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   24-JAN-2024, entry version 84.
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   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GlyCosmos; Q5B8T6; 4 sites, No reported glycans.
DR   GeneID; 2873991; -.
DR   KEGG; ani:AN3044.2; -.
DR   eggNOG; ENOG502RADR; Eukaryota.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   InParanoid; Q5B8T6; -.
DR   OrthoDB; 2655644at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   CDD; cd18831; GH43_AnAbnA-like; 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   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF5; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE D-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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
//