FKS1_ASPNC
ID FKS1_ASPNC Reviewed; 1897 AA.
AC A2QLK4; Q5DRK6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=1,3-beta-glucan synthase component FKS1;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
GN Name=fksA {ECO:0000303|PubMed:15670714};
GN Synonyms=fks1 {ECO:0000250|UniProtKB:P38631}; ORFNames=An06g01550;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1] {ECO:0000312|EMBL:CAK47999.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAS37661.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1133-1254.
RC STRAIN=ATCC 9089 / N402 {ECO:0000312|EMBL:AAS37661.1};
RX PubMed=15670714; DOI=10.1016/j.fgb.2004.11.006;
RA Damveld R.A., van Kuyk P.A., Arentshorst M., Klis F.M.,
RA van den Hondel C.A.M.J.J., Ram A.F.;
RT "Expression of agsA, one of five 1,3-alpha-D-glucan synthase-encoding genes
RT in Aspergillus niger, is induced in response to cell wall stress.";
RL Fungal Genet. Biol. 42:165-177(2005).
CC -!- FUNCTION: Catalytic subunit of the 1,3-beta-glucan synthase.
CC Synthesizes 1,3-beta-glucan, a major structural component of the cell
CC wall. Involved in cell wall synthesis, maintenance and cell wall
CC remodeling (By similarity). {ECO:0000250|UniProtKB:P38631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBUNIT: Component of the 1,3-beta-glucan synthase, composed of at
CC least catalytic subunit fksA, and a regulatory subunit.
CC {ECO:0000250|UniProtKB:P38631}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cell membrane
CC {ECO:0000250|UniProtKB:P38631, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P38631, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000255}.
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DR EMBL; AM270115; CAK47999.1; -; Genomic_DNA.
DR EMBL; AY533027; AAS37661.1; -; Genomic_DNA.
DR RefSeq; XP_001390977.1; XM_001390940.2.
DR AlphaFoldDB; A2QLK4; -.
DR DrugBank; DB00362; Anidulafungin.
DR DrugBank; DB00520; Caspofungin.
DR DrugBank; DB01141; Micafungin.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR PaxDb; A2QLK4; -.
DR EnsemblFungi; CAK47999; CAK47999; An06g01550.
DR GeneID; 4981154; -.
DR KEGG; ang:ANI_1_188054; -.
DR VEuPathDB; FungiDB:An06g01550; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 8ER.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Mitochondrion; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1897
FT /note="1,3-beta-glucan synthase component FKS1"
FT /id="PRO_0000322581"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1386..1406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1473..1493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1497..1517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1588..1608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1630..1650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1666..1686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1701..1721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1766..1786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1826..1846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1897 AA; 216975 MW; 083DB5C85CF51E15 CRC64;
MSGYPAGHYE DGYGHQEHGG DAYYQDEHGQ AYYDPNDYGD SYYDRGNYYN AEGGQAYGQE
GGYYDAGHQD DYYGDQYYDQ GNGAPRGRRR GDSEEDSETF SDFTMRSETA RAADMDYYGR
GDERYNSYAD SQYAGRGYNG YRPPSSQVSY GANRSSGAST PVYGMDYGSA LPGGPRSREP
YPAWASDGQV PVSKEEIEDI FIDLVNKFGF QRDSMRNMYD HLMTQLDSRA SRMTPNQALL
SLHADYIGGD NANYRRWYFA AHLDLDDAVG FANMKLGKAD RKTRKARKAA KAAAQQNPEN
VEENLEAMEG DNSLEAAVYR WKSRMNRMSP HDRVRQLALY MLCWGEANQV RYMPECICFI
FKCADDYYSS PECQSRVEPV EEFTYLNEII TPLYQFCRDQ GYEILDGKYV RRERDHEKII
GYDDMNQLFW YPEGIERISF EDKTRLVDVP PAERWTKLKD VDWKKAFFKT YRETRSWFHM
ITNFNRIWVI HLGAFWFFTA YNAPTLYTKN YQQQLDNKPA GSKYWSAVGF GGALVGLIQI
LATLCEWMYV PRRWAGAQHL SKRLMFLIAV FIVNLAPGVV VFGFNNVLSE TICLIIGIVH
FFIALATFFF FSVMPLGGLF GSYLKKHGRQ YVASQTFTAS YPRLNGNDMW MSYGLWICVF
GAKLVESYFF LTLSLKDPMR ILSPMRIHQC AGVTYIPNSL CHAQPQILLG LMMFMDLTLF
FLDSYLWYVI CNTIFSVARS FYLGVSIWSP WRNIFSRLPK RIYSKVLATT DMEIKYKPKV
LISQVWNAII ISMYREHLLA IDHVQKLLYH QVPSEQEGKR TLRAPTFFVS QEDQSFKTEF
FPAGSEAERR ISFFAQSVAT PMPEPLPVDN MPTFTVLIPH YGEKILLSLR EIIREDEPYS
RVTLLEYLKQ LHPHEWDCFV KDTKILADET SQLNGEPEKN EKDAQKSKID DLPFYCIGFK
SAAPEYTLRT RIWSSLRSQT LYRTISGFMN YSRAIKLLYR VENPEVVQMF GGNSEKLERE
LERMARRKFK ICVSMQRYAK FNKEERENTE FLLRAYPDLQ IAYLDEEPPA NEGEEPRLYS
ALIDGHCELL DNGMRKPKFR IQLSGNPILG DGKSDNQNHS IIFYRGEYIQ VIDANQDNYL
EECLKIRSVL AEFEELTTDN VSPYTPGIAT EAETPVAILG AREYIFSENV GVLGDVAASK
EQTFGTLFAR TLAQIGGKLH YGHPDFLNGI FMTTRGGISK AQKGLHLNED IYAGMTALCR
GGRIKHCEYF QCGKGRDLGF GSILNFTTKI GTGMGEQMLS REYYYLGTQL PLDRFLSFYY
AHPGFHLNNM FIMLSVQMFM IVLINLGALK HETITCRYNS NLPITDPLRP TYCADLTPII
AWVNRCVVSI FIVFFISFVP LAVQELTERG LWRMATRLAK HFGSFSFMFE VFVCQIYANA
VHQNLSFGGA RYIGTGRGFA TARIPFGVLY SRFAGPSIYA GSRLLLMLLF ATSTVWTPAL
IWFWVSLLAL CISPFLFNPH QFAWHDFFID YRDYIRWLSR GNSRSHASSW IAFCRLSRTR
LTGYKRKLLG VPSEKGSGDV PRAKFTNIFF SEIIAPLVQV AVTLVPYLYI NSRTGISNDN
ERASNAVVRI AIVAFGPIGV NAGVSGMFFG MACCMGPIFG MCCKKFGAVL AAIAHAIAVI
ILLVIFEVMF FLESWSWPRM VLGMISAAAI QRFIYKLIIS LALTREFKHD QSNIAWWTGK
WYNMGWHSLS QPGREFLCKI TELGYFSADF VLGHILLFVM LPALCIPYVD KFHSVILFWL
RPSRQIRPPI YSLKQSKLRK RRVVRFAILY FTMLVLFLIL LIAPLVARDE GISVNLNIMS
LMQPLDTDNN DTISSYTGNG LPVGYSAWTP SAASASA
