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Protein

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase

Gene

menD

Organism
Rhodococcus equi (strain 103S) (Corynebacterium equi)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).UniRule annotationSAAS annotation

Catalytic activityi

Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationSAAS annotation, Mn2+UniRule annotationSAAS annotation
  • thiamine diphosphateNote: Binds 1 thiamine pyrophosphate per subunit.
  • thiamine diphosphateUniRule annotationSAAS annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotationSAAS annotation

Pathwayi

GO - Molecular functioni

  1. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. manganese ion binding Source: UniProtKB-HAMAP
  4. thiamine pyrophosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. menaquinone biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotation

Keywords - Biological processi

Menaquinone biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, ManganeseUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Thiamine pyrophosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciREQU685727:GHKP-3581-MONOMER.
UniPathwayiUPA00079.
UPA01057; UER00164.

Names & Taxonomyi

Protein namesi
Recommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseUniRule annotationSAAS annotation (EC:2.2.1.9UniRule annotationSAAS annotation)
Short name:
SEPHCHC synthaseUniRule annotation
Alternative name(s):
Menaquinone biosynthesis protein MenDUniRule annotation
Gene namesi
Name:menDUniRule annotationImported
Ordered Locus Names:REQ_36990Imported
OrganismiRhodococcus equi (strain 103S) (Corynebacterium equi)Imported
Taxonomic identifieri685727 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000006892 Componenti: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family. MenD subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218359.
KOiK02551.
OMAiWRSAVCR.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01659. MenD.
InterProiIPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
PfamiPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.

Sequencei

Sequence statusi: Complete.

E4W8B1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSTAQATA VVDELIRGGV REVVLCPGSR NAPLAFALQA ADAAGRLRLH
60 70 80 90 100
LRIDERTAGF LAIGLAVASG QPVPVVMTSG TAVANLGPAV LEANYARIPL
110 120 130 140 150
IVLSANRPYE MLGTGANQTV EQFGLFGSQV RAAISLGLAE EAGDESQRGI
160 170 180 190 200
RFDEQNSQWR SAVCRVLAAA RGTRSGNAGP VHFDIPLREP LVPDVRPRGL
210 220 230 240 250
VPEGRPGGAA WTTTVHATLD VPMDLDITAD TVVVSGHGSA YRPELAGLPT
260 270 280 290 300
VAEPTAPLHG IPLHPLALPQ LKPRQAIITG RPTLHRPVSK LLADPSVAVY
310 320 330 340 350
ALTTGPRWPD VSGNVLATGT RAVVTGEPDP AWIARCRHLS EHADKAVRSQ
360 370 380 390 400
LDAHPTATGL HVAAAVMEAL SDGDQLLLGA SNPVRDAALV SYPRPGVKVL
410 420 430 440 450
SNRGVAGIDG TVSTAVGAAL AYESEGRTVA LLGDLTFLHD ASGLLIGTGE
460 470 480 490 500
PRPTDLTIVV ANDDGGGIFE LLEQGDPQYA GVFERVFGTP HGMDLAALCA
510 520 530 540
AYRVPHRRVD LAELTAVLTA PGDGIRVLEV TTERSGLREL HAAVRAQL
Length:548
Mass (Da):57,229
Last modified:February 7, 2011 - v1
Checksum:i864CFE51D4C22D8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN563149 Genomic DNA. Translation: CBH49686.1.
RefSeqiYP_004008365.1. NC_014659.1.

Genome annotation databases

EnsemblBacteriaiCBH49686; CBH49686; REQ_36990.
KEGGireq:REQ_36990.
PATRICi42664885. VBIRhoEqu141084_3702.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN563149 Genomic DNA. Translation: CBH49686.1.
RefSeqiYP_004008365.1. NC_014659.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBH49686; CBH49686; REQ_36990.
KEGGireq:REQ_36990.
PATRICi42664885. VBIRhoEqu141084_3702.

Phylogenomic databases

HOGENOMiHOG000218359.
KOiK02551.
OMAiWRSAVCR.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00164.
BioCyciREQU685727:GHKP-3581-MONOMER.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01659. MenD.
InterProiIPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
PfamiPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 103SImported.

Entry informationi

Entry nameiE4W8B1_RHOE1
AccessioniPrimary (citable) accession number: E4W8B1
Entry historyi
Integrated into UniProtKB/TrEMBL: February 7, 2011
Last sequence update: February 7, 2011
Last modified: March 31, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.