BGALA_ASPOR
ID BGALA_ASPOR Reviewed; 1005 AA.
AC Q2UCU3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Beta-galactosidase A {ECO:0000305};
DE EC=3.2.1.23 {ECO:0000269|PubMed:23688418};
DE AltName: Full=Acidic beta-galactosidase {ECO:0000303|PubMed:23688418};
DE Short=Ao-beta-gal {ECO:0000303|PubMed:23688418};
DE AltName: Full=Lactase A;
DE Flags: Precursor;
GN Name=lacA; ORFNames=AO090012000445;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GALACTOSE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP GLYCOSYLATION AT ASN-373; ASN-402; ASN-622; ASN-760; ASN-777 AND ASN-914,
RP AND DISULFIDE BOND.
RX PubMed=23688418; DOI=10.1016/j.ijbiomac.2013.05.003;
RA Maksimainen M.M., Lampio A., Mertanen M., Turunen O., Rouvinen J.;
RT "The crystal structure of acidic beta-galactosidase from Aspergillus
RT oryzae.";
RL Int. J. Biol. Macromol. 60:109-115(2013).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000269|PubMed:23688418}.
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 Evidence={ECO:0000269|PubMed:23688418};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:23688418};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23688418}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AP007161; BAE60622.1; -; Genomic_DNA.
DR RefSeq; XP_001727461.1; XM_001727409.1.
DR PDB; 4IUG; X-ray; 2.60 A; A=1-1005.
DR PDBsum; 4IUG; -.
DR AlphaFoldDB; Q2UCU3; -.
DR SMR; Q2UCU3; -.
DR STRING; 510516.Q2UCU3; -.
DR Allergome; 1261; Asp o Lactase.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR CLAE; LAC35A_ASPOR; -.
DR iPTMnet; Q2UCU3; -.
DR EnsemblFungi; BAE60622; BAE60622; AO090012000445.
DR GeneID; 5987935; -.
DR KEGG; aor:AO090012000445; -.
DR VEuPathDB; FungiDB:AO090012000445; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OMA; YNYWVPQ; -.
DR BRENDA; 3.2.1.23; 522.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1005
FT /note="Beta-galactosidase A"
FT /id="PRO_0000395218"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:23688418"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:23688418"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23688418, ECO:0007744|PDB:4IUG"
FT DISULFID 205..206
FT /evidence="ECO:0000250|UniProtKB:A2QAN3"
FT DISULFID 266..315
FT /evidence="ECO:0000269|PubMed:23688418,
FT ECO:0007744|PDB:4IUG"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 452..460
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 482..497
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 602..611
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 614..623
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 728..735
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 742..748
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 762..767
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 774..781
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 790..797
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 818..824
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 833..839
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 840..843
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 848..850
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:4IUG"
FT HELIX 859..863
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 880..882
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 884..899
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 908..912
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 918..925
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 928..934
FT /evidence="ECO:0007829|PDB:4IUG"
FT TURN 935..937
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 953..964
FT /evidence="ECO:0007829|PDB:4IUG"
FT STRAND 975..979
FT /evidence="ECO:0007829|PDB:4IUG"
SQ SEQUENCE 1005 AA; 109870 MW; BAD290D2FA9EB003 CRC64;
MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD KSLFINGERI
MLFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA LLEGKPGDYR AEGIFALEPF
FDAAKEAGIY LIARPGSYIN AEVSGGGFPG WLQRVNGTLR SSDEPFLKAT DNYIANAAAA
VAKAQITNGG PVILYQPENE YSGGCCGVKY PDADYMQYVM DQARKADIVV PFISNDASPS
GHNAPGSGTG AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ
AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW GNLGHPGGYT
SYDYGSPITE TRNVTREKYS DIKLLANFVK ASPSYLTATP RNLTTGVYTD TSDLAVTPLI
GDSPGSFFVV RHTDYSSQES TSYKLKLPTS AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS
GTNIIYSTAE VFTWKKFDGN KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS
SVIIGWDVSS TRRIVQVGDL RVFLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK
AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTGAKNLF VNGEKASHTV DKNGIWSSEV
KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSADL PKTKNTHRPL DTPTSLYSSD
YGFHTGYLIY RGHFVANGKE SEFFIRTQGG SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY
KLSQLESGKN YVITVVIDNL GLDENWTVGE ETMKNPRGIL SYKLSGQDAS AITWKLTGNL
GGEDYQDKVR GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL
PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL NYRGTNYVAL
SLWALESDGA KLGSFELSYT TPVLTGYGNV ESPEQPKYEQ RKGAY
