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C3F1F4 (C3F1F4_BACTU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methylmalonate semialdehyde dehydrogenase [acylating] 1 HAMAP MF_01670
Short name=MMSA dehydrogenase 1 HAMAP MF_01670
Short name=MMSDH 1 HAMAP MF_01670
Short name=MSDH 1 HAMAP MF_01670
EC=1.2.1.27 HAMAP MF_01670
Alternative name(s):
Malonate semialdehyde dehydrogenase [acetylating] 1 HAMAP MF_01670
Gene names
Name:iolA1 HAMAP MF_01670
ORF Names:bthur0007_21120 EMBL EEM59987.1
OrganismBacillus thuringiensis serovar monterrey BGSC 4AJ1 EMBL EEM59987.1
Taxonomic identifier527022 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
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. HAMAP MF_01670

Catalytic activity

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

3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. 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. RuleBase RU003345

Belongs to the aldehyde dehydrogenase family. IolA subfamily. HAMAP MF_01670

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding178 – 1825NAD By similarity HAMAP MF_01670

Sites

Active site2861Nucleophile By similarity HAMAP MF_01670
Binding site3861NAD By similarity HAMAP MF_01670

Sequences

Sequence LengthMass (Da)Tools
C3F1F4 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 37F24E5E70BE30D2

FASTA48653,005
        10         20         30         40         50         60 
MITTEIKRVK NHINGEWVES TGTEVEAVPN PATGKIIAYV PLSPKEDVEK AVEAAKAAYE 

        70         80         90        100        110        120 
TWSKVPVPNR SRQLYKYLQL LQENKEELAK 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 KKLKVGDGFH EDNYVGPLIR ESHKERVLGY INSGVADGAT LLVDGRKIKE 

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

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


VTERWF

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References

[1]"Annotation of the Bacillus thuringiensis BGSC 4AJ1 genome."
Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BGSC 4AJ1 EMBL EEM59987.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		ACNE01000047 Genomic DNA. Translation: EEM59987.1.

3D structure databases

ProteinModelPortalC3F1F4.
SMRC3F1F4. Positions 5-485.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000394523; EBBACP00000389577; EBBACG00000398895.
PATRIC28904513. VBIBacThu130558_4833.

Family and domain databases

HAMAPMF_01670. IolA.
[Tree]
InterProIPR016161. 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]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699:SF27. MMSDH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR01722. MMSDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC3F1F4_BACTU
AccessionPrimary (citable) accession number: C3F1F4
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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