BGALA_NEOFI
ID BGALA_NEOFI Reviewed; 1006 AA.
AC A1D1Z9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=NFIA_011250;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027688; EAW22442.1; -; Genomic_DNA.
DR RefSeq; XP_001264339.1; XM_001264338.1.
DR AlphaFoldDB; A1D1Z9; -.
DR SMR; A1D1Z9; -.
DR STRING; 36630.CADNFIAP00001763; -.
DR EnsemblFungi; EAW22442; EAW22442; NFIA_011250.
DR GeneID; 4591834; -.
DR KEGG; nfi:NFIA_011250; -.
DR VEuPathDB; FungiDB:NFIA_011250; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OMA; YNYWVPQ; -.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1006
FT /note="Probable beta-galactosidase A"
FT /id="PRO_0000395221"
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 207
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 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; 110230 MW; 0F6D74409FAE7B19 CRC64;
MKLLSVCAVA LLAAQAAGAS IKHKLNGFTI MEHSDPAKRE LLQKYVTWDE KSLFVNGERI
MIFSGEVHPF RLPVPSLWLD VFQKIKALGF NCVSFYVDWA LLEGKPGKYR AEGNFALEPF
FDAAKQAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSDPAYLKAT DNYIAHVAAT
VAKGQITNGG PVILYQPENE YSGACCNATF PDGDYMQYVI DQARNAGIVV PLINNDAWTG
GHNAPGTGKG EVDIYGHDSY PLGFDCGHPS VWPKGNLPTT FRTDHLRESP TTPYSLIEFQ
AGSFDPWGGP GFAACAALVN HEFERVFYKN DLSFGAAILN LYMTFGGTNW GNLGHPGGYT
SYDYGSPLTE SRNVTREKYS ELKLIGNFVK ASPSYLLATP GNLTTSGYAD TADLTVTPLL
GNGTGSYFVV RHTDYTSQAS TPYKLSLPTS AGRLTVPQLG GTLTLNGRDS KVHVVDYNVA
GTNILYSTAE VFTWKKFGDS KVLVLYGGPG EHHELAVSLK SDVQVVEGSN SEFTSKKVED
VVVVAWDVSA SRRIVQIGDL KIFLLDRNSA YNYWVPQLDK DDSSTGYSSE KTTASSIIVK
AGYLVRTAYT KGSGLYLTAD FNATTPVEVI GAPSNVRNLY INGEKTQFKT DKNGIWSTGV
KYSAPKIKLP SMKDLDWKYL DTLPEVQSTY DDSAWPAADL DTTPNTLRPL TMPKSLHSSD
YGFHTGYLIY RGHFVADGSE TTFDVRTQGG SAFGSSVWLN EAFLGSWTGL NANADYNSTY
RLPQVEKGKN YVLTVVIDTM GLNENWVVGT DEMKNPRGIL SYKLSGRDAS AITWKLTGNL
GGEDYQDKIR GPLNEGGLYA ERQGFHQPEP PSKKWKSASP LDGLSKPGIG FYTAQFDLDI
PSGWDVPLYF NFGNSTKSAY RVQLYVNGYQ YGKFVSNIGP QTSFPVPQGI LNYQGTNWVA
LTLWALESDG AKLDDFELVN TTPVMTALSK IRPSKQPNYR QRKGAY
