | Q81QB6. Positions 9-485. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q81QB6. 7 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000011908; EBBACP00000011664; EBBACG00000011900. EBBACT00000018097; EBBACP00000017718; EBBACG00000018088. EBBACT00000020071; EBBACP00000019556; EBBACG00000020062. |
| GeneID | 1084066. 2815765. 2852503. |
| GenomeReviews | Gene locus BA_2513 in contig AE016879_GR. Gene locus BAS2334 in contig AE017225_GR. Gene locus GBAA_2513 in contig AE017334_GR. |
| KEGG | ban:BA_2513. bar:GBAA_2513. bat:BAS2334. |
| TIGR | BA_2513. GBAA_2513. |
Phylogenomic databases | |
| GeneTree | EBGT00070000031871. |
| HOGENOM | HBG752218. |
| OMA | YAEGTRR. |
| ProtClustDB | CLSK2485196. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS2334-MONOMER. BANT261594:GBAA2513-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01670. IolA. [Tree] |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR010061. MeMal-semiAld_DH. IPR023510. MeMal-semiAld_DH_GmP_bac. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| KO | K00140. |
| PANTHER | PTHR11699:SF27. MMSDH. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR01722. MMSDH. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IOLA2_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81QB6 Secondary accession number(s): Q6HYJ3, Q6KSJ4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with