Skip Header

Contribute Send feedback
Read comments (?) or add your own

C3GJ47 (C3GJ47_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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonate semialdehyde dehydrogenase [acylating] 2 HAMAP MF_01670
Short name=MMSA dehydrogenase 2 HAMAP MF_01670
Short name=MMSDH 2 HAMAP MF_01670
Short name=MSDH 2 HAMAP MF_01670
EC=1.2.1.27 HAMAP MF_01670
Alternative name(s):
Malonate semialdehyde dehydrogenase [acetylating] 2 HAMAP MF_01670
Gene names
Name:iolA2 HAMAP MF_01670
ORF Names:bthur0010_22810 EMBL EEM77637.1
OrganismBacillus thuringiensis serovar pondicheriensis BGSC 4BA1 EMBL EEM77637.1
Taxonomic identifier527029 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length487 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
C3GJ47 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 4D650C3AE2198B74

FASTA48753,111
        10         20         30         40         50         60 
MTVQTAQIVK NYIGGEWVES ISTKMEAVYN PATGEVIAQV PLSTKVDVEQ AVLAANEAFK 

        70         80         90        100        110        120 
SWSKTAVPKR ARILFKYQQL LVDNWEELAK LITIENGKSY NEAYGEVLRG IECVEFAAGA 

       130        140        150        160        170        180 
PTLMMGKQLP DIATGIESGM YRYPIGVIGG ITPFNFPMMV PCWMFPLAIA CGNTFVLKPS 

       190        200        210        220        230        240 
ERTPLLAARL AELAEEAGLP KGVLNIVNGA HDVVNGLLEH KLVKAISFVG SQPVAEYVYK 

       250        260        270        280        290        300 
KGTENLKRVQ ALAGAKNHSI VLNDANLELA TKQIISAAFG SAGERCMAAS VVTVEEEIAD 

       310        320        330        340        350        360 
QLVERLVAEA NKIVIGNGLD EDVFLGPVIR DNHKERTIGY IDSGVEQGAT LVRDGREDTA 

       370        380        390        400        410        420 
VKGAGYFVGP TIFDHVTKEM KIWQDEIFAP VLSIVRVKSL DEAIEIANES RFANGACIYT 

       430        440        450        460        470        480 
DSGASVRQFR ETIESGMLGV NVGVPAPMAF FPFSGWKDSF YGDLHANGTD GVEFYTRKKM 


LTSRWEK

« Hide

References

[1]"Annotation of the Bacillus thuringiensis BGSC 4BA1 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 4BA1 EMBL EEM77637.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		ACNH01000048 Genomic DNA. Translation: EEM77637.1.

3D structure databases

ProteinModelPortalC3GJ47.
SMRC3GJ47. Positions 9-485.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000152996; EBBACP00000149684; EBBACG00000155122.
PATRIC28931165. VBIBacThu130330_3227.

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 nameC3GJ47_BACTU
AccessionPrimary (citable) accession number: C3GJ47
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)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info