Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

A5CUV9

- MEND_CLAM3

UniProt

A5CUV9 - MEND_CLAM3

Protein

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

Gene

menD

Organism
Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciCMIC443906:GCI2-2898-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:CMM_2812
    OrganismiClavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
    Taxonomic identifieri443906 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter
    ProteomesiUP000001564: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5885882-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthasePRO_0000341724Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi443906.CMM_2812.

    Structurei

    3D structure databases

    ProteinModelPortaliA5CUV9.
    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.

    A5CUV9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTTGSLPAQ PSSTSPRTGN PSTDRALAML LALVREGVTD VVLCPGSRSQ    50
    ALALVAAELE RVDGVRLHVR IDERAAGFLA LGLGVESGRP APVITTSGTA 100
    VANLHPAVLE GWHSGVPMLL LTGDRPAELR GIASNQTTRQ PGMFGDRVVV 150
    VDVPAPEETD EDLSRDARLA RDAYRRARDE RTPVHVNVAF RDPLSVAVPD 200
    LAEAVAEAHA AADAEAAAAP APAGPTAADV LDLPHGPRTL VVAGHAAGEA 250
    AEELARAGGW PLAAEISSGS HFGPNLVVSF RELLARPGFG DRVERVIVFG 300
    HPTLTREVPL LVGREDVEAI VVGSTGGEDY DPRHRVTAHP AAVRVVGEPA 350
    DPAEARRWTG TWVQASRAIL DEASAAESAP LLPSGTTPAE RRDFARAELA 400
    AVRADVTRRH LVRALWQATW PHDRLVLGAS RLIREADRAL PGKRVRVHAN 450
    RGLAGIDGTI STGLGIALAS QAGSGSAAAG ITRVLVGDLT LLHDVGSLLI 500
    GTGERVPRIQ VIVGNDGGGT IFDGLEVANT AAPAAIDRVM FTPQRVDLAS 550
    LAKAYGWTHL RAATHGELEA ALTTASGAPL LIEVPLVR 588
    Length:588
    Mass (Da):61,363
    Last modified:June 12, 2007 - v1
    Checksum:i52D8F8F15A9CB078
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM711867 Genomic DNA. Translation: CAN02897.1.
    RefSeqiYP_001223557.1. NC_009480.1.

    Genome annotation databases

    EnsemblBacteriaiCAN02897; CAN02897; CMM_2812.
    GeneIDi5173302.
    KEGGicmi:CMM_2812.
    PATRICi21456487. VBIClaMic82482_2937.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM711867 Genomic DNA. Translation: CAN02897.1 .
    RefSeqi YP_001223557.1. NC_009480.1.

    3D structure databases

    ProteinModelPortali A5CUV9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 443906.CMM_2812.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAN02897 ; CAN02897 ; CMM_2812 .
    GeneIDi 5173302.
    KEGGi cmi:CMM_2812.
    PATRICi 21456487. VBIClaMic82482_2937.

    Phylogenomic databases

    eggNOGi COG1165.
    HOGENOMi HOG000218359.
    KOi K02551.
    OMAi WRSAVCR.
    OrthoDBi EOG6NWBQW.

    Enzyme and pathway databases

    UniPathwayi UPA00079 ; UER00164 .
    BioCyci CMIC443906:GCI2-2898-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. "The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
      Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.
      , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
      J. Bacteriol. 190:2138-2149(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCPPB 382.

    Entry informationi

    Entry nameiMEND_CLAM3
    AccessioniPrimary (citable) accession number: A5CUV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 56 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