GEL4_ASPFC
ID GEL4_ASPFC Reviewed; 548 AA.
AC B0XVI5; Q4WHH9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=1,3-beta-glucanosyltransferase gel4;
DE EC=2.4.1.-;
DE AltName: Full=Glucan elongating glucanosyltransferase 4;
DE Flags: Precursor;
GN Name=gel4; ORFNames=AFUB_022370;
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 [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 [2]
RP PROTEIN SEQUENCE OF 142-153; 207-218 AND 443-452, AND 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 [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; 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; DS499595; EDP54185.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XVI5; -.
DR SMR; B0XVI5; -.
DR EnsemblFungi; EDP54185; EDP54185; AFUB_022370.
DR HOGENOM; CLU_021855_2_1_1; -.
DR PhylomeDB; B0XVI5; -.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..519
FT /note="1,3-beta-glucanosyltransferase gel4"
FT /id="PRO_0000372609"
FT PROPEP 520..548
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372610"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 106
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 133..141
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 174
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 175
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 217
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 222
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 309
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 519
FT /note="GPI-like-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..117
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 231..364
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 249..280
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 386..437
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 395..461
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 414..419
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 548 AA; 58873 MW; 191DA9A1D29778FE CRC64;
MKFVYAAAGA SLVGSALATL PVIEAKVLKA CCWTIALDAN SYGNKFFYSN NGTEFFIRGV
AYQQEYQANG TSTENSDYTD PLANVDNCKR DIPYLKQLRT NVIRTYAVDP TKDHDECMKL
LDDAGIYLIT DLSAPSESIN RADPAWNTDL YKRYTSVIDA FAKYSNVIGF FAGNEVANDN
NNTNSIAYVK AAVRDMKSYI KSKDYRSSLL VGYATDDDAH IRADLADYLV CGDKESSIDM
FGYNIYEWCG DSSFEKSGYK DRTEEFSKYP VPAFFSEYGC IDPKPRKFTD VAALYGPQMN
DVWSGGIVYM YFQEANDYGL VSVSGDNVKT KEDFSYLSVQ MQKVTATGVN SASYTASNTA
VPTCPSVGAK WEASNKLPPS PNSELCDCMV ETLSCTVKDS VDEKEYGDLF DYLCAAGVCG
GINSNSTSGD YGAYSVCSAK QKLSFVMNQY YKKNNKAATA CDFDGKAQTK KGADASGSCA
SLISQAGTAG TGSVTAGATG SSGSGSASET SKGAAGVAAS PMAVKVGNWQ FGAYIATALF
AGVGMLVL
