Skip Header

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

Q8EMV4 (IOLA2_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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] 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
Name:iolA2
Ordered Locus Names:OB2736
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Oceanobacillus

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Methylmalonate semialdehyde dehydrogenase [acylating] 2 HAMAP MF_01670
PRO_0000352349

Regions

Nucleotide binding178 – 1825NAD By similarity

Sites

Active site2861Nucleophile By similarity
Binding site3861NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EMV4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9C50FC90021C4E4A

FASTA48653,503
        10         20         30         40         50         60 
MTQTTVKNVK NYIGGEWIES RTEKTEDVFN PATGEVIAQV PISTTEDVHH AIEVANEAFK 

        70         80         90        100        110        120 
TWKEVPVPKR ARILFKYQQL LVEHWEELAK LITLENGKNY AEAYGEVQRG IENVEFATGA 

       130        140        150        160        170        180 
PSLMMGEQLA SIATELESGV YRYPIGVIGG ITPFNFPMMV PCWMFPMAIA TGNTFVMKPS 

       190        200        210        220        230        240 
ERTPLLANRL AELLEEAGLP NGVFNIVHGA HDVVNGLLDH KKVAAISFVG SQPVAEYVYK 

       250        260        270        280        290        300 
RGTQNLKRVQ ALAGAKNHSI VLSDANLENA TTQILNAAFG SAGERCMAAS VVAVEEDVAD 

       310        320        330        340        350        360 
EFVTLLTQKA NEIKIGNGLD EGVFLGPVIR DQHKERTLQY IESGEEEGAN LVRDGRTDEA 

       370        380        390        400        410        420 
AKQEGYFVGP TIFDHVTSEM KIWQDEIFAP VLSIARVNNL EEGVDLANES RFANGACIFT 

       430        440        450        460        470        480 
RDGGSVRRFR ETIDAGMLGV NIGVPAPMAF LPFSGWKDSF YGDLHANGKD GLQFYTRKKV 


LTTKWV

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000028 Genomic DNA. Translation: BAC14692.1.
RefSeqNP_693658.1. NC_004193.1.

3D structure databases

HSSPHSSP built from PDB template 1T90 based on UniProtKB P42412.
ProteinModelPortalQ8EMV4.
SMRQ8EMV4. Positions 6-485.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1016156.
GenomeReviewsGene locus OB2736 in contig BA000028_GR.
KEGGoih:OB2736.
NMPDRfig|221109.1.peg.2736.
PATRIC22796540. VBIOceIhe82024_2774.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG752218.
OMAYAEGTRR.

Enzyme and pathway databases

BioCycOIHE221109:OB2736-MONOMER.

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.
KOK00140.
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.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLA2_OCEIH
AccessionPrimary (citable) accession number: Q8EMV4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 62 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