GEL2_ASPFC
ID GEL2_ASPFC Reviewed; 475 AA.
AC B0Y8H9; Q4WM30; Q9P8U4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=1,3-beta-glucanosyltransferase gel2;
DE EC=2.4.1.-;
DE AltName: Full=Glucan elongating glucanosyltransferase 2;
DE Flags: Precursor;
GN Name=gel2; ORFNames=AFUB_077400;
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}.
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DR EMBL; AF208039; AAF40139.1; -; Genomic_DNA.
DR EMBL; DS499599; EDP49710.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y8H9; -.
DR SMR; B0Y8H9; -.
DR Allergome; 8986; Asp f GT.
DR EnsemblFungi; EDP49710; EDP49710; AFUB_077400.
DR VEuPathDB; FungiDB:AFUB_077400; -.
DR HOGENOM; CLU_021855_1_2_1; -.
DR PhylomeDB; B0Y8H9; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..451
FT /note="1,3-beta-glucanosyltransferase gel2"
FT /id="PRO_0000372605"
FT PROPEP 452..475
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372606"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 87
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 159
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 160
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 201
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 294
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 451
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..98
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 215..350
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 234..265
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 475 AA; 51718 MW; AD974DE49CDF0A91 CRC64;
MLPTYVRLFT AVCALATTAS AVVPIEVKGK DFVNSKTGDR FQILGVDYQP GGSSGFTKDK
DPLSDPDACL RDAALMQRLG VNTIRIYNLS PSLNHDECAS IFNAAGIYMI LDVNSPLYGG
YLDRTDPEST YNDVYFKQVF GVIEAFKNFP NTLAFFAGNE VINEQSVKNV PTYVRAIQRD
MKDYIAKNLD RSIPVGYSAA DIRPILMDTL NYFMCADDAN SQSDFFGLNS YSWCGNSSYT
KSGYDVLTKD FADASIPVFF SEYGCNEVQP RYFSEVQALY GQEMTQSFSG GLVYEYTQEE
NDYGLVQIND NGTVTLLVDY DNLMAQYSKL DMSRIQASNT TQTSAKPPKC ESSLITNSTF
TDSFDLPKRP SKVQTMIDKG LSDANTGKLV EVKNTDIKQK IYNANGEEIT GIKLSILASG
ESNTPGAHSS GSTSGSSSSG GSSSSSSDKE SAAGTISVPF VGLLSAASFM AFFML
