XGEA_EMENI
ID XGEA_EMENI Reviewed; 239 AA.
AC Q5BG78; C8VT79; Q1HFV8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase A;
DE EC=3.2.1.151;
DE AltName: Full=Xyloglucanase A;
DE AltName: Full=Xyloglucanendohydrolase A;
DE Flags: Precursor;
GN Name=xgeA; ORFNames=AN0452;
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 [MRNA], 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).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in
CC xyloglucan with retention of the beta-configuration of the glycosyl
CC residues. Specific for xyloglucan and does not hydrolyze other cell
CC wall components. Active against tamarind xyloglucan.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 47 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {ECO:0000305}.
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DR EMBL; DQ490466; ABF50842.1; -; mRNA.
DR EMBL; AACD01000007; EAA66551.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89457.1; -; Genomic_DNA.
DR RefSeq; XP_658056.1; XM_652964.1.
DR AlphaFoldDB; Q5BG78; -.
DR SMR; Q5BG78; -.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR CLAE; XEG12A_EMENI; -.
DR EnsemblFungi; CBF89457; CBF89457; ANIA_00452.
DR EnsemblFungi; EAA66551; EAA66551; AN0452.2.
DR GeneID; 2876228; -.
DR KEGG; ani:AN0452.2; -.
DR VEuPathDB; FungiDB:AN0452; -.
DR eggNOG; ENOG502RW43; Eukaryota.
DR HOGENOM; CLU_051064_0_1_1; -.
DR OMA; KSLPSVW; -.
DR OrthoDB; 1236368at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase 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; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..239
FT /note="Xyloglucan-specific endo-beta-1,4-glucanase A"
FT /id="PRO_0000394075"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 25150 MW; 6E3EA90EC366AC34 CRC64;
MKLLALSLAS LASAATITRR ADFCGQWDTA TAGNFIVYNN LWGQDNADSG SQCTGVDSAN
GNSVSWHTTW SWSGGSSSVK SYANAAYQFT ATQLSSLSSI PSTWEWQYST TDVVANVAYD
LFTSSSIGGD SEYEIMIWLA ALGGAGPISS TGSSIATVTL GGVTWNLYSG PNGSMQVYSF
VASSTTESFS ADLMDFINYL VENQGLSNSQ YLTHVQAGTE PFTGSDATLT VSSYSVSVS
