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 03-AUG-2022, entry version 90.
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 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: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides (By
CC similarity). Not active on paranitrophenyl-alpha-galactoside and
CC raffinose. {ECO:0000250}.
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 -!- 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. {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; 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 AlphaFoldDB; Q5ARP5; -.
DR SMR; Q5ARP5; -.
DR STRING; 162425.CADANIAP00007818; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR PRIDE; Q5ARP5; -.
DR EnsemblFungi; CBF84419; CBF84419; ANIA_09035.
DR EnsemblFungi; EAA64367; EAA64367; AN9035.2.
DR GeneID; 2868244; -.
DR KEGG; ani:AN9035.2; -.
DR VEuPathDB; FungiDB:AN9035; -.
DR eggNOG; ENOG502QWG1; Eukaryota.
DR HOGENOM; CLU_009640_2_1_1; -.
DR InParanoid; Q5ARP5; -.
DR OMA; FNSWEAT; -.
DR OrthoDB; 472260at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled 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; 2.60.40.1180; -; 1.
DR Gene3D; 2.70.98.60; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Magnesium;
KW NAD; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..726
FT /note="Probable alpha-galactosidase G"
FT /id="PRO_0000395069"
FT ACT_SITE 485
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT ACT_SITE 547
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
