SubmitCancel

Skip Header

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

Q96YK1

- MCR_SULTO

UniProt

Q96YK1 - MCR_SULTO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Malonyl-CoA reductase
Gene
mcr, scr, STK_21710
Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed - 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

Divalent cations such as magnesium or manganese 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)

pH dependencei

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

Temperature dependencei

Optimum temperature is 85 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Acyl-thioester intermediate By similarity
Active sitei248 – 2481Proton acceptor By similarity

Regions

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

GO - Molecular functioni

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

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.

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: 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 reductase
PRO_0000418855Add
BLAST

Interactioni

Subunit structurei

Homodimer and possibly a tetramer.1 Publication

Protein-protein interaction databases

STRINGi273063.ST2171.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliQ96YK1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013358.
KOiK15017.
OMAiRISAACN.

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

MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE    50
VVRWQTVGQV PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA 100
KEGFPVISNS PDHRFDPDVP LLVPELNPHT ISLIDEQRKR REWKGFIVTT 150
PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ SLSGAGYPGI PSLDVVDNIL 200
PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH RIATIHGHYE 250
VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV 300
YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL 350
LVEKGYIEK 359
Length:359
Mass (Da):39,560
Last modified:December 1, 2001 - v1
Checksum:i426AAE51597DD0E8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BA000023 Genomic DNA. Translation: BAB67276.1 .
RefSeqi NP_378167.1. NC_003106.2.
WP_010980251.1. NC_003106.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DPK X-ray 2.05 A/B/C/D 1-359 [» ]
4DPL X-ray 1.90 A/B/C/D 1-359 [» ]
4DPM X-ray 2.30 A/B/C/D/E/F 1-359 [» ]
ProteinModelPortali Q96YK1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273063.ST2171.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB67276 ; BAB67276 ; STK_21710 .
GeneIDi 1460244.
KEGGi sto:ST2171.

Phylogenomic databases

eggNOGi COG0136.
HOGENOMi HOG000013358.
KOi K15017.
OMAi RISAACN.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13611.
STOK273063:GJC7-2380-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005676. 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 ]
Pfami PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view ]
PIRSFi PIRSF000148. ASA_dh. 1 hit.
SMARTi SM00859. Semialdhyde_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00978. asd_EA. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 72 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

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