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   24-JAN-2024, entry version 102.
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 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 [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   [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., 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: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {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};
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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   AlphaFoldDB; Q5BFC4; -.
DR   SMR; Q5BFC4; -.
DR   STRING; 227321.Q5BFC4; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q5BFC4; 7 sites, No reported glycans.
DR   GeneID; 2876531; -.
DR   KEGG; ani:AN0756.2; -.
DR   VEuPathDB; FungiDB:AN0756; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   InParanoid; Q5BFC4; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
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; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 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:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1007
FT                   /note="Probable beta-galactosidase A"
FT                   /id="PRO_0000395220"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        775
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        914
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        205..206
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..315
FT                   /evidence="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
//