GEL1_ASPFU
ID GEL1_ASPFU Reviewed; 452 AA.
AC P0C7S9; O74687; Q4WIP0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=AFUA_2G01170;
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:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
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; AAHF01000008; EAL87215.1; -; Genomic_DNA.
DR RefSeq; XP_749253.1; XM_744160.1.
DR AlphaFoldDB; P0C7S9; -.
DR SMR; P0C7S9; -.
DR STRING; 746128.CADAFUBP00001780; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR EnsemblFungi; EAL87215; EAL87215; AFUA_2G01170.
DR GeneID; 3506970; -.
DR KEGG; afm:AFUA_2G01170; -.
DR VEuPathDB; FungiDB:Afu2g01170; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; P0C7S9; -.
DR OMA; MFAKYDN; -.
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; IDA:AspGD.
DR GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:AspGD.
DR GO; GO:0042123; F:glucanosyltransferase activity; IDA:AspGD.
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 GO; GO:0031505; P:fungal-type cell wall organization; ISA:AspGD.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..419
FT /note="1,3-beta-glucanosyltransferase gel1"
FT /id="PRO_0000245547"
FT PROPEP 420..452
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245548"
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:0000250"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 452 AA; 48077 MW; 017169E2BCDCB66E CRC64;
MKASAVTAAL AVGASTVLAA PSIKARDDVT PITVKGNAFF KGAERFYIRG 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
