Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malonyl-CoA reductase

Gene

mcr

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations such as Mg(2+) and Mn2+ ions at 5 mM.1 Publication

Enzyme regulationi

Activated by dithioerythritol (5 mM) and inhibited by the thiol-blocking agent iodoacetamide (0.1 mM).1 Publication

Kineticsi

  1. KM=25 µM for NADP (with 0.2 mM malonyl-CoA)1 Publication
  2. KM=40 µM for malonyl-CoA (with 0.5 mM NADP)1 Publication

pH dependencei

Optimum pH is 7.2, with half-maximal activities at pH 6 and 8.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Acyl-thioester intermediateBy similarity
Active sitei248 – 2481Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 194NADPBy similarity
Nucleotide bindingi183 – 1842NADPBy similarity
Nucleotide bindingi335 – 3362NADPBy similarity

GO - Molecular functioni

  1. aspartate-semialdehyde dehydrogenase activity Source: InterPro
  2. N-acetyl-gamma-glutamyl-phosphate reductase activity Source: InterPro
  3. NAD binding Source: InterPro
  4. NADP binding Source: InterPro
  5. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. aspartate metabolic process Source: InterPro
  2. isoleucine biosynthetic process Source: InterPro
  3. lysine biosynthetic process via diaminopimelate Source: InterPro
  4. methionine biosynthetic process Source: InterPro
  5. threonine biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP, RNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13611.
STOK273063:GJC7-2380-MONOMER.
BRENDAi1.2.1.75. 6166.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA reductase (EC:1.2.1.75)
Gene namesi
Name:mcr
Synonyms:scr
Ordered Locus Names:STK_21710
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001015 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Malonyl-CoA reductasePRO_0000418855Add
BLAST

Interactioni

Subunit structurei

Homodimer and possibly a tetramer.1 Publication

Protein-protein interaction databases

STRINGi273063.ST2171.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Turni13 – 164Combined sources
Helixi20 – 289Combined sources
Beta strandi31 – 4111Combined sources
Turni42 – 454Combined sources
Helixi48 – 514Combined sources
Beta strandi56 – 583Combined sources
Helixi62 – 654Combined sources
Helixi74 – 763Combined sources
Beta strandi82 – 854Combined sources
Turni89 – 913Combined sources
Helixi92 – 10110Combined sources
Beta strandi105 – 1084Combined sources
Turni112 – 1154Combined sources
Turni124 – 1263Combined sources
Helixi128 – 1325Combined sources
Helixi133 – 1419Combined sources
Beta strandi144 – 1496Combined sources
Helixi153 – 16816Combined sources
Beta strandi171 – 18010Combined sources
Helixi182 – 1854Combined sources
Helixi192 – 1954Combined sources
Helixi204 – 21815Combined sources
Helixi230 – 2323Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi248 – 25811Combined sources
Helixi262 – 2709Combined sources
Helixi275 – 2784Combined sources
Beta strandi288 – 2925Combined sources
Helixi300 – 3034Combined sources
Turni307 – 3115Combined sources
Beta strandi313 – 32311Combined sources
Beta strandi326 – 3338Combined sources
Turni335 – 3406Combined sources
Helixi341 – 35313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013358.
KOiK15017.
OMAiIKPAYLA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005676. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00978. asd_EA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96YK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE
60 70 80 90 100
VVRWQTVGQV PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA
110 120 130 140 150
KEGFPVISNS PDHRFDPDVP LLVPELNPHT ISLIDEQRKR REWKGFIVTT
160 170 180 190 200
PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ SLSGAGYPGI PSLDVVDNIL
210 220 230 240 250
PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH RIATIHGHYE
260 270 280 290 300
VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV
310 320 330 340 350
YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL

LVEKGYIEK
Length:359
Mass (Da):39,560
Last modified:December 1, 2001 - v1
Checksum:i426AAE51597DD0E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB67276.1.
RefSeqiNP_378167.1. NC_003106.2.
WP_010980251.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
GeneIDi1460244.
KEGGisto:ST2171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB67276.1.
RefSeqiNP_378167.1. NC_003106.2.
WP_010980251.1. NC_003106.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273063.ST2171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
GeneIDi1460244.
KEGGisto:ST2171.

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013358.
KOiK15017.
OMAiIKPAYLA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13611.
STOK273063:GJC7-2380-MONOMER.
BRENDAi1.2.1.75. 6166.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005676. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00978. asd_EA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiMCR_SULTO
AccessioniPrimary (citable) accession number: Q96YK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This enzyme contains bound RNA, but the physiological role is not known.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.