GenomeNet

Database: UniProt
Entry: BGALB_EMENI
LinkDB: BGALB_EMENI
Original site: BGALB_EMENI 
ID   BGALB_EMENI             Reviewed;        1025 AA.
AC   Q5BEQ0; C8VU89;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 86.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=AN0980;
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 [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   [2]
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: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF88404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA66009.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACD01000014; EAA66009.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF88404.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_658584.1; XM_653492.1.
DR   ProteinModelPortal; Q5BEQ0; -.
DR   SMR; Q5BEQ0; -.
DR   STRING; 162425.CADANIAP00001672; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   EnsemblFungi; EAA66009; EAA66009; AN0980.2.
DR   GeneID; 2876757; -.
DR   KEGG; ani:AN0980.2; -.
DR   HOGENOM; HOG000181922; -.
DR   InParanoid; Q5BEQ0; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1025       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395229.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    308    308       Nucleophile. {ECO:0000255}.
FT   BINDING      90     90       Substrate. {ECO:0000250}.
FT   BINDING     135    135       Substrate. {ECO:0000250}.
FT   BINDING     136    136       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     137    137       Substrate. {ECO:0000250}.
FT   BINDING     195    195       Substrate. {ECO:0000250}.
FT   BINDING     265    265       Substrate. {ECO:0000250}.
FT   BINDING     373    373       Substrate. {ECO:0000250}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    411    411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    736    736       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    776    776       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    884    884       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    925    925       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    926    926       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    324       {ECO:0000250}.
SQ   SEQUENCE   1025 AA;  112791 MW;  042F7E48B07F2BD4 CRC64;
     MATAFWLLLF LLGSLHVLTA AQNSSQSEWP IHDNGLSKVV QWDHYSFYIN GQRIFLFSGE
     FHYWRIPVPA LWRDILEKIK AIGFTGFAFY SSWAYHAPNN QTVDFSTGAR DITPIYDLAK
     ELGMYIIVRP GPYVNAEASA GGFPLWLTTG AYGSTRNDDP RYTAAWEPYF AEVSEITSKY
     QVTDGHYTLC YQIENEYGQQ WIGDPRDRNP NQTAIAYMEL LQASARENGI TVPLTGNDPN
     MNTKSWGSDW SDAGGNLDTV GLDSYPSCWS CDVSVCTGTN GEYVPYKVLD YYDYFQEVQP
     TMPFFMPEFQ GGSYNPWDGP EGGCTEDTGA DFANLFYRWN IGQRVSAMSL YMMFGGTNWG
     GIAAPVTASS YDYSAPISED RSIGSKYYET KLLALFTRCA KDLTMTDRLG NGTQYTDNEA
     VIASELRNPD TNAAFYVTTH LDTTVGTDES FKLHVNTSKG ALTIPRHGGT IRLNGHHSKI
     IVTDFNFGSE TLLYSTAEVL TYAVFDRKPT LVLWVPTGES GEFAIKGAKS GSVAKCSGCS
     NIKFHRDSGS LTVAFTQGEG ISVLQLDNGV RVVLLDRQKA YTFWAPALTD NPLVPEGESV
     LVSGPYLVRT ARLARSTLTL RGDSKGETLE IFAPRKIKKV TWNGKAVEAT RTSYGSLKAI
     LAKPPSVELP TLNGWKYSDS LPERFPTYDD SGAAWVEIDA NHMTTPNPNK PATLPVLYAD
     EYGFHNGVRL WRGYFNSSAS GVYLNIQGGA AFGWSAWLNG HFLGSHLGSA SIQQANGTLD
     FPANTLNTEG TPNVLLVVHD DTGHDQTTGV LNPRGILEAR LLSEASDNND DDSPGFTHWR
     VAGTAGGESD LDPVRGVYNE DGLYAERVGW HLPGFDDSKW ATVNGTSLSF TGATVRFFRT
     VIPPLSIPEN TDVSISFVFS TPNVNNTSAG NTSAFRAQLF VNGYQYGRYN PYVGNQVVYP
     VPPGILDYNG ENTIGVAVWA QTEAGARLNL DWRVNYVLGS SLDAGRLDLS FVAIAYVYIF
     ECLQL
//
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