BGALA_ASPFC
ID BGALA_ASPFC Reviewed; 1006 AA.
AC B0XMP7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 62.
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=AFUB_013710;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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=EDP56654.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499594; EDP56654.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0XMP7; -.
DR SMR; B0XMP7; -.
DR PRIDE; B0XMP7; -.
DR PhylomeDB; B0XMP7; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.20.10; -; 1.
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; IPR019801; Glyco_hydro_35_CS.
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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1006
FT /note="Probable beta-galactosidase A"
FT /id="PRO_0000395215"
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 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
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 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
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 1006 AA; 110405 MW; 86CF2FDEF43A85BD CRC64;
MKLLSVCAIA LLAAQAAGAS IKHMLNGFTL MEHSDPAKRE LLQKYVTWDE KSLFVNGERI
MIFSGEVHPF RLPVPSLWLD VFQKIKALGF NCVSFYVDWA LLEGKPGEYR AEGNFALEPF
FDVAKQAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSDPAYLKAT DNYIAHVAAT
IAKGQITNGG PVILYQPENE YSGACCDATF PDGDYMQYVI DQARNAGIVV PLINNDAWTG
GHNAPGTGKG EVDIYGHDSY PLGFDCGHPS VWPKGNLPTT FRTDHLKQSP TTPYSLIEFQ
AGSFDPWGGP GFAACAALVN HEFERVFYKN DLSFGAAILN LYMTFGGTNW GNLGHPGGYT
SYDYGSPLTE SRNVTREKYS ELKLIGNFVK ASPSYLLATP GNLTTSGYAD TADLTVTPLL
GNGTGSYFVV RHTDYTSQAS TPYKLSLPTS AGRLTVPQLG GTLTLNGRDS KIHVVDYNVA
GTNIIYSTAE VFTWKNFGDS KVLILYGGPG EHHELAVSFK SDVQVVEGSN SEFKSKKVGD
VAVVAWDVSP SRRIVQIGDL KIFLLDRNSV YNYWVPQLDK DDSSTGYSSE KTTASSIIVK
AGYLVRTAYT KGSGLYLTAD FNATTPVEVI GAPSNVRNLY INGEKTQFKT DKNGIWSTEV
KYSAPKIKLP SMKDLDWKYL DTLQEVQSTY DDSAWPAADL DTTPNTLRPL TTPKSLYSSD
YGFHTGYLIY RGHFVADGSE TTFDVRTQGG SAFGSSVWLN ESFLGSWTGL NANADYNSTY
KLPQVEQGKN YVLTILIDTM GLNENWVVGT DEMKNPRGIL SYKLSGRDAS AITWKLTGNL
GGEDYQDKIR GPLNEGGLYA ERQGFHQPQP PSQKWKSASP LDGLSKPGIG FYTAQFDLDI
PSGWDVPLYF NFGNSTKSAY RVQLYVNGYQ YGKFVSNIGP QTSFPVPQGI LNYQGTNWVA
LTLWALESDG AKLDDFELVN TTPVMTALSK IRPSKQPNYR QRKGAY
