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Q0I316

- MEND_HISS1

UniProt

Q0I316 - MEND_HISS1

Protein

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

Gene

menD

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      Previous versions | rss
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    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

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

    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

    GO - Biological processi

    1. menaquinone biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Menaquinone biosynthesis

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciHSOM205914:GJ7V-644-MONOMER.
    UniPathwayiUPA00079; 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:HS_0617
    OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
    Taxonomic identifieri205914 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
    ProteomesiUP000001970: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5685682-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthasePRO_0000341756Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi205914.HS_0617.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0I316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1165.
    HOGENOMiHOG000218360.
    KOiK02551.
    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.

    Q0I316-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSASVFNRCW SKVILETLSR QGVSHFCIAP GSRSTPLTLE AIRLQENGRG    50
    TCHAHFDERS LGFFALGIAK ASKKPVAVIV TSGTATANLY PAIIEARQTD 100
    VPLIILTADR PPELLECGAN QAILQQNMFA QYPIASINLP RPSQNYSAQW 150
    LISVLDQACF RQKQGGVIHI NVPFAEPLYN ANNDEIDLHP WLSNIQSWLT 200
    QNKNWIQHQE QHTEVITHKY WDQWRTKKGI IIVGRLPSEQ AMGIAEWADN 250
    MGWIMITDIQ SHVKPTLPYA DIWLANQTVR KKLLQAEIVI QFGSGFIGKR 300
    INQFLAEFKG EYWIIENNQK AVDPYHHAHT RFNAKPHHWL RAHPPMRKKP 350
    WLLEPLALAK FCADFIKQRV GSNLNEASLA HNIELLLPKS NSVLFLGNSL 400
    FVRLADALSQ PSANYPIYTN RGASGIDGLL ATAAGIAVGS EQTLVAMIGD 450
    TSTLYDLNSF ALFKQLNQPA IIFVINNNGG AIFDMLPVDI AVKEKYYRMS 500
    HYLEFSHIAA MFDLKYARPY TWADLATVLK QAYSRRETTV IEIKVNPNDG 550
    SNIYKDLIDK IGHALIGV 568
    Length:568
    Mass (Da):63,786
    Last modified:October 3, 2006 - v1
    Checksum:i83A7C0CCC0908D3A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI24894.1.
    RefSeqiYP_718829.1. NC_008309.1.

    Genome annotation databases

    EnsemblBacteriaiABI24894; ABI24894; HS_0617.
    GeneIDi4240103.
    KEGGihso:HS_0617.
    PATRICi20281207. VBIHaeSom53361_0646.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI24894.1 .
    RefSeqi YP_718829.1. NC_008309.1.

    3D structure databases

    ProteinModelPortali Q0I316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 205914.HS_0617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI24894 ; ABI24894 ; HS_0617 .
    GeneIDi 4240103.
    KEGGi hso:HS_0617.
    PATRICi 20281207. VBIHaeSom53361_0646.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00079 ; UER00164 .
    BioCyci HSOM205914:GJ7V-644-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 genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
      Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
      J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129Pt.

    Entry informationi

    Entry nameiMEND_HISS1
    AccessioniPrimary (citable) accession number: Q0I316
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 66 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