(data stored in ACNUC16935 zone)

SWISSPROT: 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   05-JUL-2017, entry version 67.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community 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
RT   reducing end-specific xyloglucanobiohydrolase from Aspergillus
RT   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
RT   enzymes for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
CC   -!- FUNCTION: Oligoxyloglucan-reducing end-specific xyloglucanase
CC       involved in degradation of xyloglucans. Releases the first two
CC       glycosyl segments from oligoxyloglucans. Active against cotton
CC       xyloglucan, tamarind xyloglucan and tamarind xyloglucan oligomers
CC       (Probable). {ECO:0000305|PubMed:16214120,
CC       ECO:0000305|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of cellobiose from the reducing end
CC       of xyloglucans consisting of a beta-(1->4)-linked glucan carrying
CC       alpha-D-xylosyl groups on O-6 of the glucose residues. To be a
CC       substrate, the first residue must be unsubstituted, the second
CC       residue may bear a xylosyl group, whether further glycosylated or
CC       not, and the third residue, which becomes the new terminus by the
CC       action of the enzyme, is preferably xylosylated, but this xylose
CC       residue must not be further substituted.
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.
CC       {ECO:0000305}.
DR   EMBL; AACD01000025; EAA64249.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85075.1; -; Genomic_DNA.
DR   RefSeq; XP_659146.1; XM_654054.1.
DR   SMR; Q5BD38; -.
DR   STRING; 162425.CADANIAP00008169; -.
DR   CAZy; GH74; Glycoside Hydrolase Family 74.
DR   mycoCLAP; XBH74A_EMENI; -.
DR   EnsemblFungi; CADANIAT00008169; CADANIAP00008169; CADANIAG00008169.
DR   EnsemblFungi; EAA64249; EAA64249; AN1542.2.
DR   GeneID; 2875384; -.
DR   KEGG; ani:AN1542.2; -.
DR   HOGENOM; HOG000020380; -.
DR   InParanoid; Q5BD38; -.
DR   KO; K18651; -.
DR   OMA; NGRGIQY; -.
DR   OrthoDB; EOG092C1CTC; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled 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.
PE   1: Evidence at protein level;
DR   PRODOM; Q5BD38.
DR   SWISS-2DPAGE; Q5BD38.
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Complete proteome; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    810       Oligoxyloglucan-reducing end-specific
FT                                xyloglucanase.
FT                                /FTId=PRO_0000394077.
FT   REPEAT      126    135       BNR 1.
FT   REPEAT      226    236       BNR 2.
FT   REPEAT      359    369       BNR 3.
FT   REPEAT      554    564       BNR 4.
FT   REPEAT      617    626       BNR 5.
FT   REPEAT      658    667       BNR 6.
FT   REPEAT      705    716       BNR 7.
FT   REPEAT      759    769       BNR 8.
FT   ACT_SITE     66     66       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    498    498       Proton donor. {ECO:0000250}.
FT   CARBOHYD     32     32       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    188    188       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    298    298       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    312    312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    321    321       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    544    544       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    573    573       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    612    612       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    638    638       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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