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Protein

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

Gene

menD

Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
Status
Reviewed-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 annotation

Catalytic activityi

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

Cofactori

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

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciPACN267747:GHO9-912-MONOMER.
UniPathwayiUPA00079.
UPA01057; UER00164.

Names & Taxonomyi

Protein namesi
Recommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseUniRule annotation (EC:2.2.1.9UniRule annotation)
Short name:
SEPHCHC synthaseUniRule annotation
Alternative name(s):
Menaquinone biosynthesis protein MenDUniRule annotation
Gene namesi
Name:menDUniRule annotation
Ordered Locus Names:PPA0903
OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
ProteomesiUP000000603 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5085082-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthasePRO_0000341809Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267747.PPA0903.

Structurei

3D structure databases

ProteinModelPortaliQ6A9B0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1165.
HOGENOMiHOG000218359.
KOiK02551.
OMAiWRSAVCR.
OrthoDBiEOG6NWBQW.

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.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6A9B0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSTAVARR LVNALVEAGV EHVVYCPGSR DAPIGYALAD AETAGWLRVY
60 70 80 90 100
VRLDERSAGF VALGLGRAGC PAALVTTSGT AVANIHPAVL EADAAGVPLI
110 120 130 140 150
VLSADRPAEM WHTGANQTTV QTGIFGSAPR LSTDVPAGFP ADERLDALVL
160 170 180 190 200
RAVTAATGAL SADPGPVHLN VSFRDSLVPD GPWQPQALVP RRVSSFPTAP
210 220 230 240 250
TPLVMPARTV VVAGDGAGSL ARELAQQGGW PLLAEPTSGS RVGDNALTDY
260 270 280 290 300
QTVLGSELVD DVEAVLVLGH PTLSRPVSRL LARPDVTVVT DRSRWTDVAG
310 320 330 340 350
VARVVTGPVE LAEIDTDPAW LGRWKDADRP VVPTAKQRLC RDIWWACTTP
360 370 380 390 400
NAPVLVIGAS EVIRCFDRFA VPGDIAPTAL ANRGLAGIDG TIATAIGVGL
410 420 430 440 450
GTGRPVRVVV GDLTFAHDAM SLLLGETEPE PDVQVVVLDD RGGAIFSGLE
460 470 480 490 500
HAAAPAPVLR RMFLTPQRLD SAALAHALGA SHRRVSPDDL QFLDEPVVGR

QVVSVPLT
Length:508
Mass (Da):53,075
Last modified:July 1, 2008 - v2
Checksum:iB9ADC09A593370E0
GO

Sequence cautioni

The sequence AAT82656.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82656.1. Different initiation.
RefSeqiWP_011183774.1. NC_006085.1.
YP_055614.1. NC_006085.1.

Genome annotation databases

EnsemblBacteriaiAAT82656; AAT82656; PPA0903.
KEGGipac:PPA0903.
PATRICi23036523. VBIProAcn64440_0936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82656.1. Different initiation.
RefSeqiWP_011183774.1. NC_006085.1.
YP_055614.1. NC_006085.1.

3D structure databases

ProteinModelPortaliQ6A9B0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267747.PPA0903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT82656; AAT82656; PPA0903.
KEGGipac:PPA0903.
PATRICi23036523. VBIProAcn64440_0936.

Phylogenomic databases

eggNOGiCOG1165.
HOGENOMiHOG000218359.
KOiK02551.
OMAiWRSAVCR.
OrthoDBiEOG6NWBQW.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00164.
BioCyciPACN267747:GHO9-912-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.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
    Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
    Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KPA171202 / DSM 16379.

Entry informationi

Entry nameiMEND_PROAC
AccessioniPrimary (citable) accession number: Q6A9B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: May 27, 2015
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.