ABFA_EMENI
ID ABFA_EMENI Reviewed; 565 AA.
AC Q5BA89; C8VPS5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Probable alpha-L-arabinofuranosidase A;
DE Short=ABF A;
DE Short=Arabinosidase A;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=abfA; ORFNames=AN2541;
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: Alpha-L-arabinofuranosidase involved in the degradation of
CC arabinoxylan, a major component of plant hemicellulose. Acts only on
CC small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR EMBL; AACD01000043; EAA64646.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF87061.1; -; Genomic_DNA.
DR RefSeq; XP_660145.1; XM_655053.1.
DR AlphaFoldDB; Q5BA89; -.
DR SMR; Q5BA89; -.
DR STRING; 162425.CADANIAP00009271; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR EnsemblFungi; CBF87061; CBF87061; ANIA_02541.
DR EnsemblFungi; EAA64646; EAA64646; AN2541.2.
DR GeneID; 2875725; -.
DR KEGG; ani:AN2541.2; -.
DR VEuPathDB; FungiDB:AN2541; -.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_1_1_1; -.
DR InParanoid; Q5BA89; -.
DR OMA; MFEEMDH; -.
DR OrthoDB; 366915at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; ISS:UniProtKB.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019566; P:arabinose metabolic process; ISS:UniProtKB.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 2.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..565
FT /note="Probable alpha-L-arabinofuranosidase A"
FT /id="PRO_0000394601"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 565 AA; 62771 MW; 18B9A9B5206AFBC3 CRC64;
MPLSAAIKSS LSVSVRADAK GLVGFANTGY NGITVLKQTY WTSFYMKGEY SGTVLLRLTG
TDSGTVYGSR NLSVKSTGGK WTQYETTFEA NESYVAENEW QLLFDAATAK GHPLHFGLVQ
LFPPTYKNRT NGLRNDIARP IADLKPKFLR FPGGNNIQAD RPGDWHYPNT DALGLDEYLW
WCEDMDMVPV LSVWDGKSYG GIVSGEELQP YLDDIKDELE VTLPLTLLSH PLRAYLTPNT
NEQYLLGPPS TPFGALRARN GHPDPWPIQY IEIGNEDDYS GGCDTYPDRL VQIYDTIHAS
YPNLTLIANN MDENCLPEIP LPGLWHDYHY YRSADDLVAM FNYWDNHDRG DRVLVGEYGC
RNDSNPDGVF WSFMQGSCAE AVHMIGLERN SDVVMMAAYA PLLQHFGYTQ WSVCTPSASL
AYLGIHPADR GEEQPTLFGF ESRPNSLTLS TSYYVNRMFS TNQGSTVHKV HSTAGFGPLY
WVATSNETAY QVKLANYGAA NQTVNIRVPG VGRGVLEMIS GPKDASNLPG DIKIVPVSRN
IRAGKEGYTV HMPPWGVAVL VVVFK