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   24-JAN-2024, entry version 86.
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   STRING; 227321.Q5AUX2; -.
DR   CAZy; GH62; Glycoside Hydrolase Family 62.
DR   GlyCosmos; Q5AUX2; 1 site, No reported glycans.
DR   EnsemblFungi; CBF73503; CBF73503; ANIA_07908.
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; VNSWGAA; -.
DR   OrthoDB; 1772551at2759; -.
DR   BRENDA; 3.2.1.55; 517.
DR   Proteomes; UP000000560; Chromosome II.
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   InterPro; IPR005193; GH62_arabinosidase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   Pfam; PF03664; Glyco_hydro_62; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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
//