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Q96YK1 (MCR_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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

Names and origin

Protein namesRecommended name:
Malonyl-CoA reductase

EC=1.2.1.75
Gene names
Name:mcr
Synonyms:scr
Ordered Locus Names:STK_21710
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Ref.2

Catalytic activity

Malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH. Ref.2

Cofactor

Divalent cations such as magnesium or manganese ions at 5 mM. Ref.2

Enzyme regulation

Activated by dithioerythritol (5 mM) and inhibited by the thiol-blocking agent iodoacetamide (0.1 mM). Ref.2

Subunit structure

Homodimer and possibly a tetramer. Ref.2

Miscellaneous

This enzyme contains bound RNA, but the physiological role is not known (Ref.2).

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for NADP (with 0.2 mM malonyl-CoA) Ref.2

KM=40 µM for malonyl-CoA (with 0.5 mM NADP)

pH dependence:

Optimum pH is 7.2, with half-maximal activities at pH 6 and 8.

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Malonyl-CoA reductase
PRO_0000418855

Regions

Nucleotide binding16 – 194NADP By similarity
Nucleotide binding183 – 1842NADP By similarity
Nucleotide binding335 – 3362NADP By similarity

Sites

Active site1531Acyl-thioester intermediate By similarity
Active site2481Proton acceptor By similarity

Secondary structure

.................................................................. 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96YK1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 426AAE51597DD0E8

FASTA35939,560
        10         20         30         40         50         60 
MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE VVRWQTVGQV 

        70         80         90        100        110        120 
PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA KEGFPVISNS PDHRFDPDVP 

       130        140        150        160        170        180 
LLVPELNPHT ISLIDEQRKR REWKGFIVTT PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ 

       190        200        210        220        230        240 
SLSGAGYPGI PSLDVVDNIL PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH 

       250        260        270        280        290        300 
RIATIHGHYE VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV 

       310        320        330        340        350 
YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL LVEKGYIEK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7."
Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.
DNA Res. 8:123-140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
[2]"Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp."
Alber B., Olinger M., Rieder A., Kockelkorn D., Jobst B., Hugler M., Fuchs G.
J. Bacteriol. 188:8551-8559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A MALONYL COA REDUCTASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, RNA BINDING, NOMENCLATURE, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAB67276.1.
RefSeqNP_378167.1. NC_003106.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DPKX-ray2.05A/B/C/D1-359[»]
4DPLX-ray1.90A/B/C/D1-359[»]
4DPMX-ray2.30A/B/C/D/E/F1-359[»]
ProteinModelPortalQ96YK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273063.ST2171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB67276; BAB67276; STK_21710.
GeneID1460244.
KEGGsto:ST2171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHOG000013358.
KOK15017.
OMARISAACN.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13611.
STOK273063:GJC7-2380-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005676. Asp_semi-ald_DH_pep-lack.
IPR012080. Asp_semialdehyde_DH.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
PfamPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFPIRSF000148. ASA_dh. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00978. asd_EA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCR_SULTO
AccessionPrimary (citable) accession number: Q96YK1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references