ABNA_EMENI
ID ABNA_EMENI Reviewed; 322 AA.
AC Q5BA96; C8VPL6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase A;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase A;
DE Short=ABN A;
DE Flags: Precursor;
GN Name=abnA; ORFNames=AN2534;
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).
CC -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF87045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA64639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000043; EAA64639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF87045.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_660138.1; XM_655046.1.
DR AlphaFoldDB; Q5BA96; -.
DR SMR; Q5BA96; -.
DR STRING; 162425.CADANIAP00009262; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR EnsemblFungi; EAA64639; EAA64639; AN2534.2.
DR GeneID; 2875157; -.
DR KEGG; ani:AN2534.2; -.
DR VEuPathDB; FungiDB:AN2534; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR InParanoid; Q5BA96; -.
DR OrthoDB; 796026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..322
FT /note="Probable arabinan endo-1,5-alpha-L-arabinosidase A"
FT /id="PRO_0000394623"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT SITE 149
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000250|UniProtKB:P94522"
SQ SEQUENCE 322 AA; 34488 MW; 067FCEEC827BD29F CRC64;
MYLPTLAASA SLLVGVAHGY ASPGACSGAC NIHDPALIRR ESDGKYFRFS TGNKISYASA
SSIEGPWTAI GSVLPGGSSI DLDGNDDLWA PDVQLVNGVY YVLYSVSTFG SQNSAIGLAT
SDTMDLNTWT DHGSTGIRSD SSKPYNAIDG NLFQDDSGTW YMNFGSFWND IYQAQMKSPP
TAVASSSYQI AYQPAGEHAV EGAYLYKYGN YYYLFFSEGK CCGYDSSRPA TGEEYKIKVC
RSTTATGNFV DANGVSCTSG GGTIVLESHD NVYGPGGQGV FTDPTLGPVL YYHYVDTTIG
YADSQKLFGW NVLDFSSGWP VV
