XGCA_NEOFI
ID XGCA_NEOFI Reviewed; 815 AA.
AC A1DAU0;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Probable oligoxyloglucan-reducing end-specific xyloglucanase;
DE Short=OREX;
DE EC=3.2.1.150;
DE Flags: Precursor;
GN Name=xgcA; ORFNames=NFIA_096000;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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).
CC -!- FUNCTION: Oligoxyloglucan-reducing end-specific xyloglucanase involved
CC in degradation of xyloglucans. Releases the first two glycosyl segments
CC from oligoxyloglucans. Active against cotton xyloglucan, tamarind
CC xyloglucan and tamarind xyloglucan oligomers.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of cellobiose from the reducing end of xyloglucans
CC consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl
CC groups on O-6 of the glucose residues. To be a substrate, the first
CC residue must be unsubstituted, the second residue may bear a xylosyl
CC group, whether further glycosylated or not, and the third residue,
CC which becomes the new terminus by the action of the enzyme, is
CC preferably xylosylated, but this xylose residue must not be further
CC substituted.; EC=3.2.1.150;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027694; EAW19980.1; -; Genomic_DNA.
DR RefSeq; XP_001261877.1; XM_001261876.1.
DR AlphaFoldDB; A1DAU0; -.
DR SMR; A1DAU0; -.
DR EnsemblFungi; EAW19980; EAW19980; NFIA_096000.
DR GeneID; 4588332; -.
DR KEGG; nfi:NFIA_096000; -.
DR VEuPathDB; FungiDB:NFIA_096000; -.
DR eggNOG; ENOG502SJCI; Eukaryota.
DR HOGENOM; CLU_004180_1_0_1; -.
DR OMA; FGWWIQA; -.
DR OrthoDB; 266453at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033945; F:oligoxyloglucan reducing-end-specific cellobiohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR002860; BNR_rpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF02012; BNR; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..815
FT /note="Probable oligoxyloglucan-reducing end-specific
FT xyloglucanase"
FT /id="PRO_0000394078"
FT REPEAT 118..128
FT /note="BNR 1"
FT REPEAT 218..228
FT /note="BNR 2"
FT REPEAT 351..361
FT /note="BNR 3"
FT REPEAT 545..555
FT /note="BNR 4"
FT REPEAT 649..658
FT /note="BNR 5"
FT REPEAT 696..706
FT /note="BNR 6"
FT REPEAT 749..759
FT /note="BNR 7"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 489
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 815 AA; 87559 MW; 415A7F57CB93739B CRC64;
MKFWLQQLGL AVLCASSAAA RTAEHAYEFK SVAITGGGYI TGIVGHPAEK NLLYARTDIG
STYRWEQELN KWIPLTDFLG PEDENLLGTE SVAMDPTDPN RLYLAQGRYL SSNNSAFFVS
NDRGATFTRY RAPFPMGANE LGRNNGERLA VNPFKPNELW MGTRNAGLMK SSDRAKTWTN
VTNFPDAAAN GIGITFVIFD PQHEGTIYVG ACIPGGLYYT TDGGKNWESI PGQPMQWDPS
LLVYPNETQP QSAGPQPMKA VLASNGALYV TYADYPGPWG VAYGAVHVYN TTASIWTDIT
PNANNTSPKP YTPQAFPAGG YCGLSVAPDD PDTVVVVSLD RDPGPALDSM YLSRDGGKTW
KDVSQLSTPP GSGGYWGHPI AEAALSNGTT VPWLSFNWGP QWGGYGAPSP VKGLTKFGWW
MTAVLIDPSN PDHVLYGTGA TIWATDTIAQ ADKNLAPKWY IQAQGIEETV TLAMISPREG
AHLLSGAGDI NGFRHDDLDT PQPMFGLPVF SNLNTLDWAG QRPEVIVRGG PCGHQYPDGC
GQAAYSTDGG SEWTKFQTCI KGVNTSVHNP GVMTIDASGK YVVWTSAMYV VSPSVQAVTP
PANDSGPYAS SDWGKTWTSP RGLTVQTPYI SADRVQPKTF YAFSGGVWYV STDGGLSYDA
FNATKLGLPA HTGAVPVVSV DRAGEIWLAL GSNGVYHTTD FGKRWKRITH KGTVADLITV
GAAAPGSTKP ALFIRGSPGH PKKSDYGIYR SDDNGSTWDR VDDDDHRYGG FNLIQGDPRV
YGRVYLGTGG RGLLYADIVP GQSDKEGNVP GTGGI