ABND_EMENI
ID ABND_EMENI Reviewed; 383 AA.
AC Q5B8T6; C8VIS9; Q1HFU2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase D;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase D;
DE Short=ABN D;
DE Flags: Precursor;
GN Name=abnD; ORFNames=AN3044;
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].
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: 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: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF83510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA63615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490482; ABF50858.1; -; mRNA.
DR EMBL; AACD01000051; EAA63615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF83510.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_660648.1; XM_655556.1.
DR AlphaFoldDB; Q5B8T6; -.
DR SMR; Q5B8T6; -.
DR STRING; 162425.CADANIAP00010035; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PRIDE; Q5B8T6; -.
DR EnsemblFungi; EAA63615; EAA63615; AN3044.2.
DR GeneID; 2873991; -.
DR KEGG; ani:AN3044.2; -.
DR eggNOG; ENOG502RADR; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR InParanoid; Q5B8T6; -.
DR OrthoDB; 796026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell membrane; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal; Xylan degradation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..356
FT /note="Probable arabinan endo-1,5-alpha-L-arabinosidase D"
FT /id="PRO_0000394640"
FT PROPEP 357..383
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000394641"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT SITE 169
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"
FT LIPID 356
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 383 AA; 42055 MW; 32573F128157AE8A CRC64;
MVHITLPGLL LCLCLYLSVA PANPLNAHAR VSDTTAFPLP NEGHVVAHDP SIVRHHEHFY
LFKGGIHIPV FRASNLSGPW ERLGTVLNGP SLVQKQNQRR PWAPMVTQWK NRFYCFYSIS
QNGKRNSAIG VASSDSVEPG GWTDHGPLIN TGHGPGSGVY PFNVSNAIDP AFFADPITGQ
PYLQYGSYWK GIFQVPLAED LLSVENATHP NTDHLVFLPK KKPKPNEGVF MSYRAPYYYA
WFSHGQCCHF KTQGFPKEGN EYSIRVGRST SVHGPFVDRD NKDLLNGGGS VVYGSNHGKV
YAPGGLGVLP GANGEPDVLY YHYHNASIGF AQGDARLGWN YLDYVDGWPV PRAPSNPGNS
LQPPSSVSLQ IVAFLCLVIL FTL
