Skip Header

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

Q65IX1 (IOLA1_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonate semialdehyde dehydrogenase [acylating] 1
Short name=MMSA dehydrogenase 1
Short name=MMSDH 1
Short name=MSDH 1
EC=1.2.1.27
Alternative name(s):
Malonate semialdehyde dehydrogenase [acetylating] 1
Short name=MSA dehydrogenase 1
EC=1.2.1.18
Gene names
Name:iolA1
Ordered Locus Names:BLi02104, BL00293
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length484 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-Rule MF_01670

Catalytic activity

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

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

Pathway

Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7. HAMAP-Rule 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 – 484484Methylmalonate semialdehyde dehydrogenase [acylating] 1 HAMAP-Rule MF_01670
PRO_0000352329

Regions

Nucleotide binding178 – 1825NAD By similarity

Sites

Active site2861Nucleophile By similarity
Binding site3841NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65IX1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: C82EA4B0C8E8C8CB

FASTA48452,593
        10         20         30         40         50         60 
MITTNAKKMM NHIDGEWVNS LGAESEEVVN PANGNVIAYA PLSVRADVDR AVQAAKHAYQ 

        70         80         90        100        110        120 
TWSLVPVPNR ARLLYKYLQL LQEQKEQLAD IITTENGKTL KDARGEVQRG IEVVELATAT 

       130        140        150        160        170        180 
PTLMMGESLP AIAGGIDGSI WRYPLGVVAG ITPFNFPMMV PLWMFPLAIA CGNTFVLKPS 

       190        200        210        220        230        240 
ERTPILAGKL VELFYEAGFP KGVLNLVHGG KDVVNGILEN DDIKAVSFVG SEPVAKYVYQ 

       250        260        270        280        290        300 
TGTANGKRVQ ALAGAKNHAI VMPDCHLEKT VQGIIGAAFG SSGERCMACS VAAVVDDIAD 

       310        320        330        340        350        360 
DFMEMLVSET RKLKTGDGRS EDHFVGPLIR EVHKQRVLDY IDSGIKEGAA LAVDGRNPDV 

       370        380        390        400        410        420 
REGYFVGATI FDHVTPEMKI WQDEIFAPVL SVVRVQDLDE GIELANQSKF ANGAVIYTSS 

       430        440        450        460        470        480 
GKSAQQFRDK IDAGMIGVNV NVPAPMAFFS FAGNKASFYG DLGTNGKDGV QFYTRKKVVT 


ERWF

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000002 Genomic DNA. Translation: AAU23628.1.
AE017333 Genomic DNA. Translation: AAU40993.1.
RefSeqYP_006713470.1. NC_006322.1.
YP_079266.1. NC_006270.3.

3D structure databases

HSSPHSSP built from PDB template 1T90 based on UniProtKB P42412.
ProteinModelPortalQ65IX1.
SMRQ65IX1. Positions 7-483.
ModBaseSearch...

Protein-protein interaction databases

STRING279010.BL00293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23628; AAU23628; BL00293.
AAU40993; AAU40993; BLi02104.
GeneID3031378.
3099477.
KEGGbld:BLi02104.
bli:BL00293.
PATRIC18949823. VBIBacLic203714_2115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271507.
KOK00140.
OMAVGHYIDG.
ProtClustDBCLSK873284.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-2086-MONOMER.
UniPathwayUPA00076; UER00148.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPMF_01670. IolA.
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]
PANTHERPTHR11699:SF27. PTHR11699:SF27. 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.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLA1_BACLD
AccessionPrimary (citable) accession number: Q65IX1
Secondary accession number(s): Q62UD1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 25, 2004
Last modified: May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents