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Database: UniProt
Entry: BGALA_NEOFI
LinkDB: BGALA_NEOFI
Original site: 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   16-JAN-2019, entry version 74.
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
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; DS027688; EAW22442.1; -; Genomic_DNA.
DR   RefSeq; XP_001264339.1; XM_001264338.1.
DR   ProteinModelPortal; A1D1Z9; -.
DR   SMR; A1D1Z9; -.
DR   STRING; 36630.CADNFIAP00001763; -.
DR   PRIDE; A1D1Z9; -.
DR   EnsemblFungi; EAW22442; EAW22442; NFIA_011250.
DR   GeneID; 4591834; -.
DR   KEGG; nfi:NFIA_011250; -.
DR   EuPathDB; FungiDB:NFIA_011250; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; GGEDYVD; -.
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; 2.60.120.260; -; 2.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1006       Probable beta-galactosidase A.
FT                                /FTId=PRO_0000395221.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000255}.
FT   ACT_SITE    298    298       Nucleophile. {ECO:0000255}.
FT   BINDING      96     96       Substrate. {ECO:0000250}.
FT   BINDING     140    140       Substrate. {ECO:0000250}.
FT   BINDING     141    141       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     142    142       Substrate. {ECO:0000250}.
FT   BINDING     199    199       Substrate. {ECO:0000250}.
FT   BINDING     260    260       Substrate. {ECO:0000250}.
FT   BINDING     364    364       Substrate. {ECO:0000250}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    373    373       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    422    422       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    622    622       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    777    777       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    914    914       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    205    206       {ECO:0000250}.
FT   DISULFID    266    315       {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
//
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