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Q96YK1

- MCR_SULTO

UniProt

Q96YK1 - MCR_SULTO

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Protein

Malonyl-CoA reductase

Gene

mcr

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)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.

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 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 – 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.
ModBaseiSearch...
MobiDBiSearch...

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

        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:
EMBL
GenBank
DDBJ
Links Updated
BA000023 Genomic DNA. Translation: BAB67276.1.
RefSeqiNP_378167.1. 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.

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: October 29, 2014
This is version 74 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