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Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene

mvaA

Organism
Pseudomonas mevalonii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.

Catalytic activityi

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH.

Pathwayi: (R)-mevalonate degradation

This protein is involved in step 1 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate.
Proteins known to be involved in this subpathway in this organism are:
  1. 3-hydroxy-3-methylglutaryl-coenzyme A reductase (mvaA)
This subpathway is part of the pathway (R)-mevalonate degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate, the pathway (R)-mevalonate degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei83Charge relay system1
Active sitei267Charge relay system1
Active sitei283Charge relay system1
Active sitei381Proton donorPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11829.
BRENDAi1.1.1.88. 5143.
SABIO-RKP13702.
UniPathwayiUPA00257; UER00367.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC:1.1.1.88)
Short name:
HMG-CoA reductase
Gene namesi
Name:mvaA
OrganismiPseudomonas mevalonii
Taxonomic identifieri32044 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52E → Q: No loss of activity. 1 Publication1
Mutagenesisi83E → Q: Greatly reduced activity. 1 Publication1
Mutagenesisi183D → A or N: Reduced activity. 1 Publication1
Mutagenesisi381H → A, N, Q or K: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001144671 – 4283-hydroxy-3-methylglutaryl-coenzyme A reductaseAdd BLAST428

Expressioni

Inductioni

Coinduction with mevalonate transport system.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Helixi15 – 26Combined sources12
Helixi30 – 37Combined sources8
Helixi44 – 50Combined sources7
Beta strandi51 – 65Combined sources15
Beta strandi77 – 80Combined sources4
Beta strandi82 – 85Combined sources4
Helixi86 – 98Combined sources13
Turni99 – 101Combined sources3
Beta strandi103 – 107Combined sources5
Beta strandi111 – 120Combined sources10
Helixi124 – 133Combined sources10
Helixi135 – 144Combined sources10
Helixi147 – 151Combined sources5
Beta strandi155 – 164Combined sources10
Beta strandi172 – 180Combined sources9
Helixi187 – 205Combined sources19
Beta strandi208 – 214Combined sources7
Beta strandi221 – 229Combined sources9
Helixi231 – 234Combined sources4
Beta strandi237 – 239Combined sources3
Helixi241 – 257Combined sources17
Helixi259 – 279Combined sources21
Helixi284 – 295Combined sources12
Turni296 – 298Combined sources3
Beta strandi304 – 309Combined sources6
Beta strandi315 – 322Combined sources8
Beta strandi327 – 329Combined sources3
Turni330 – 334Combined sources5
Helixi336 – 345Combined sources10
Helixi350 – 374Combined sources25
Helixi378 – 393Combined sources16
Turni398 – 400Combined sources3
Helixi405 – 408Combined sources4
Turni409 – 411Combined sources3
Helixi415 – 420Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QAXX-ray2.80A/B1-428[»]
1QAYX-ray2.80A/B1-428[»]
1R31X-ray2.10A/B1-428[»]
1R7IX-ray2.21A/B1-428[»]
1T02X-ray2.60A/B1-428[»]
4I4BX-ray1.70A/B1-428[»]
4I56X-ray1.50A/B1-428[»]
4I64X-ray1.75A/B1-428[»]
4I6AX-ray1.85A/B1-428[»]
4I6WX-ray1.66A/B1-428[»]
4I6YX-ray1.45A/B1-428[»]
ProteinModelPortaliP13702.
SMRiP13702.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13702.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA reductase family.Curated

Family and domain databases

CDDicd00644. HMG-CoA_reductase_classII. 1 hit.
Gene3Di3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProiIPR002202. HMG_CoA_Rdtase.
IPR004553. HMG_CoA_Rdtase_bac-typ.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd_dom.
IPR009029. HMG_CoA_Rdtase_sub-bd_dom.
[Graphical view]
PANTHERiPTHR10572. PTHR10572. 1 hit.
PfamiPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
SUPFAMiSSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsiTIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEiPS00066. HMG_COA_REDUCTASE_1. 1 hit.
PS00318. HMG_COA_REDUCTASE_2. 1 hit.
PS01192. HMG_COA_REDUCTASE_3. 1 hit.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM
60 70 80 90 100
IENVIGTFEL PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN
110 120 130 140 150
GGFTTSSSAP LMHAQVQIVG IQDPLNARLS LLRRKDEIIE LANRKDQLLN
160 170 180 190 200
SLGGGCRDIE VHTFADTPRG PMLVAHLIVD VRDAMGANTV NTMAEAVAPL
210 220 230 240 250
MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS GEAVIEGILD
260 270 280 290 300
AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH
310 320 330 340 350
YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA
360 370 380 390 400
QALAEIAVAV GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV
410 420
DWVARQLVEY HDVRADRAVA LLKQKRGQ
Length:428
Mass (Da):45,590
Last modified:January 1, 1990 - v1
Checksum:i3302701FE6E1B1F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QAXX-ray2.80A/B1-428[»]
1QAYX-ray2.80A/B1-428[»]
1R31X-ray2.10A/B1-428[»]
1R7IX-ray2.21A/B1-428[»]
1T02X-ray2.60A/B1-428[»]
4I4BX-ray1.70A/B1-428[»]
4I56X-ray1.50A/B1-428[»]
4I64X-ray1.75A/B1-428[»]
4I6AX-ray1.85A/B1-428[»]
4I6WX-ray1.66A/B1-428[»]
4I6YX-ray1.45A/B1-428[»]
ProteinModelPortaliP13702.
SMRiP13702.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00257; UER00367.
BioCyciMetaCyc:MONOMER-11829.
BRENDAi1.1.1.88. 5143.
SABIO-RKP13702.

Miscellaneous databases

EvolutionaryTraceiP13702.

Family and domain databases

CDDicd00644. HMG-CoA_reductase_classII. 1 hit.
Gene3Di3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProiIPR002202. HMG_CoA_Rdtase.
IPR004553. HMG_CoA_Rdtase_bac-typ.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd_dom.
IPR009029. HMG_CoA_Rdtase_sub-bd_dom.
[Graphical view]
PANTHERiPTHR10572. PTHR10572. 1 hit.
PfamiPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
SUPFAMiSSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsiTIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEiPS00066. HMG_COA_REDUCTASE_1. 1 hit.
PS00318. HMG_COA_REDUCTASE_2. 1 hit.
PS01192. HMG_COA_REDUCTASE_3. 1 hit.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMVAA_PSEMV
AccessioniPrimary (citable) accession number: P13702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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 one 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.