GEL3_ASPFC
ID GEL3_ASPFC Reviewed; 547 AA.
AC B0XT09; Q4X0N8; Q9P8U3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=1,3-beta-glucanosyltransferase gel3;
DE EC=2.4.1.-;
DE AltName: Full=Glucan elongating glucanosyltransferase 3;
DE Flags: Precursor;
GN Name=gel3; ORFNames=AFUB_028470;
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 [GENOMIC DNA].
RX PubMed=10769178; DOI=10.1042/bj3470741;
RA Mouyna I., Monod M., Fontaine T., Henrissat B., Lechenne B., Latge J.-P.;
RT "Identification of the catalytic residues of the first family of beta(1-
RT 3)glucanosyltransferases identified in fungi.";
RL Biochem. J. 347:741-747(2000).
RN [2]
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 [3]
RP STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. Involved in cell wall morphogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF40140.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF208040; AAF40140.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DS499595; EDP54787.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XT09; -.
DR SMR; B0XT09; -.
DR EnsemblFungi; EDP54787; EDP54787; AFUB_028470.
DR VEuPathDB; FungiDB:AFUB_028470; -.
DR HOGENOM; CLU_021855_2_1_1; -.
DR PhylomeDB; B0XT09; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042123; F:glucanosyltransferase activity; IEA:UniProt.
DR GO; GO:0071840; P:cellular component organization or biogenesis; IEA:UniProt.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:UniProt.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..515
FT /note="1,3-beta-glucanosyltransferase gel3"
FT /id="PRO_0000372607"
FT PROPEP 516..547
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372608"
FT REGION 471..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 154
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 155
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 197
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 202
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 289
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT LIPID 515
FT /note="GPI-like-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..97
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 211..343
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 229..260
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 366..419
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 375..443
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 394..401
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT CONFLICT 485
FT /note="G -> E (in Ref. 1; AAF40140)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Missing (in Ref. 1; AAF40140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 57218 MW; 76F1F2C6C09E31C3 CRC64;
MRYSLVVGVV LLSGCAIATG SKFFYANNGS EFYIRGVAYQ EDYSGGGAGG TGQSEANYVD
PLADGSKCER DIPYLLQLRT NVIRTYAVNP SLNHDACMQK LSDAGIYVIT DLASPDESIT
SNSPVWTVDQ YARYTSVIDA FQKYDNVIGF FAGNEVVNQA NQSAGAAFVK AAARDMKAYI
KTKGYRQSLA IGYATTDNPE IRLPLSDYLN CGDQADAVDF FGYNIYEWCG DKTFQTSGYQ
NRTEEYKDYS IPIFFSEYGC NTEKPRKFTD VPVLFGPQMD NVWSGGIVYM YFETTNDYGL
VSVSGSAVTP EPDFTYLSSE IQSATPTGVN SASYSPTNSP RACPTVDDTW LAKSSPLPPI
PNAELCSCMV SSLSCVVKDS VDAEKYGELF GQVCGYGGGI CDGIARNATA GSYGAYSVCT
SKDQLSYVFD RYYKSQKKAA SACDFAGAAS VQSPKGESAD CKSLVSQAGS AGTGTVTSQP
TGGSGSTGGG GGGGGGGGGG GGAAASTSTS KGAAAGAASP AAVRVGGWPL VTYGLVAAMA
GILMISL
