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Entry: Q5AX28
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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   29-OCT-2014, entry version 52.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   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
RT   enzymes 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as
CC       well as more complex molecules such as oligosaccharides and
CC       polysaccharides. Active on paranitrophenyl-alpha-galactoside but
CC       not on raffinose, locust bean gum and gum guar.
CC       {ECO:0000269|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
CC       galactose residues in alpha-D-galactosides, including galactose
CC       oligosaccharides, galactomannans and galactolipids.
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.
CC       {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};
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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   mycoCLAP; MEL27D_EMENI; -.
DR   EnsemblFungi; CADANIAT00000305; CADANIAP00000305; CADANIAG00000305.
DR   GeneID; 2870158; -.
DR   KEGG; ani:AN7152.2; -.
DR   eggNOG; NOG68897; -.
DR   HOGENOM; HOG000217283; -.
DR   InParanoid; Q5AX28; -.
DR   OrthoDB; EOG7CNZQQ; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:RefGenome.
DR   GO; GO:0046477; P:glycosylceramide catabolic process; IBA:RefGenome.
DR   GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IBA:RefGenome.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013780; Glyco_hydro_13_b.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_GHD.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02065; Melibiase; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    659       Alpha-galactosidase D.
FT                                /FTId=PRO_0000395075.
FT   REGION      201    205       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    156    156       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    223    223       Proton donor. {ECO:0000250}.
FT   CARBOHYD     48     48       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     86     86       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    183    183       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    438    438       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    450    450       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    484    484       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    551    551       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    583    583       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    125    158       {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
//
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