AFUMA_ASPFC
ID AFUMA_ASPFC Reviewed; 738 AA.
AC B0Y565;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Squalene hopane cyclase afumA {ECO:0000303|PubMed:30977375};
DE EC=5.4.99.- {ECO:0000269|PubMed:30977375};
DE AltName: Full=Fumihopaside A biosynthesis cluster protein A {ECO:0000303|PubMed:30977375};
GN Name=afumA {ECO:0000303|PubMed:30977375}; ORFNames=AFUB_071550;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30977375; DOI=10.1021/acs.orglett.9b00984;
RA Ma K., Zhang P., Tao Q., Keller N.P., Yang Y., Yin W.B., Liu H.;
RT "Characterization and Biosynthesis of a Rare Fungal Hopane-Type
RT Triterpenoid Glycoside Involved in the Antistress Property of Aspergillus
RT fumigatus.";
RL Org. Lett. 21:3252-3256(2019).
CC -!- FUNCTION: Squalene hopane cyclase; part of the gene cluster that
CC mediates the biosynthesis fumihopaside A, a hopane-type glucoside that
CC enhances the thermotolerance and UV resistance of N.fumigata
CC (PubMed:30977375). The first step of fumihopaside A biosynthesis is
CC performed by the squalene hopane cyclase afumA that catalyzes the
CC cyclization of 3S-oxidosqualene into the hopene 21-beta-H-hopane-3-
CC beta,22-diol (PubMed:30977375). The cytochrome P450 monooxygenase afumB
CC is responsible for both hydroxylation at C-24 and oxidations at C-30 of
CC the afumA product (PubMed:30977375). The glycosyltransferase afumC then
CC catalyzes the glycosylation at C-24, using UDP-D-glucose as a donor, to
CC produce fumihopaside A (PubMed:30977375). AfumC is also able to accept
CC UDP-D-galactose and UDP-D-glucuronic acid as donors to yield minor
CC derivatives (PubMed:30977375). Fumihopaside B, another minor derivative
CC produced, is different from fumihopaside A due to the presence of a
CC double bond between C-22 and C-29 (PubMed:30977375).
CC {ECO:0000269|PubMed:30977375}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30977375}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fumihopaside A.
CC {ECO:0000269|PubMed:30977375}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; DS499598; EDP50814.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y565; -.
DR SMR; B0Y565; -.
DR EnsemblFungi; EDP50814; EDP50814; AFUB_071550.
DR VEuPathDB; FungiDB:AFUB_071550; -.
DR HOGENOM; CLU_019345_0_0_1; -.
DR PhylomeDB; B0Y565; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
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; 2.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
PE 1: Evidence at protein level;
KW Isomerase; Repeat.
FT CHAIN 1..738
FT /note="Squalene hopane cyclase afumA"
FT /id="PRO_0000452738"
FT REPEAT 132..173
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 321..361
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 482..523
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 581..621
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 634..675
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 460
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 392
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 449
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 602
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 738 AA; 82164 MW; E3CDD5B9AAB6DE2F CRC64;
MLGAIREPPI DVQIALHSRD DNQTGLVLRG TRRTVDRVLK GLCSSPCFFC SVSLTMATLT
TTMATTATMA TTEASKPLEA QARTALTKAT NYAWEIFSNR HWCGELESNV TVTCEHIFFL
YVLYQHIDPG EGSQYRQWLL SQQNSDGSWG IAPNYPGDIS TSAEAYLALR IIGMSTDSPE
LYRARTFIRA AGGLSKMRMF TRIFFAEFGL VPWTAIPQLP AEFILVPAHF PISIYRLASW
ARSNVVPLLI IAHHRPLYPL PNGLHKQNPF LDELWLDPAT KPLPYGSSDP TDPVAFVFTI
LDKALSYLGG LRRSPTRGYA RRRCVQWILQ HQEKAGDWAG IIPPMHAGIK ALLLEGYKLH
DEPIQLGLAA IERFTWADNR GKRLQCCISP VWDTVLMIRA LQDTPASLGI KLDPRIADAL
AWTAENQHRG PEGDWRVYKP NIPVGGWAFE YHNTWYPDID DTAAAVLAFL THDPATARSR
LVRDAVLWIV GMQNADGGWA AFDHENNQLF LNKIPFSDME SLCDPSTPDV TGRTIECLGM
LRDLLMRPAE NAENGEKYGY PDGEGDAAAD AHLLQIINTA CARAIPYLIR SQEATGTWYG
RWAVNYVYGT CLVLCGLQYF KHDPKFAPEI QAMAARAVKW LKQVQNSDGG WGESLLSYRE
PWRAGCGPST PSQTAWALMG ILTVCGGEDR SVQRGVRHLV DTQDDTLSQG DGGAAAWTER
EFTIREPLHE ASQRIGSD
