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SHC1_SCHJY
ID   SHC1_SCHJY              Reviewed;         656 AA.
AC   B6K412;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Squalene-hopene cyclase {ECO:0000303|PubMed:34353908};
DE            Short=SHC {ECO:0000303|PubMed:34353908};
DE            EC=4.2.1.129 {ECO:0000305|PubMed:34353908};
DE            EC=5.4.99.17 {ECO:0000305|PubMed:34353908};
GN   Name=shc1 {ECO:0000303|PubMed:34353908}; ORFNames=SJAG_03360;
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936;
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [2]
RP   FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=34353908; DOI=10.1073/pnas.2105225118;
RA   Bouwknegt J., Wiersma S.J., Ortiz-Merino R.A., Doornenbal E.S.R.,
RA   Buitenhuis P., Giera M., Mueller C., Pronk J.T.;
RT   "A squalene-hopene cyclase in Schizosaccharomyces japonicus represents a
RT   eukaryotic adaptation to sterol-limited anaerobic environments.";
RL   Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC   -!- FUNCTION: Squalene cyclase that catalyzes the oxygen-independent
CC       cyclization of squalene into hopanoids, a class of cyclic triterpenoids
CC       including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22-
CC       ol. {ECO:0000269|PubMed:34353908}.
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         Evidence={ECO:0000305|PubMed:34353908};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17638;
CC         Evidence={ECO:0000305|PubMed:34353908};
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; Evidence={ECO:0000305|PubMed:34353908};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16562;
CC         Evidence={ECO:0000305|PubMed:34353908};
CC   -!- BIOTECHNOLOGY: The fast anaerobic growth of Schizosaccharomyces
CC       japonicus in sterol-free media is an interesting trait for developing
CC       robust fungal cell factories for application in anaerobic industrial
CC       processes. {ECO:0000269|PubMed:34353908}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; KE651167; EEB08219.1; -; Genomic_DNA.
DR   RefSeq; XP_002174512.1; XM_002174476.2.
DR   STRING; 4897.EEB08219; -.
DR   EnsemblFungi; EEB08219; EEB08219; SJAG_03360.
DR   GeneID; 7050081; -.
DR   VEuPathDB; FungiDB:SJAG_03360; -.
DR   eggNOG; KOG0497; Eukaryota.
DR   HOGENOM; CLU_019345_0_0_1; -.
DR   OMA; DYYRHYF; -.
DR   OrthoDB; 365003at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051007; F:squalene-hopene cyclase activity; IEA:RHEA.
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; 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.
PE   1: Evidence at protein level;
KW   Isomerase; Lyase; Reference proteome; Repeat.
FT   CHAIN           1..656
FT                   /note="Squalene-hopene cyclase"
FT                   /id="PRO_0000455302"
FT   REPEAT          68..110
FT                   /note="PFTB 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          417..459
FT                   /note="PFTB 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          485..525
FT                   /note="PFTB 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          533..582
FT                   /note="PFTB 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          591..634
FT                   /note="PFTB 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        396
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            324
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            506
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   656 AA;  74242 MW;  0A9E4F20813CCD0A CRC64;
     MKTDGNTTLD TTISMEELER TVKSAYEALA KDQQDDGHWI YELEADVTIP AQFILLEHTL
     DKIDEELEQK IANYLRRCQS REHWGWPVYY GGEFNISASV QAYFALKMTG EDINAPHMVR
     AREAILAHGG PEYANVFTRI QLSLFGEASW LATPFMPVEI MLLPRWMYFS IWNMSYWSRT
     TVAPLLIVAD LKPKAINPRN VHIPELFPTP PDKVKTWIHG PFRSKWGHVF KFIDTAIRPF
     TRFVPSFLHK KAYKAALDFI EPRLNGVDGL GAIYPPMSYS AVMYRALGIP DDDPRAATNW
     EALKGLLVIK EREAYCQACV SPVWDTALSG HALMEASFGP DGINADRTEK LIDRAAHWLR
     AHQVLNVVGD WAINNPNLQP GGWAFQYGND YYPDVDDTAV AAMLLHRQNL PENEEALDRA
     RKWIIGMQSS NGGWGAFDID NDKQILNDIP FADHGALLDP PTADVSARCI SLLAELGHPE
     DRPVIERGIK YLRKEQEEDG SWFGRWGTNY IYGAWSVLCA FNASGVPHDD PSVLKCVNFL
     KSVQREDGGW GESCETYEGS AHGVYTESLP SQTAWAVLGL MASGRRTDPA VKRGIVWLIQ
     HQQDNGEWAE EPFNAVGFPR MFYLHYLGYK QFFPLLALAR YRHMEKSGTN NVSFAF
 
 
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