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Protein

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

Gene

menD

Organism
Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium acnes)
Status
Reviewed-Annotation score: -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: 1,4-dihydroxy-2-naphthoate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. no protein annotated in this organism
  4. o-succinylbenzoate synthase (menC)
  5. no protein annotated in this organism
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. no protein annotated in this organism
This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processMenaquinone biosynthesis
LigandMagnesium, Manganese, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

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
OrganismiCutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium acnes)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaeCutibacterium
Proteomesi
  • UP000000603 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003418091 – 5082-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseAdd BLAST508

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

eggNOGiENOG4105C4A Bacteria
COG1165 LUCA
HOGENOMiHOG000218359
KOiK02551
OMAiIFRILPG

Family and domain databases

HAMAPiMF_01659 MenD, 1 hit
InterProiView protein in InterPro
IPR004433 MenaQ_synth_MenD
IPR029061 THDP-binding
IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
IPR011766 TPP_enzyme-bd_C
PANTHERiPTHR42916 PTHR42916, 1 hit
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF02776 TPP_enzyme_N, 1 hit
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 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.

Genome annotation databases

EnsemblBacteriaiAAT82656; AAT82656; PPA0903
KEGGipac:PPA0903

Similar proteinsi

Entry informationi

Entry nameiMEND_CUTAK
AccessioniPrimary (citable) accession number: Q6A9B0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: March 28, 2018
This is version 84 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health