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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}.
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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
 
 
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