GenomeNet

Database: UniProt
Entry: BGALA_EMENI
LinkDB: BGALA_EMENI
Original site: BGALA_EMENI 
ID   BGALA_EMENI             Reviewed;        1007 AA.
AC   Q5BFC4; C8VQX7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 87.
DE   RecName: Full=Probable beta-galactosidase A;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase A;
DE   Flags: Precursor;
GN   Name=lacA; ORFNames=AN0756;
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=CBF88847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA65398.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACD01000012; EAA65398.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF88847.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_658360.1; XM_653268.1.
DR   ProteinModelPortal; Q5BFC4; -.
DR   SMR; Q5BFC4; -.
DR   STRING; 162425.CADANIAP00001909; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PRIDE; Q5BFC4; -.
DR   EnsemblFungi; EAA65398; EAA65398; AN0756.2.
DR   GeneID; 2876531; -.
DR   KEGG; ani:AN0756.2; -.
DR   HOGENOM; HOG000181922; -.
DR   InParanoid; Q5BFC4; -.
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; IDA:AspGD.
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     18       {ECO:0000255}.
FT   CHAIN        19   1007       Probable beta-galactosidase A.
FT                                /FTId=PRO_0000395220.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000255}.
FT   ACT_SITE    298    298       Nucleophile. {ECO:0000255}.
FT   BINDING      96     96       Substrate. {ECO:0000250}.
FT   BINDING     140    140       Substrate. {ECO:0000250}.
FT   BINDING     141    141       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     142    142       Substrate. {ECO:0000250}.
FT   BINDING     199    199       Substrate. {ECO:0000250}.
FT   BINDING     260    260       Substrate. {ECO:0000250}.
FT   BINDING     364    364       Substrate. {ECO:0000250}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    405    405       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    422    422       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    621    621       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    740    740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    775    775       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    914    914       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    205    206       {ECO:0000250}.
FT   DISULFID    266    315       {ECO:0000250}.
SQ   SEQUENCE   1007 AA;  111099 MW;  0C80D0D7E3893C4F CRC64;
     MRLLPVWTAA LLAAQAAGVA LTHKLNGFTI TEHPDAEKRE LLQKYVTWDD KSLFINGERI
     MIFGAEIHPW RLPVPSLWRD ILQKVKALGF NCVSFYVDWA LLEGKPGEYR AEGSFAWEPF
     FDAASDLGIY LIARPGPYIN AEASGGGFPG WLQRLNGTIR SSDQSYLDAT ENYVSHIGGL
     IAKYQITNGG PVILYQPDNE YSGGCCGQEF PNPDYFQYVI DQARRAGIVV PTISNDAWPG
     GHNAPGTGKG EVDIYGHDNY PLGFDCANPD VWPEGNLPTD YRDLHLEISP STPYALVEYQ
     VGAFDPWGGP GFEQCAALTG YEFERVFHKN TFSFGVGILS LYMTFGGTNW GNLGHPGGYT
     SYDYGSPIKE TREITREKYS ELKLLGNFIK SSPGYLLATP GKLTNTTYTN TADLTVTPLL
     GNGTGSFFVL RHSDYSSQAS TPYKLRLPTS AGQLTIPQLG GSLVLNGRDS KVHLVDYDVA
     GTKILYSTAE VFTWKKFHDG KVLVLYGGPG EHHELAVSSK AKVKVVEGLG SGISSKQIRG
     AVVVAWDVEP ARRIVQIGDL KIFLLDRNSA YNYWVPQLGT ETSIPYATEK AVAASVIVKA
     GYLVRTAYVK GRDLHLTADF NATTPVEVIG APKTAENLFI NGKKAHHTVD KNGIWSTEVG
     YSPPKIVLPV LEDLKWKSID TLPEIQPSYD DSPWPDANLP TKNTIYPLRT PTSLYASDYG
     FHTGYLLFRG HFTANGRESN FSIQTQGGQA FGSSVWLSGT YLGSWTGDND YQDYNATYTL
     PSLKAGKEYV FTVVVDNMGL NENWIVGQDE MKKPRGILNY ELSGHEASDI TWKLTGNFGG
     EDYVDKVRGP LNEGGLYAER HGYHQPYPPT KSKDWKSSTP LTGLSKPGIS FYTASFDLDI
     KSGWDVPIYF EFGNSTTPAP AYRVQLYVNG WQYGKYVNNI GPQTRFPVPE GILNYKGTNW
     VAVTLWALEG SGAKLDSFKL VHGIPVRTAL DVEGVELPRY QSRKGVY
//
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