SQHC_ALIAD
ID SQHC_ALIAD Reviewed; 631 AA.
AC P33247; C8WSG4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Squalene--hopene cyclase;
DE EC=4.2.1.129;
DE EC=5.4.99.17;
DE AltName: Full=Squalene--hopanol cyclase;
GN Name=shc; OrderedLocusNames=Aaci_2443;
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1729216; DOI=10.1128/jb.174.1.298-302.1992;
RA Ochs D., Kaletta C., Entian K.-D., Beck-Sickinger A., Poralla K.;
RT "Cloning, expression, and sequencing of squalene-hopene cyclase, a key
RT enzyme in triterpenoid metabolism.";
RL J. Bacteriol. 174:298-302(1992).
RN [2]
RP SEQUENCE REVISION.
RA Ochs D., Kaletta C., Entian K.-D., Beck-Sickinger A., Poralla K.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9532806; DOI=10.1271/bbb.62.407;
RA Sato T., Kanai Y., Hoshino T.;
RT "Overexpression of squalene-hopene cyclase by the pET vector in Escherichia
RT coli and first identification of tryptophan and aspartic acid residues
RT inside the QW motif as active sites.";
RL Biosci. Biotechnol. Biochem. 62:407-411(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 2-25, AND CHARACTERIZATION.
RX PubMed=2253626; DOI=10.1111/j.1432-1033.1990.tb19429.x;
RA Ochs D., Tappe C.H., Gaertner P., Kellner R., Poralla K.;
RT "Properties of purified squalene-hopene cyclase from Bacillus
RT acidocaldarius.";
RL Eur. J. Biochem. 194:75-80(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=9295270; DOI=10.1126/science.277.5333.1811;
RA Wendt K.U., Poralla K., Schulz G.E.;
RT "Structure and function of a squalene cyclase.";
RL Science 277:1811-1815(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9931258; DOI=10.1006/jmbi.1998.2470;
RA Wendt K.U., Lenhart A., Schulz G.E.;
RT "The structure of the membrane protein squalene-hopene cyclase at 2.0-A
RT resolution.";
RL J. Mol. Biol. 286:175-187(1999).
CC -!- FUNCTION: Catalyzes the cyclization of squalene into hopene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=squalene = hop-22(29)-ene; Xref=Rhea:RHEA:17637,
CC ChEBI:CHEBI:4648, ChEBI:CHEBI:15440; EC=5.4.99.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + squalene = hopan-22-ol; Xref=Rhea:RHEA:16561,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15440, ChEBI:CHEBI:36484;
CC EC=4.2.1.129;
CC -!- PATHWAY: Secondary metabolite biosynthesis; hopanoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; M73834; AAA75452.1; -; Genomic_DNA.
DR EMBL; AB007002; BAA25185.1; -; Genomic_DNA.
DR EMBL; CP001727; ACV59449.1; -; Genomic_DNA.
DR PIR; A43300; A43300.
DR RefSeq; WP_012811690.1; NC_013205.1.
DR PDB; 1GSZ; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H35; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H36; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H37; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H39; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H3A; X-ray; 2.85 A; A/B/C=2-631.
DR PDB; 1H3B; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1H3C; X-ray; 2.90 A; A/B/C=2-631.
DR PDB; 1O6H; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1O6Q; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1O6R; X-ray; 2.70 A; A/B/C=2-631.
DR PDB; 1O79; X-ray; 2.80 A; A/B/C=2-631.
DR PDB; 1SQC; X-ray; 2.85 A; A=1-631.
DR PDB; 1UMP; X-ray; 2.13 A; A/B/C=2-631.
DR PDB; 2SQC; X-ray; 2.00 A; A/B=1-631.
DR PDB; 3SQC; X-ray; 2.80 A; A/B/C=1-631.
DR PDBsum; 1GSZ; -.
DR PDBsum; 1H35; -.
DR PDBsum; 1H36; -.
DR PDBsum; 1H37; -.
DR PDBsum; 1H39; -.
DR PDBsum; 1H3A; -.
DR PDBsum; 1H3B; -.
DR PDBsum; 1H3C; -.
DR PDBsum; 1O6H; -.
DR PDBsum; 1O6Q; -.
DR PDBsum; 1O6R; -.
DR PDBsum; 1O79; -.
DR PDBsum; 1SQC; -.
DR PDBsum; 1UMP; -.
DR PDBsum; 2SQC; -.
DR PDBsum; 3SQC; -.
DR AlphaFoldDB; P33247; -.
DR SMR; P33247; -.
DR STRING; 521098.Aaci_2443; -.
DR BindingDB; P33247; -.
DR ChEMBL; CHEMBL3569; -.
DR DrugBank; DB02139; (2e)-N-Allyl-4-{[3-(4-Bromophenyl)-5-Fluoro-1-Methyl-1h-Indazol-6-Yl]Oxy}-N-Methyl-2-Buten-1-Amine.
DR DrugBank; DB03234; (4'-{[Allyl(Methyl)Amino]Methyl}-1,1'-Biphenyl-4-Yl)(4-Bromophenyl)Methanone.
DR DrugBank; DB08458; (4-BROMOPHENYL)[4-({(2E)-4-[CYCLOPROPYL(METHYL)AMINO]BUT-2-ENYL}OXY)PHENYL]METHANONE.
DR DrugBank; DB03874; (4e,8e,12z,16z)-N,N,4,8,13,17,21-Heptamethyldocosa-4,8,12,16,20-Pentaen-1-Amine.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB03771; Allyl-{4-[3-(4-Bromo-Phenyl)-Benzofuran-6-Yloxy]-but-2-Enyl}-Methyl-Amine.
DR DrugBank; DB02339; Allyl-{6-[3-(4-Bromo-Phenyl)-Benzofuran-6-Yloxy]-Hexyl-}-Methyl-Amin.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB03748; Methyl-[4-(4-Piperidine-1-Ylmethyl-Phenyl)-Cyclohexyl]-Carbaminic Acid-(4-Chlorophenyl)-Ester.
DR DrugBank; DB02544; N-(6-{[3-(4-Bromophenyl)-1,2-Benzisothiazol-6-Yl]Oxy}Hexyl)-N-Methylprop-2-En-1-Amine.
DR DrugBank; DB03888; N-Allyl-6-{[3-(4-bromophenyl)-1-methyl-1H-indazol-6-yl]oxy}-N-methyl-1-hexanamine.
DR PRIDE; P33247; -.
DR EnsemblBacteria; ACV59449; ACV59449; Aaci_2443.
DR KEGG; aac:Aaci_2443; -.
DR eggNOG; COG1657; Bacteria.
DR HOGENOM; CLU_019345_0_0_9; -.
DR OMA; LIGEWPW; -.
DR OrthoDB; 260889at2; -.
DR BioCyc; MetaCyc:MON-17503; -.
DR BRENDA; 4.2.1.129; 243.
DR BRENDA; 5.4.99.17; 243.
DR SABIO-RK; P33247; -.
DR UniPathway; UPA00337; -.
DR EvolutionaryTrace; P33247; -.
DR PRO; PR:P33247; -.
DR Proteomes; UP000001917; Chromosome.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0051007; F:squalene-hopene cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR006400; Hopene-cyclase.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR002365; Terpene_synthase_CS.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01507; hopene_cyclase; 1.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Isomerase; Lyase;
KW Membrane; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2253626"
FT CHAIN 2..631
FT /note="Squalene--hopene cyclase"
FT /id="PRO_0000072650"
FT REPEAT 15..56
FT /note="PFTB 1"
FT REPEAT 61..102
FT /note="PFTB 2"
FT REPEAT 241..282
FT /note="PFTB 3"
FT REPEAT 400..441
FT /note="PFTB 4"
FT REPEAT 468..508
FT /note="PFTB 5"
FT REPEAT 516..557
FT /note="PFTB 6"
FT REPEAT 574..622
FT /note="PFTB 7"
FT ACT_SITE 376
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT CONFLICT 600..601
FT /note="GF -> AS (in Ref. 1; AAA75452)"
FT /evidence="ECO:0000305"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1GSZ"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1O6R"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1GSZ"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1H37"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1UMP"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2SQC"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1O6H"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1UMP"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:1O6R"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1O6R"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:2SQC"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:1GSZ"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 493..506
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 514..525
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:1SQC"
FT HELIX 553..565
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 572..584
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1H37"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:2SQC"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:2SQC"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:2SQC"
FT HELIX 612..629
FT /evidence="ECO:0007829|PDB:2SQC"
SQ SEQUENCE 631 AA; 71570 MW; E389635BD6486C3A CRC64;
MAEQLVEAPA YARTLDRAVE YLLSCQKDEG YWWGPLLSNV TMEAEYVLLC HILDRVDRDR
MEKIRRYLLH EQREDGTWAL YPGGPPDLDT TIEAYVALKY IGMSRDEEPM QKALRFIQSQ
GGIESSRVFT RMWLALVGEY PWEKVPMVPP EIMFLGKRMP LNIYEFGSWA RATVVALSIV
MSRQPVFPLP ERARVPELYE TDVPPRRRGA KGGGGWIFDA LDRALHGYQK LSVHPFRRAA
EIRALDWLLE RQAGDGSWGG IQPPWFYALI ALKILDMTQH PAFIKGWEGL ELYGVELDYG
GWMFQASISP VWDTGLAVLA LRAAGLPADH DRLVKAGEWL LDRQITVPGD WAVKRPNLKP
GGFAFQFDNV YYPDVDDTAV VVWALNTLRL PDERRRRDAM TKGFRWIVGM QSSNGGWGAY
DVDNTSDLPN HIPFCDFGEV TDPPSEDVTA HVLECFGSFG YDDAWKVIRR AVEYLKREQK
PDGSWFGRWG VNYLYGTGAV VSALKAVGID TREPYIQKAL DWVEQHQNPD GGWGEDCRSY
EDPAYAGKGA STPSQTAWAL MALIAGGRAE SEAARRGVQY LVETQRPDGG WDEPYYTGTG
FPGDFYLGYT MYRHVFPTLA LGRYKQAIER R
