AXHA2_EMENI
ID AXHA2_EMENI Reviewed; 325 AA.
AC Q5AUX2; C8V4U9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Alpha-L-arabinofuranosidase axhA-2;
DE EC=3.2.1.55;
DE AltName: Full=Arabinoxylan arabinofuranohydrolase axhA-2;
DE Flags: Precursor;
GN Name=axhA-2; ORFNames=AN7908;
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=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: Alpha-L-arabinofuranosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. Releases L-arabinose from arabinoxylan (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.4. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 47 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family. {ECO:0000305}.
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DR EMBL; AACD01000135; EAA59562.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73503.1; -; Genomic_DNA.
DR RefSeq; XP_681177.1; XM_676085.1.
DR PDB; 5UBJ; X-ray; 1.70 A; A=1-325.
DR PDBsum; 5UBJ; -.
DR AlphaFoldDB; Q5AUX2; -.
DR SMR; Q5AUX2; -.
DR CAZy; GH62; Glycoside Hydrolase Family 62.
DR EnsemblFungi; CBF73503; CBF73503; ANIA_07908.
DR EnsemblFungi; EAA59562; EAA59562; AN7908.2.
DR GeneID; 2869048; -.
DR KEGG; ani:AN7908.2; -.
DR VEuPathDB; FungiDB:AN7908; -.
DR eggNOG; ENOG502QUZT; Eukaryota.
DR HOGENOM; CLU_041805_0_0_1; -.
DR InParanoid; Q5AUX2; -.
DR OMA; STYRWNS; -.
DR OrthoDB; 814559at2759; -.
DR BRENDA; 3.2.1.55; 517.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:UniProtKB.
DR GO; GO:0019566; P:arabinose metabolic process; IDA:UniProtKB.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631; PTHR40631; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..325
FT /note="Alpha-L-arabinofuranosidase axhA-2"
FT /id="PRO_0000393537"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 59..71
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5UBJ"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5UBJ"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 112..130
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:5UBJ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5UBJ"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 234..246
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 252..264
FT /evidence="ECO:0007829|PDB:5UBJ"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5UBJ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:5UBJ"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:5UBJ"
SQ SEQUENCE 325 AA; 35560 MW; CD0DC28566CB8064 CRC64;
MRNLSTWPTF AALLWSAPRV LAQCGLPSTY SWTSTGPLAE PKDGWASLKD FTAVPYNGQY
LVYATYHDTG TSWGSMNFGL FSNWSDMATA SQNAMTQSTV APTLFYFEPK DVWILAYQWG
PTAFSYLTSS DPTDANGWSS PQPLFSGSIS DSDTGVIDQT VIGDSTTMYL FFAGDNGRIY
RASMPIDQFP GDFGTESEII LSDERNNLFE AVQVYTVSGQ SKDTYLMIVE AIGAQGRYFR
SFTADSLGGS WTPQAATESA PFAGKANSGA TWTDDISHGD LVRSTPDQTM SIDPCNLQLL
YQGRDPSLNP GYDLLPYRPG LLTLK
