GEL1_ASPFC
ID GEL1_ASPFC Reviewed; 452 AA.
AC B0XT72; O74687; Q4WIP0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=1,3-beta-glucanosyltransferase gel1;
DE EC=2.4.1.-;
DE AltName: Full=Glucan elongating glucanosyltransferase 1;
DE Flags: Precursor;
GN Name=gel1; Synonyms=bgt2; ORFNames=AFUB_018250;
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], PROTEIN SEQUENCE OF 20-22; 29-47 AND
RP 349-363, AND FUNCTION.
RX PubMed=10809732; DOI=10.1074/jbc.275.20.14882;
RA Mouyna I., Fontaine T., Vai M., Monod M., Fonzi W.A., Diaquin M.,
RA Popolo L., Hartland R.P., Latge J.-P.;
RT "Glycosylphosphatidylinositol-anchored glucanosyltransferases play an
RT active role in the biosynthesis of the fungal cell wall.";
RL J. Biol. Chem. 275:14882-14889(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 PROTEIN SEQUENCE OF 36-38; 78-82; 240-242; 313-316 AND 378-389, AND
RP GPI-ANCHOR.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8900166; DOI=10.1074/jbc.271.43.26843;
RA Hartland R.P., Fontaine T., Debeaupuis J.-P., Simenel C., Delepierre M.,
RA Latge J.-P.;
RT "A novel beta-(1-3)-glucanosyltransferase from the cell wall of Aspergillus
RT fumigatus.";
RL J. Biol. Chem. 271:26843-26849(1996).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLU-160 AND GLU-261.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND 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.
CC {ECO:0000269|PubMed:10769178, ECO:0000269|PubMed:10809732,
CC ECO:0000269|PubMed:8900166}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. Active from pH 2.5 to 6.0.
CC {ECO:0000269|PubMed:8900166};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; AF072700; AAC35942.1; -; Genomic_DNA.
DR EMBL; DS499595; EDP53781.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XT72; -.
DR SMR; B0XT72; -.
DR EnsemblFungi; EDP53781; EDP53781; AFUB_018250.
DR VEuPathDB; FungiDB:AFUB_018250; -.
DR HOGENOM; CLU_021855_1_0_1; -.
DR PhylomeDB; B0XT72; -.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10809732"
FT CHAIN 20..419
FT /note="1,3-beta-glucanosyltransferase gel1"
FT /id="PRO_0000343198"
FT PROPEP 420..452
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343199"
FT REGION 325..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT BINDING 89
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 206
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 292
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 419
FT /note="GPI-like-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..100
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 215..345
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 233..264
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT MUTAGEN 160
FT /note="E->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:10769178"
FT MUTAGEN 261
FT /note="E->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:10769178"
FT CONFLICT 103
FT /note="A -> T (in Ref. 1; AAC35942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 48121 MW; 75266B9207488269 CRC64;
MKASAVTAAL AVGASTVLAA PSIKARDDVT PITVKGNAFF KGDERFYIRG VDYQPGGSSD
LADPIADADG CKRDIAKFKE LGLNTIRVYS VDNSKNHDEC MNALADAGIY LVLDVNTPKY
SINRAKPKES YNDVYLQYIF ATVDAFAGYK NTLAFFSGNE VINDGPSSSA APYVKAVTRD
LRQYIRSRKY REIPVGYSAA DIDTNRLQMA QYMNCGSDDE RSDFFAFNDY SWCDPSSFKT
SGWDQKVKNF TGYGLPLFLS EYGCNTNKRQ FQEVSSLYST DMTGVYSGGL VYEYSQEASN
YGLVEISGNN VKELPDFDAL KTAFEKTSNP SGDGNYNKTG GANPCPAKDA PNWDVDNDAL
PAIPEPAKKY MTEGAGKGPG FAGPGSQDRG TQSTATAEPG SGSATGSSSS GTSTSSKGAA
AGLTVPSLTM APVVVGAVTL LSTVFGAGLV LL
