BGALC_ASPFN
ID BGALC_ASPFN Reviewed; 984 AA.
AC B8N2I5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable beta-galactosidase C;
DE EC=3.2.1.23;
DE AltName: Full=Lactase C;
DE Flags: Precursor;
GN Name=lacC; ORFNames=AFLA_037600;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
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DR EMBL; EQ963473; EED56486.1; -; Genomic_DNA.
DR RefSeq; XP_002375268.1; XM_002375227.1.
DR AlphaFoldDB; B8N2I5; -.
DR SMR; B8N2I5; -.
DR STRING; 5059.CADAFLAP00003133; -.
DR EnsemblFungi; EED56486; EED56486; AFLA_037600.
DR VEuPathDB; FungiDB:AFLA_037600; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_1_1; -.
DR OMA; PEFEGGW; -.
DR Proteomes; UP000001875; 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; 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; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..984
FT /note="Probable beta-galactosidase C"
FT /id="PRO_0000395236"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 257..304
FT /evidence="ECO:0000250"
SQ SEQUENCE 984 AA; 108670 MW; 3E91614086ACDEB2 CRC64;
MRLLSFIYLV WLALLTGTPQ VSATDNGKTS DVAWDKYSLS VKGERLFVFS GEFHYQRLPV
PELWLDVFQK LRANGFNTIS VYFFWSYHSA SEDVFDFTTG AHDIQRLFDY AKQAGLYVIA
RAGPYCNAET SAGGFALWAA NGQMGSERTS DEAYYKKWKP WILEVGKIIA ANQITNGGPV
ILNQHENELQ ETTYDSNDTK VIYMEQVAKA FEEAGVVVPS SHNEKGMRTV SWSTDYKNVG
GAVNVYGLDS YPGSLSCANP NSGFNLLRTY YQWFQNYSYT QPEYLAEFEG GWFQPWGGSF
YDSCASELSP EFADVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYGSPLRET
REIRDKLKQT KLLGLFTRVS KDLLKTYMEG NGTSYTSDDS IYTWALRNPD SDAGFYVVAH
NTSSSREVTT FSLNITTSAG ALTIPDIELD GRQSKIIVTD YSIGSESSLL YSSAEVLTYA
TLDVDVLVFY LNAGQKGAFV FKDAPADLKY QTYGNSNLSA LETSQGTQYS YTQGEGVTAV
KFSNGVLVYL LDKETAWNFF APPTVSSPTV APNEHILVFG PYLVRGASIK HDTVEIVGDN
SNSTSIEIYT GDEHVKKVSW NGNLIDTRAT AYGSLIGTVP GAEDIEISLP SLSSWKAQDT
LPEISPDYDD SRWTICNKTT SVNSVAPLSL PVLYSGDYGY HTGTKIYRGR FDGQNATGAN
VTVQNGVAAG WAAWLNGAYV GGFSGDPDKV ASWEVLKFNH SSLRSRDNVL TIITDYTGHD
QNSQKPIGTQ NPRGIMGATL IGGGNFTLWR IQGNAGGEKN IDPVRGPMNE GGLYGERMGW
HLPGYQVPES ALDSSPLEGV SGAEGRFYTT SFQLDLEEDL DVPIGLQLSA PAGTEAVVQI
FMNGYQFGHY LPHIGPQSLF PFPPGVIYNR GQNSLAISMW ALTDAGARLE QVELKAYAKY
RSGFDFNRDW TYLQPGWKDR TEYA
