AGALD_EMENI
ID AGALD_EMENI Reviewed; 659 AA.
AC Q5AX28; C8VD73; Q1HFR9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-galactosidase D;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase D;
DE Flags: Precursor;
GN Name=aglD; ORFNames=AN7152;
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], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC Active on paranitrophenyl-alpha-galactoside but not on raffinose,
CC locust bean gum and gum guar. {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 52 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF78972.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA61404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ490505; ABF50881.1; -; mRNA.
DR EMBL; AACD01000122; EAA61404.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001304; CBF78972.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_664756.1; XM_659664.1.
DR AlphaFoldDB; Q5AX28; -.
DR SMR; Q5AX28; -.
DR STRING; 162425.CADANIAP00000305; -.
DR CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR CLAE; MEL27D_EMENI; -.
DR EnsemblFungi; EAA61404; EAA61404; AN7152.2.
DR GeneID; 2870158; -.
DR KEGG; ani:AN7152.2; -.
DR VEuPathDB; FungiDB:AN7152; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_0_1; -.
DR InParanoid; Q5AX28; -.
DR OrthoDB; 964130at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..659
FT /note="Alpha-galactosidase D"
FT /id="PRO_0000395075"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..158
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 71482 MW; F7D5BC5D10F6ECAB CRC64;
MRALVPMVVA ATALASPAPA LKPRLDDGLA RTPQMGWNTY NQYNCFPNES IVHENAQALV
DTGLADLGYR YVTIDCGWGV EDRLPNGTIT WNPELFPQGF PAMGQYLHDL GLLFGVYGDS
GILLCGSPPN ITGSLYYEDI DARTFAEWGA DSLKYDNCYS DAATNYPNVN YAPSTSPHPR
FANMSRYIQA QDRDILFQVC EWGIDFPALW APEIGHSWRI GNDIIPHWRS IFRTLNQAVP
QTDFAGPGQW PDLDMLLVGL DGVLTVPEEQ THFSLWSILK SPLTIGAAIP GMRAESLEIL
SNADVIAFNQ DALGVSAALR RRWSDEGYEV WSGPLEGGRT IAAVINWRDE DREITLDLPD
IGLQYAETLQ NVWADETVNG VKTSYSSVVE AHGVMLVQLA ETVEEGVYPA DVFAATNRDV
TTFSDVYAIT SSPNFVLNIT LTEVTAAATN ITIITDSSRR PISTSIPAGS SSISTSVSLI
AGSNNTITIR NAPPLSSITL SPPEPTYYTG AQDFTLTSPA GAYTCPDAYC LPAGSKIVDL
STESAATAHI NSSTSGSKYL EIDYINNEVA FDSSWGWGAN SRNLTIKVND NNPVRLEVPL
SGRHSELFGP GLGWWDSGRL GVLTDGWIKG TNELVLSNEG GEGGFTKYAP DVVGIAVYD
