GEL3_ASPFU
ID GEL3_ASPFU Reviewed; 544 AA.
AC P0C955; Q4X0N8; Q9P8U3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=AFUA_2G12850;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL93577.1; -; Genomic_DNA.
DR RefSeq; XP_755615.1; XM_750522.1.
DR AlphaFoldDB; P0C955; -.
DR SMR; P0C955; -.
DR STRING; 746128.CADAFUBP00002786; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR EnsemblFungi; EAL93577; EAL93577; AFUA_2G12850.
DR GeneID; 3513563; -.
DR KEGG; afm:AFUA_2G12850; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR InParanoid; P0C955; -.
DR OMA; AEYGCIE; -.
DR OrthoDB; 728071at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..512
FT /note="1,3-beta-glucanosyltransferase gel3"
FT /id="PRO_0000245551"
FT PROPEP 513..544
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245552"
FT REGION 471..501
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 512
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"
SQ SEQUENCE 544 AA; 57079 MW; C590CABC71A57974 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 GGGGGGGGGA AASTSTSKGA AAGAASPAAV RMGGWPLVTY GLVAAMAGIL
MISL
