Skip Header

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

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase

Gene

menH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro.2 Publications

Catalytic activityi

5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate.UniRule annotation1 Publication

Kineticsi

  1. KM=10.1 µM for SEPHCHC (at 25 degrees Celsius and pH 7)1 Publication

    Pathwayi: 1,4-dihydroxy-2-naphthoate biosynthesis

    This protein is involved in step 3 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. Isochorismate synthase MenF (menF)
    2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
    3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
    4. o-succinylbenzoate synthase (menC)
    5. 2-succinylbenzoate--CoA ligase (menE)
    6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
    7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
    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

    • menaquinone biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Menaquinone biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12438-MONOMER.
    ECOL316407:JW2258-MONOMER.
    MetaCyc:EG12438-MONOMER.
    BRENDAi3.1.2.2. 2026.
    UniPathwayiUPA00079.
    UPA01057; UER00900.

    Protein family/group databases

    ESTHERiecoli-YFBB. MenH_SHCHC.
    MEROPSiS33.996.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthaseUniRule annotation (EC:4.2.99.20UniRule annotation)
    Short name:
    SHCHC synthaseUniRule annotation
    Gene namesi
    Name:menHUniRule annotation
    Synonyms:yfbB
    Ordered Locus Names:b2263, JW2258
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12438. menH.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861S → A: 1400-fold decrease in catalytic activity. 1 Publication
    Mutagenesisi210 – 2101D → A: Loss of activity. 1 Publication
    Mutagenesisi232 – 2321H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2522522-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthasePRO_0000169174Add
    BLAST

    Proteomic databases

    PaxDbiP37355.
    PRIDEiP37355.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi4260505. 14 interactions.
    IntActiP37355. 5 interactions.
    STRINGi511145.b2263.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84Combined sources
    Beta strandi16 – 205Combined sources
    Turni27 – 304Combined sources
    Helixi31 – 344Combined sources
    Helixi35 – 373Combined sources
    Beta strandi40 – 456Combined sources
    Helixi51 – 533Combined sources
    Helixi61 – 7414Combined sources
    Beta strandi79 – 857Combined sources
    Helixi87 – 9812Combined sources
    Beta strandi103 – 1108Combined sources
    Helixi118 – 13720Combined sources
    Helixi140 – 1478Combined sources
    Helixi151 – 1533Combined sources
    Helixi158 – 16811Combined sources
    Helixi173 – 18210Combined sources
    Helixi185 – 1873Combined sources
    Helixi192 – 1965Combined sources
    Beta strandi199 – 2079Combined sources
    Helixi211 – 2188Combined sources
    Beta strandi220 – 2278Combined sources
    Helixi234 – 2374Combined sources
    Helixi239 – 25012Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GDMX-ray2.75A/B/C1-252[»]
    4GECX-ray2.50A/B/C1-252[»]
    4GEGX-ray2.49A/B/C1-252[»]
    4MXDX-ray1.45A1-252[»]
    4MYDX-ray1.37A/B/C1-252[»]
    4MYSX-ray1.42A/B/C1-252[»]
    ProteinModelPortaliP37355.
    SMRiP37355. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. MenH family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4107J5P. Bacteria.
    COG0596. LUCA.
    HOGENOMiHOG000028072.
    InParanoidiP37355.
    KOiK08680.
    OMAiLNDWYQQ.
    PhylomeDBiP37355.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_01660. MenH. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR022485. SHCHC_synthase_MenH.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR03695. menH_SHCHC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37355-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MILHAQAKHG KPGLPWLVFL HGFSGDCHEW QEVGEAFADY SRLYVDLPGH
    60 70 80 90 100
    GGSAAISVDG FDDVTDLLRK TLVSYNILDF WLVGYSLGGR VAMMAACQGL
    110 120 130 140 150
    AGLCGVIVEG GHPGLQNAEQ RAERQRSDRQ WVQRFLTEPL TAVFADWYQQ
    160 170 180 190 200
    PVFASLNDDQ RRELVALRSN NNGATLAAML EATSLAVQPD LRANLSARTF
    210 220 230 240 250
    AFYYLCGERD SKFRALAAEL AADCHVIPRA GHNAHRENPA GVIASLAQIL

    RF
    Length:252
    Mass (Da):27,682
    Last modified:April 27, 2001 - v2
    Checksum:iFE7D77861842B68C
    GO

    Sequence cautioni

    The sequence AAA24151 differs from that shown. Reason: Frameshift at position 182. Curated
    The sequence M93421 differs from that shown. Reason: Frameshift at position 182. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761L → V in AAA24151 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L35030 Genomic DNA. Translation: AAA24151.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC75323.1.
    AP009048 Genomic DNA. Translation: BAA16087.2.
    M93421 Genomic DNA. No translation available.
    PIRiE64997.
    RefSeqiNP_416766.1. NC_000913.3.
    WP_000600499.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75323; AAC75323; b2263.
    BAA16087; BAA16087; BAA16087.
    GeneIDi946736.
    KEGGiecj:JW2258.
    eco:b2263.
    PATRICi32119893. VBIEscCol129921_2356.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L35030 Genomic DNA. Translation: AAA24151.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC75323.1.
    AP009048 Genomic DNA. Translation: BAA16087.2.
    M93421 Genomic DNA. No translation available.
    PIRiE64997.
    RefSeqiNP_416766.1. NC_000913.3.
    WP_000600499.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GDMX-ray2.75A/B/C1-252[»]
    4GECX-ray2.50A/B/C1-252[»]
    4GEGX-ray2.49A/B/C1-252[»]
    4MXDX-ray1.45A1-252[»]
    4MYDX-ray1.37A/B/C1-252[»]
    4MYSX-ray1.42A/B/C1-252[»]
    ProteinModelPortaliP37355.
    SMRiP37355. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260505. 14 interactions.
    IntActiP37355. 5 interactions.
    STRINGi511145.b2263.

    Protein family/group databases

    ESTHERiecoli-YFBB. MenH_SHCHC.
    MEROPSiS33.996.

    Proteomic databases

    PaxDbiP37355.
    PRIDEiP37355.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75323; AAC75323; b2263.
    BAA16087; BAA16087; BAA16087.
    GeneIDi946736.
    KEGGiecj:JW2258.
    eco:b2263.
    PATRICi32119893. VBIEscCol129921_2356.

    Organism-specific databases

    EchoBASEiEB2333.
    EcoGeneiEG12438. menH.

    Phylogenomic databases

    eggNOGiENOG4107J5P. Bacteria.
    COG0596. LUCA.
    HOGENOMiHOG000028072.
    InParanoidiP37355.
    KOiK08680.
    OMAiLNDWYQQ.
    PhylomeDBiP37355.

    Enzyme and pathway databases

    UniPathwayiUPA00079.
    UPA01057; UER00900.
    BioCyciEcoCyc:EG12438-MONOMER.
    ECOL316407:JW2258-MONOMER.
    MetaCyc:EG12438-MONOMER.
    BRENDAi3.1.2.2. 2026.

    Miscellaneous databases

    PROiP37355.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_01660. MenH. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR022485. SHCHC_synthase_MenH.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR03695. menH_SHCHC. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMENH_ECOLI
    AccessioniPrimary (citable) accession number: P37355
    Secondary accession number(s): P76477, P76932
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: April 27, 2001
    Last modified: September 7, 2016
    This is version 131 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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 one 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.