GenomeNet

Database: UniProt
Entry: A2QN51_ASPNC
LinkDB: A2QN51_ASPNC
Original site: A2QN51_ASPNC 
ID   A2QN51_ASPNC            Unreviewed;      1009 AA.
AC   A2QN51;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   16-JAN-2019, entry version 79.
DE   SubName: Full=Aspergillus niger contig An07c0100, genomic contig {ECO:0000313|EMBL:CAK48192.1};
DE            EC=3.2.1.23 {ECO:0000313|EMBL:CAK48192.1};
GN   ORFNames=An07g04420 {ECO:0000313|EMBL:CAK48192.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK48192.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G., Debets A.J., Dekker P., van Dijck P.W., van Dijk A.,
RA   Dijkhuizen L., Driessen A.J., d'Enfert C., Geysens S., Goosen C.,
RA   Groot G.S., de Groot P.W., Guillemette T., Henrissat B., Herweijer M.,
RA   van den Hombergh J.P., van den Hondel C.A., van der Heijden R.T.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J., Meulenberg R.,
RA   Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M.,
RA   Pal K., van Peij N.N., Ram A.F., Rinas U., Roubos J.A., Sagt C.M.,
RA   Schmoll M., Sun J., Ussery D., Varga J., Vervecken W.,
RA   van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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; AM270128; CAK48192.1; -; Genomic_DNA.
DR   ProteinModelPortal; A2QN51; -.
DR   STRING; 5061.CADANGAP00005602; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; A2QN51; -.
DR   EnsemblFungi; CAK48192; CAK48192; An07g04420.
DR   HOGENOM; HOG000181922; -.
DR   Proteomes; UP000006706; Chromosome 4L.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006706};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888,
KW   ECO:0000313|EMBL:CAK48192.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:CAK48192.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT   DOMAIN      415    577       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  111421 MW;  81EFC5F0980D3EBB CRC64;
     MEHIGPASFP IRILNSSVSS DSKIDSISLA RLRLPLLLKF VVALTSLCQA LSVSNTSTGS
     VTWDEYSLLI NGERAFINAA EFHYQRLPVP EMWLDVLQKL KANGFNTISV YFFWSYHSAS
     KDAYDFKTGA HNIQRLFDMA KQAGLWVIAR PGPYVNAQTN AGGLALWGSD GSMGKLRTSD
     EAFHQAWLPY MRKVGQIIAA NQITRGGPVI LCQVENELQE TTHEPNNTLV TYMEQLEAVI
     RDAGITVPTT HNEKGMRYVS WSRDYGNVGG AVDIYGLDTY PAGFLVGNRC DGATGFNVFR
     TYYQWFMNYS WTGPIYLAEF EGGRTLTWGA PQNYDDCRSE HSTTFVDIYY KNNIGQRVTL
     QSIYEGYGGT NWGHSASPVA YTSNDYMTPL RETREQWAKL WQTKLIQLFS GSAPDLLKTY
     MYGNGSGYNT QATFTVLQQN ETPSTTTIAF SAYLNTSLGN MTVPDIQLQG RQSKILVTDY
     MFGNQTLLYS STDVLTNAIL PGHDVLALYL WEGQTGEFAL KTPRNLTLQV YGASIVSSTL
     HPGYQKIKYT QATGSTVLRF TNGVIVLLLD QPTAWHFWAP STSNYPSPRP DQKLFILGPY
     LVRSASVENE VLQVSGDNNG TTTLESFIGD VPIKAIEWNG QRLTATKTPY GSYTAQIPGT
     EHRSVNLPSL NHWRSADSLP EAQPGYDDSR WTVANKNSTL SPQAPLTLPV LFSSDYGYYA
     GAKIYRGYFD GTNHTAVNIT ASGGLAFGWN AWLNGHLIGG HTGDPNLSAT NMTLTLPGPH
     LRTMNNVITV IVDYHGHDET NIANGAGNPR GILGAYLLPG GTRTATGFKL WKIQGNAGGA
     KNIDPVRGPM NEGGLYAERL GWFLPGFPAS DNKEFNSTSS PLDGISKPGV RFYVTAFDLD
     IDRDLDAPIG VSFSAPNGTI ARVMLWVNGY QYGKYVPHIG PQTKFPVPPG IINNRGQNTL
     ALSLWAQTND GAKLDTVELF TYGLYQTDFQ FDRDWSYLQP GWEGRSVYA
//
DBGET integrated database retrieval system