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P33247

- SQHC_ALIAD

UniProt

P33247 - SQHC_ALIAD

Protein

Squalene--hopene cyclase

Gene

shc

Organism
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the cyclization of squalene into hopene.

    Catalytic activityi

    Squalene = hop-22(29)-ene.
    Hopan-22-ol = squalene + H2O.

    Pathwayi

    GO - Molecular functioni

    1. lyase activity Source: UniProtKB-KW
    2. squalene-hopene cyclase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hopanoid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase, Lyase

    Enzyme and pathway databases

    BioCyciAACI521098:GCIO-2514-MONOMER.
    MetaCyc:MONOMER-17503.
    SABIO-RKP33247.
    UniPathwayiUPA00337.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Squalene--hopene cyclase (EC:4.2.1.129, EC:5.4.99.17)
    Alternative name(s):
    Squalene--hopanol cyclase
    Gene namesi
    Name:shc
    Ordered Locus Names:Aaci_2443
    OrganismiAlicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
    Taxonomic identifieri521098 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus
    ProteomesiUP000001917: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 631630Squalene--hopene cyclasePRO_0000072650Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi521098.Aaci_2443.

    Structurei

    Secondary structure

    1
    631
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2516
    Beta strandi28 – 303
    Helixi41 – 5212
    Helixi58 – 7114
    Beta strandi79 – 813
    Helixi88 – 10114
    Beta strandi105 – 1073
    Helixi108 – 11912
    Helixi123 – 1253
    Helixi128 – 1369
    Helixi142 – 1443
    Helixi150 – 1545
    Beta strandi157 – 1593
    Helixi163 – 1653
    Helixi168 – 18316
    Helixi191 – 1933
    Helixi196 – 1994
    Beta strandi210 – 2123
    Helixi216 – 23015
    Helixi237 – 25115
    Beta strandi256 – 2583
    Helixi262 – 27413
    Helixi281 – 2888
    Helixi289 – 2935
    Beta strandi294 – 2963
    Turni298 – 3003
    Beta strandi302 – 3043
    Helixi310 – 32314
    Helixi331 – 34212
    Helixi350 – 3534
    Beta strandi365 – 3684
    Helixi375 – 38511
    Helixi393 – 40917
    Beta strandi415 – 4173
    Beta strandi419 – 4235
    Helixi428 – 4314
    Beta strandi432 – 4343
    Beta strandi436 – 4383
    Helixi446 – 45712
    Turni458 – 4603
    Beta strandi463 – 4653
    Helixi466 – 47813
    Beta strandi488 – 4925
    Helixi493 – 50614
    Helixi514 – 52512
    Helixi537 – 5404
    Helixi543 – 5453
    Beta strandi549 – 5513
    Helixi553 – 56513
    Beta strandi569 – 5713
    Helixi572 – 58413
    Beta strandi587 – 5893
    Beta strandi598 – 6014
    Turni602 – 6043
    Beta strandi605 – 6095
    Helixi612 – 62918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GSZX-ray2.80A/B/C2-631[»]
    1H35X-ray2.80A/B/C2-631[»]
    1H36X-ray2.80A/B/C2-631[»]
    1H37X-ray2.80A/B/C2-631[»]
    1H39X-ray2.80A/B/C2-631[»]
    1H3AX-ray2.85A/B/C2-631[»]
    1H3BX-ray2.80A/B/C2-631[»]
    1H3CX-ray2.90A/B/C2-631[»]
    1O6HX-ray2.80A/B/C2-631[»]
    1O6QX-ray2.80A/B/C2-631[»]
    1O6RX-ray2.70A/B/C2-631[»]
    1O79X-ray2.80A/B/C2-631[»]
    1SQCX-ray2.85A1-631[»]
    1UMPX-ray2.13A/B/C2-631[»]
    2SQCX-ray2.00A/B1-631[»]
    3SQCX-ray2.80A/B/C1-631[»]
    ProteinModelPortaliP33247.
    SMRiP33247. Positions 10-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33247.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati15 – 5642PFTB 1Add
    BLAST
    Repeati61 – 10242PFTB 2Add
    BLAST
    Repeati241 – 28242PFTB 3Add
    BLAST
    Repeati400 – 44142PFTB 4Add
    BLAST
    Repeati468 – 50841PFTB 5Add
    BLAST
    Repeati516 – 55742PFTB 6Add
    BLAST
    Repeati574 – 62249PFTB 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the terpene cyclase/mutase family.Curated
    Contains 7 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1657.
    HOGENOMiHOG000220823.
    KOiK06045.
    OMAiCKPGGWA.
    OrthoDBiEOG6K6V4Q.

    Family and domain databases

    Gene3Di1.50.10.20. 2 hits.
    InterProiIPR006400. Hopene-cyclase.
    IPR001330. Prenyltrans.
    IPR018333. Squalene_cyclase.
    IPR002365. Terpene_synthase_CS.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF00432. Prenyltrans. 3 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 2 hits.
    TIGRFAMsiTIGR01507. hopene_cyclase. 1 hit.
    TIGR01787. squalene_cyclas. 1 hit.
    PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33247-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEQLVEAPA YARTLDRAVE YLLSCQKDEG YWWGPLLSNV TMEAEYVLLC    50
    HILDRVDRDR MEKIRRYLLH EQREDGTWAL YPGGPPDLDT TIEAYVALKY 100
    IGMSRDEEPM QKALRFIQSQ GGIESSRVFT RMWLALVGEY PWEKVPMVPP 150
    EIMFLGKRMP LNIYEFGSWA RATVVALSIV MSRQPVFPLP ERARVPELYE 200
    TDVPPRRRGA KGGGGWIFDA LDRALHGYQK LSVHPFRRAA EIRALDWLLE 250
    RQAGDGSWGG IQPPWFYALI ALKILDMTQH PAFIKGWEGL ELYGVELDYG 300
    GWMFQASISP VWDTGLAVLA LRAAGLPADH DRLVKAGEWL LDRQITVPGD 350
    WAVKRPNLKP GGFAFQFDNV YYPDVDDTAV VVWALNTLRL PDERRRRDAM 400
    TKGFRWIVGM QSSNGGWGAY DVDNTSDLPN HIPFCDFGEV TDPPSEDVTA 450
    HVLECFGSFG YDDAWKVIRR AVEYLKREQK PDGSWFGRWG VNYLYGTGAV 500
    VSALKAVGID TREPYIQKAL DWVEQHQNPD GGWGEDCRSY EDPAYAGKGA 550
    STPSQTAWAL MALIAGGRAE SEAARRGVQY LVETQRPDGG WDEPYYTGTG 600
    FPGDFYLGYT MYRHVFPTLA LGRYKQAIER R 631
    Length:631
    Mass (Da):71,570
    Last modified:January 23, 2007 - v4
    Checksum:iE389635BD6486C3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti600 – 6012GF → AS in AAA75452. (PubMed:1729216)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73834 Genomic DNA. Translation: AAA75452.1.
    AB007002 Genomic DNA. Translation: BAA25185.1.
    CP001727 Genomic DNA. Translation: ACV59449.1.
    PIRiA43300.
    RefSeqiWP_012811690.1. NC_013205.1.
    YP_003185838.1. NC_013205.1.

    Genome annotation databases

    EnsemblBacteriaiACV59449; ACV59449; Aaci_2443.
    GeneIDi8425972.
    KEGGiaac:Aaci_2443.
    PATRICi20848382. VBIAliAci73240_2414.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73834 Genomic DNA. Translation: AAA75452.1 .
    AB007002 Genomic DNA. Translation: BAA25185.1 .
    CP001727 Genomic DNA. Translation: ACV59449.1 .
    PIRi A43300.
    RefSeqi WP_012811690.1. NC_013205.1.
    YP_003185838.1. NC_013205.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GSZ X-ray 2.80 A/B/C 2-631 [» ]
    1H35 X-ray 2.80 A/B/C 2-631 [» ]
    1H36 X-ray 2.80 A/B/C 2-631 [» ]
    1H37 X-ray 2.80 A/B/C 2-631 [» ]
    1H39 X-ray 2.80 A/B/C 2-631 [» ]
    1H3A X-ray 2.85 A/B/C 2-631 [» ]
    1H3B X-ray 2.80 A/B/C 2-631 [» ]
    1H3C X-ray 2.90 A/B/C 2-631 [» ]
    1O6H X-ray 2.80 A/B/C 2-631 [» ]
    1O6Q X-ray 2.80 A/B/C 2-631 [» ]
    1O6R X-ray 2.70 A/B/C 2-631 [» ]
    1O79 X-ray 2.80 A/B/C 2-631 [» ]
    1SQC X-ray 2.85 A 1-631 [» ]
    1UMP X-ray 2.13 A/B/C 2-631 [» ]
    2SQC X-ray 2.00 A/B 1-631 [» ]
    3SQC X-ray 2.80 A/B/C 1-631 [» ]
    ProteinModelPortali P33247.
    SMRi P33247. Positions 10-628.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 521098.Aaci_2443.

    Chemistry

    BindingDBi P33247.
    ChEMBLi CHEMBL3569.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACV59449 ; ACV59449 ; Aaci_2443 .
    GeneIDi 8425972.
    KEGGi aac:Aaci_2443.
    PATRICi 20848382. VBIAliAci73240_2414.

    Phylogenomic databases

    eggNOGi COG1657.
    HOGENOMi HOG000220823.
    KOi K06045.
    OMAi CKPGGWA.
    OrthoDBi EOG6K6V4Q.

    Enzyme and pathway databases

    UniPathwayi UPA00337 .
    BioCyci AACI521098:GCIO-2514-MONOMER.
    MetaCyc:MONOMER-17503.
    SABIO-RK P33247.

    Miscellaneous databases

    EvolutionaryTracei P33247.

    Family and domain databases

    Gene3Di 1.50.10.20. 2 hits.
    InterProi IPR006400. Hopene-cyclase.
    IPR001330. Prenyltrans.
    IPR018333. Squalene_cyclase.
    IPR002365. Terpene_synthase_CS.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    Pfami PF00432. Prenyltrans. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 2 hits.
    TIGRFAMsi TIGR01507. hopene_cyclase. 1 hit.
    TIGR01787. squalene_cyclas. 1 hit.
    PROSITEi PS01074. TERPENE_SYNTHASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and sequencing of squalene-hopene cyclase, a key enzyme in triterpenoid metabolism."
      Ochs D., Kaletta C., Entian K.-D., Beck-Sickinger A., Poralla K.
      J. Bacteriol. 174:298-302(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Ochs D., Kaletta C., Entian K.-D., Beck-Sickinger A., Poralla K.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Overexpression of squalene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues inside the QW motif as active sites."
      Sato T., Kanai Y., Hoshino T.
      Biosci. Biotechnol. Biochem. 62:407-411(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27009 / DSM 446 / 104-1A.
    5. "Properties of purified squalene-hopene cyclase from Bacillus acidocaldarius."
      Ochs D., Tappe C.H., Gaertner P., Kellner R., Poralla K.
      Eur. J. Biochem. 194:75-80(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25, CHARACTERIZATION.
    6. "Structure and function of a squalene cyclase."
      Wendt K.U., Poralla K., Schulz G.E.
      Science 277:1811-1815(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    7. "The structure of the membrane protein squalene-hopene cyclase at 2.0-A resolution."
      Wendt K.U., Lenhart A., Schulz G.E.
      J. Mol. Biol. 286:175-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiSQHC_ALIAD
    AccessioniPrimary (citable) accession number: P33247
    Secondary accession number(s): C8WSG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3