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Protein

Squalene--hopene cyclase

Gene

shc

Organism
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A) (Bacillus acidocaldarius)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cyclization of squalene into hopene.

Catalytic activityi

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

Pathway:ihopanoid biosynthesis

This protein is involved in the pathway hopanoid biosynthesis, which is part of Secondary metabolite biosynthesis.
View all proteins of this organism that are known to be involved in the pathway hopanoid biosynthesis and in Secondary metabolite biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Enzyme and pathway databases

BioCyciAACI521098:GCIO-2514-MONOMER.
MetaCyc:MONOMER-17503.
BRENDAi5.4.99.17. 243.
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 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A) (Bacillus acidocaldarius)
Taxonomic identifieri521098 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus
ProteomesiUP000001917 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiRQENDGC.
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

        10         20         30         40         50
MAEQLVEAPA YARTLDRAVE YLLSCQKDEG YWWGPLLSNV TMEAEYVLLC
60 70 80 90 100
HILDRVDRDR MEKIRRYLLH EQREDGTWAL YPGGPPDLDT TIEAYVALKY
110 120 130 140 150
IGMSRDEEPM QKALRFIQSQ GGIESSRVFT RMWLALVGEY PWEKVPMVPP
160 170 180 190 200
EIMFLGKRMP LNIYEFGSWA RATVVALSIV MSRQPVFPLP ERARVPELYE
210 220 230 240 250
TDVPPRRRGA KGGGGWIFDA LDRALHGYQK LSVHPFRRAA EIRALDWLLE
260 270 280 290 300
RQAGDGSWGG IQPPWFYALI ALKILDMTQH PAFIKGWEGL ELYGVELDYG
310 320 330 340 350
GWMFQASISP VWDTGLAVLA LRAAGLPADH DRLVKAGEWL LDRQITVPGD
360 370 380 390 400
WAVKRPNLKP GGFAFQFDNV YYPDVDDTAV VVWALNTLRL PDERRRRDAM
410 420 430 440 450
TKGFRWIVGM QSSNGGWGAY DVDNTSDLPN HIPFCDFGEV TDPPSEDVTA
460 470 480 490 500
HVLECFGSFG YDDAWKVIRR AVEYLKREQK PDGSWFGRWG VNYLYGTGAV
510 520 530 540 550
VSALKAVGID TREPYIQKAL DWVEQHQNPD GGWGEDCRSY EDPAYAGKGA
560 570 580 590 600
STPSQTAWAL MALIAGGRAE SEAARRGVQY LVETQRPDGG WDEPYYTGTG
610 620 630
FPGDFYLGYT MYRHVFPTLA LGRYKQAIER R
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi521098.Aaci_2443.

Chemistry

BindingDBiP33247.
ChEMBLiCHEMBL3569.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1657.
HOGENOMiHOG000220823.
KOiK06045.
OMAiRQENDGC.
OrthoDBiEOG6K6V4Q.

Enzyme and pathway databases

UniPathwayiUPA00337.
BioCyciAACI521098:GCIO-2514-MONOMER.
MetaCyc:MONOMER-17503.
BRENDAi5.4.99.17. 243.
SABIO-RKP33247.

Miscellaneous databases

EvolutionaryTraceiP33247.
PROiP33247.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 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: July 22, 2015
This is version 121 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

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 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.