SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B1IXS2

- MEND_ECOLC

UniProt

B1IXS2 - MEND_ECOLC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Gene
menD, EcolC_1384
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Status
Reviewed - 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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium or manganese By similarity.UniRule annotation
Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathwayi

GO - Molecular functioni

  1. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. thiamine pyrophosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciECOL481805:GI3G-1422-MONOMER.
UniPathwayiUPA00079; UER00164.

Names & Taxonomyi

Protein namesi
Recommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (EC:2.2.1.9)
Short name:
SEPHCHC synthase
Alternative name(s):
Menaquinone biosynthesis protein MenD
Gene namesi
Name:menD
Ordered Locus Names:EcolC_1384
OrganismiEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Taxonomic identifieri481805 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000317: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5565562-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseUniRule annotation
PRO_0000341738Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi481805.EcolC_1384.

Structurei

3D structure databases

ProteinModelPortaliB1IXS2.
SMRiB1IXS2. Positions 1-556.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1165.
HOGENOMiHOG000218360.
KOiK02551.
OMAiQKPWLLE.
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.

B1IXS2-1 [UniParc]FASTAAdd to Basket

« Hide

MSVSAFNRRW AAVILEALTR HGVRHICIAP GSRSTPLTLA AAENSAFIHH    50
THFDERGLGH LALGLAKVSK QPVAMIVTSG TAVANLYPAL IEAGLTGEKL 100
ILLTADRPPE LIDCGANQAI RQPGMFASHP THSISLPRPT QDIPARWLVS 150
TIDHALGTLH AGGVHINCPF AEPLYGEMDD TGLSWQQRLG DWWQDDKPWL 200
REAPRLESEK QRDWFFWRQK RGVVVAGRMS AEEGKKVALW AQTLGWPLIG 250
DVLSQTGQPL PCADLWLGNA KATSELQQAQ IVVQLGSSLT GKRLLQWQAS 300
CEPEEYWIVD DIEGRLDPAH HRGRRLIANI ADWLELHPAE KRQPWCVEIP 350
RLAEQAMQAV IARRDAFGEA QLAHRICDYL PEQGQLFVGN SLVVRLIDAL 400
SQLPAGYPVY SNRGASGIDG LLSTAAGVQR ASGKPTLAIV GDLSALYDLN 450
ALALLRQVSA PLVLIVVNNN GGQIFSLLPT PQSERERFYL MPQNVHFEHA 500
AAMFELKYHR PQNWQELETA FADAWRTPTT TVIEMVVNDT DGAQTLQQLL 550
AQVSHL 556
Length:556
Mass (Da):61,399
Last modified:April 29, 2008 - v1
Checksum:i76433D36EC2F01A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000946 Genomic DNA. Translation: ACA77048.1.
RefSeqiWP_012304851.1. NC_010468.1.
YP_001724375.1. NC_010468.1.

Genome annotation databases

EnsemblBacteriaiACA77048; ACA77048; EcolC_1384.
GeneIDi6068024.
KEGGiecl:EcolC_1384.
PATRICi18225487. VBIEscCol82905_1478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000946 Genomic DNA. Translation: ACA77048.1 .
RefSeqi WP_012304851.1. NC_010468.1.
YP_001724375.1. NC_010468.1.

3D structure databases

ProteinModelPortali B1IXS2.
SMRi B1IXS2. Positions 1-556.
ModBasei Search...

Protein-protein interaction databases

STRINGi 481805.EcolC_1384.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA77048 ; ACA77048 ; EcolC_1384 .
GeneIDi 6068024.
KEGGi ecl:EcolC_1384.
PATRICi 18225487. VBIEscCol82905_1478.

Phylogenomic databases

eggNOGi COG1165.
HOGENOMi HOG000218360.
KOi K02551.
OMAi QKPWLLE.
OrthoDBi EOG6NWBQW.

Enzyme and pathway databases

UniPathwayi UPA00079 ; UER00164 .
BioCyci ECOL481805:GI3G-1422-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
HAMAPi MF_01659. MenD.
InterProi IPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view ]
Pfami PF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF004983. MenD. 1 hit.
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00173. menD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Escherichia coli C str. ATCC 8739."
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8739 / DSM 1576 / Crooks.

Entry informationi

Entry nameiMEND_ECOLC
AccessioniPrimary (citable) accession number: B1IXS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: April 29, 2008
Last modified: September 3, 2014
This is version 46 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

Complete 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