XGCA_EMENI
ID XGCA_EMENI Reviewed; 810 AA.
AC Q5BD38; C8VMX9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Oligoxyloglucan-reducing end-specific xyloglucanase;
DE Short=OREX;
DE EC=3.2.1.150;
DE Flags: Precursor;
GN Name=xgcA; ORFNames=AN1542;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16214120; DOI=10.1016/j.carres.2005.09.014;
RA Bauer S., Vasu P., Mort A.J., Somerville C.R.;
RT "Cloning, expression, and characterization of an oligoxyloglucan reducing
RT end-specific xyloglucanobiohydrolase from Aspergillus nidulans.";
RL Carbohydr. Res. 340:2590-2597(2005).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
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 (Probable).
CC {ECO:0000305|PubMed:16214120, ECO:0000305|PubMed:16844780}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH 3.0. {ECO:0000269|PubMed:16214120,
CC ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:16214120, ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family. {ECO:0000305}.
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DR EMBL; AACD01000025; EAA64249.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85075.1; -; Genomic_DNA.
DR RefSeq; XP_659146.1; XM_654054.1.
DR AlphaFoldDB; Q5BD38; -.
DR SMR; Q5BD38; -.
DR CAZy; GH74; Glycoside Hydrolase Family 74.
DR CLAE; XBH74A_EMENI; -.
DR EnsemblFungi; CBF85075; CBF85075; ANIA_01542.
DR EnsemblFungi; EAA64249; EAA64249; AN1542.2.
DR GeneID; 2875384; -.
DR KEGG; ani:AN1542.2; -.
DR VEuPathDB; FungiDB:AN1542; -.
DR eggNOG; ENOG502SJCI; Eukaryota.
DR HOGENOM; CLU_004180_1_0_1; -.
DR InParanoid; Q5BD38; -.
DR OMA; FGWWIQA; -.
DR OrthoDB; 266453at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033945; F:oligoxyloglucan reducing-end-specific cellobiohydrolase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010411; P:xyloglucan metabolic process; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..810
FT /note="Oligoxyloglucan-reducing end-specific xyloglucanase"
FT /id="PRO_0000394077"
FT REPEAT 126..135
FT /note="BNR 1"
FT REPEAT 226..236
FT /note="BNR 2"
FT REPEAT 359..369
FT /note="BNR 3"
FT REPEAT 554..564
FT /note="BNR 4"
FT REPEAT 617..626
FT /note="BNR 5"
FT REPEAT 658..667
FT /note="BNR 6"
FT REPEAT 705..716
FT /note="BNR 7"
FT REPEAT 759..769
FT /note="BNR 8"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 810 AA; 87098 MW; EDAC0B7B4CE061EA CRC64;
MRAKNGPGSW LALTAIATSL NTLALAAAKT INHSYEFNPV VVSGGGYITG IIAHPTEKNL
LYARTDIGGT YRWNADEDKW IPLNDFISGA DENLLGTESV ALDPNDPDRL YLAQGRYLNS
ENSAFFVSQD RGATFDVYPA PFKMGANELG RNNGERLAVN PFKTDELWMG TRDAGLMVSE
DGAQTWRNVS GFPQANANGI GIYWVIFDPR SEGTVYVGVG VPGGIYVTRD SGESWEAVPG
QPVEWDEDIL VFPAESQPQS TGPQPMKGVL AENGALYVTY ADAPGPYGVT YGGVYVYNTT
SSAWTNITPK TNNSFPAPFD NQTFPAGGFC GISVDSKNPE RLVVVSLDRD PGPALDSMYL
SHDGGKSWKD VSQLSTPSGS GGYWGHPIEE AAFKDGTAVP WLSFNWGPQW GGYGAPSPVR
GLTKFGWWMT AVVIDPSDSD HVLYGTGATI WATDNLSKVD KNQSPGWYIQ AQGIEESVAL
ALASPNGGDS HLLTGLGDIN GYRYGDLDVP QPMFDLPVLS NLNALDWAGQ KPEIIIRAGP
CGHNYTDGCG LAAYSADGGS SWTKFATCIP GINTSSSNPG VIAIDASGKD IVWSSAMTAY
WPTLQAITPR TNQSGPYVTT DLGQTWVSPT GLNVQTPNIS ADRVQPRTFY SFTDGTWYLS
RDGGLSYRAY KAKEVGLPAY SGALPIANFN RAGEIWLGLG DHGIYHTRNF GKKWTKITGR
GVTARQLTIG AGARRSSEPT LFIVGKAASH GALSKDGVYR SDDNGKTWVR VNDEKHQYGG
IAMIQGDPRV YGRVYLGTGG RGIIYADIKE
