(data stored in ACNUC16935 zone)

SWISSPROT: AGALG_EMENI

ID   AGALG_EMENI             Reviewed;         726 AA.
AC   Q5ARP5; C8VKR4; Q1HFQ4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 69.
DE   RecName: Full=Probable alpha-galactosidase G;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase G;
GN   Name=aglG; ORFNames=AN9035;
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].
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 (By similarity). Not active on paranitrophenyl-
CC       alpha-galactoside and raffinose. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family.
CC       {ECO:0000305}.
DR   EMBL; DQ490520; ABF50896.1; -; mRNA.
DR   EMBL; AACD01000168; EAA64367.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF84419.1; -; Genomic_DNA.
DR   RefSeq; XP_682304.1; XM_677212.1.
DR   ProteinModelPortal; Q5ARP5; -.
DR   SMR; Q5ARP5; -.
DR   STRING; 162425.CADANIAP00007818; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   EnsemblFungi; CADANIAT00007818; CADANIAP00007818; CADANIAG00007818.
DR   EnsemblFungi; EAA64367; EAA64367; AN9035.2.
DR   GeneID; 2868244; -.
DR   KEGG; ani:AN9035.2; -.
DR   HOGENOM; HOG000170018; -.
DR   InParanoid; Q5ARP5; -.
DR   KO; K07407; -.
DR   OMA; VKEINLM; -.
DR   OrthoDB; EOG092C0NDW; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   Pfam; PF02065; Melibiase; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q5ARP5.
DR   SWISS-2DPAGE; Q5ARP5.
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Magnesium; NAD; Polysaccharide degradation;
KW   Reference proteome; Secreted.
FT   CHAIN         1    726       Probable alpha-galactosidase G.
FT                                /FTId=PRO_0000395069.
FT   ACT_SITE    485    485       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    511    511       Proton donor. {ECO:0000250}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    166    166       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    657    657       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    673    673       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   726 AA;  80682 MW;  5923C95FB42AA7C1 CRC64;
     MTNSKARYVL EPVQVTGTTF ALNGTTLSYQ FHVDEPSADL RSDHFGGSIS GPIPVDPEPI
     VDGWTGMPDR VRREFPDQGR GDFRVPAFRI RQAEGHTVSA FRYREHEIVP GKEVSASGLP
     GVFGDAHDAT TLIVRLVDPY SDLAAELKYT VFPKYDTVVR SASITNKSNS DVTIESLASL
     SVDFPFDELE MIGLRGDWAR EAHRLRRKVD YGVQSFGSTT GFSSHLHNPF VALVHPSTTE
     SQGEAWGFSL IYSGSFTINV EKSSQGLTRV SIGPSQLSWT LKPGETFDSP ECVAVYSSTG
     IGGMSRSLHG LYRKHLMKSK FATEDRPVLL NSWEGLYFHI DQDRMYRLAQ EAAALGVKLL
     VMDDGWFGDE HPRTSDDAGL GDWIPNPARF PDGLTPLVNR ITALKVANSQ RNMRFGIWVE
     PEMVNPRSTL YQQHPDWVLH AGNYPRTEQR NQLVLNMSLP EVQEFIISAM SEILNAADIT
     YVKWDHNRGL AETPSPCANH AYMLGAYRVF DVLTTRFPNV IWEGCASGGG RFDPGILQYF
     PQVWTSDDSD AVERIFIQFG TSLAYPASAM GGHISSVPNH QTGRTTPLTF RAHVAMMCGS
     FGLELDPAHL TDSERRDIPG LIALAEKISP IVVKGDLWRL ALPEDSNWPA ALFLSENRTQ
     GVLFFFQLAP MVNHSLPRVR LQGLEDGALY RVDGEGPYSG SMLMNLGLQY SFRGDYGSRL
     AFIERE
//

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