BGALC_ASPCL
ID BGALC_ASPCL Reviewed; 985 AA.
AC A1CE56;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=ACLA_088440;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
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DR EMBL; DS027052; EAW11155.1; -; Genomic_DNA.
DR RefSeq; XP_001272581.1; XM_001272580.1.
DR AlphaFoldDB; A1CE56; -.
DR SMR; A1CE56; -.
DR STRING; 5057.CADACLAP00008328; -.
DR EnsemblFungi; EAW11155; EAW11155; ACLA_088440.
DR GeneID; 4704994; -.
DR KEGG; act:ACLA_088440; -.
DR VEuPathDB; FungiDB:ACLA_088440; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_1_1; -.
DR OMA; PEFEGGW; -.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000006701; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..985
FT /note="Probable beta-galactosidase C"
FT /id="PRO_0000395234"
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 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 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 DISULFID 257..304
FT /evidence="ECO:0000250"
SQ SEQUENCE 985 AA; 108394 MW; 64345E996ADB15F8 CRC64;
MRILSLLFLL LLGFLAGNRV VSATDHGKTT DVTWDRYSLS VKGERLFVFS GEFHYQRLPV
PEMWLDVFQK LRANGFNAIS VYFFWGYHSA SEGEFDFETG AHNIQRLFDY AKEAGIYVIA
RAGPYCNAET TAGGYALWAA NGQMGNERTS DDAYYAKWRP WILEVGKIIA ANQITNGGPV
ILNQHENELQ ETSYEADNTL VVYMKQIARV FQEAGIVVPS SHNEKGMRAV SWSTDHHDVG
GAVNIYGLDS YPGGLSCTNP SSGFNLVRTY YQWFQNSSYT QPEYLPEFEG GWFQPWGGHD
YDTCATELSP EFADVYYKNN IGSRVTLQNI YMVFGGTNWG HSAAPVVYTS YDYSAPLRET
REIRDKLKQT KLIGLFTRVS SDLLKTHMEG NGTGYTSDSS IYTWALHNPD TNAGFYVLAH
KTSSSRSVTE FSLNVTTSAG AISIPDIQLD GRQSKIIVTD YQFGKSSALL YSSAEVLTYA
NLDVDVLVLY LNVGQKGLFV FKDERSKLSF QTYGNTNVTA SVSSHGTQYI YTQAEGVTAV
KFSNGVLAYL LDKESAWNFF APPTTSNPQV APDEHILVQG PYLVRGVTIN HDTVEIIGDN
ANTTSLEVYA GNLRVKVVKW NGKAIKSRRT AYGSLVGRAP GAEDARISPP SLDSWSAQDT
LPDIQPDYDD SRWTVCNKTA SVNAVPLLSL PVLYSGDYGY HAGTKVYRGR FDGRNVTGAN
VTVQNGVASG WAAWLNGQFV GGVAGAIDLA VTSAVLSFNS SLLHDRDNVL TVVTDYTGHD
QNSVRPKGTQ NPRGILGATL IGGGKFTSWR IQGNAGGEKN IDPVRGPINE GGLYGERMGW
HLPGYKAPRS AAKSSPLDGI SGAEGRFYTT TFTLKLDRDL DVPIGLQLGA PAGTQAVVQV
FMNGYQFGHY LPHIGPQSLF PFPPGVINNR GENTLAISMW ALTDAGAKLD QVELVAYGKY
RSGFDFNQDW GYLQPQWKDN RRQYA
