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Protein

Probable beta-galactosidase A

Gene

lacA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.By similarity

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96SubstrateBy similarity1
Binding sitei140SubstrateBy similarity1
Binding sitei141Substrate; via amide nitrogenBy similarity1
Binding sitei142SubstrateBy similarity1
Binding sitei199SubstrateBy similarity1
Active sitei200Proton donorSequence analysis1
Binding sitei260SubstrateBy similarity1
Active sitei298NucleophileSequence analysis1
Binding sitei364SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.
mycoCLAPiLAC35A_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-galactosidase A (EC:3.2.1.23)
Alternative name(s):
Lactase A
Gene namesi
Name:lacA
ORF Names:AO090012000445
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 4

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039521819 – 1005Probable beta-galactosidase AAdd BLAST987

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi205 ↔ 206By similarity
Disulfide bondi266 ↔ 315By similarity
Glycosylationi373N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi453N-linked (GlcNAc...)Sequence analysis1
Glycosylationi478N-linked (GlcNAc...)Sequence analysis1
Glycosylationi522N-linked (GlcNAc...)Sequence analysis1
Glycosylationi622N-linked (GlcNAc...)Sequence analysis1
Glycosylationi760N-linked (GlcNAc...)Sequence analysis1
Glycosylationi777N-linked (GlcNAc...)Sequence analysis1
Glycosylationi805N-linked (GlcNAc...)Sequence analysis1
Glycosylationi914N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

11005
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 48Combined sources5
Beta strandi53 – 55Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi62 – 67Combined sources6
Helixi69 – 71Combined sources3
Helixi75 – 77Combined sources3
Helixi78 – 87Combined sources10
Beta strandi92 – 96Combined sources5
Helixi99 – 102Combined sources4
Helixi113 – 115Combined sources3
Helixi118 – 127Combined sources10
Beta strandi130 – 137Combined sources8
Helixi144 – 147Combined sources4
Helixi150 – 154Combined sources5
Helixi164 – 169Combined sources6
Helixi171 – 183Combined sources13
Helixi186 – 188Combined sources3
Beta strandi190 – 200Combined sources11
Helixi213 – 224Combined sources12
Turni225 – 227Combined sources3
Beta strandi236 – 240Combined sources5
Beta strandi257 – 259Combined sources3
Helixi281 – 288Combined sources8
Beta strandi295 – 302Combined sources8
Helixi312 – 318Combined sources7
Helixi321 – 332Combined sources12
Turni333 – 335Combined sources3
Beta strandi337 – 345Combined sources9
Helixi350 – 352Combined sources3
Helixi377 – 390Combined sources14
Helixi393 – 395Combined sources3
Beta strandi404 – 410Combined sources7
Beta strandi412 – 420Combined sources9
Beta strandi422 – 424Combined sources3
Beta strandi426 – 434Combined sources9
Beta strandi440 – 443Combined sources4
Beta strandi445 – 449Combined sources5
Beta strandi452 – 460Combined sources9
Beta strandi463 – 468Combined sources6
Beta strandi471 – 479Combined sources9
Beta strandi482 – 497Combined sources16
Beta strandi500 – 507Combined sources8
Beta strandi512 – 518Combined sources7
Beta strandi524 – 528Combined sources5
Beta strandi534 – 538Combined sources5
Beta strandi541 – 547Combined sources7
Beta strandi553 – 557Combined sources5
Beta strandi560 – 566Combined sources7
Helixi567 – 570Combined sources4
Beta strandi580 – 583Combined sources4
Helixi590 – 594Combined sources5
Beta strandi598 – 600Combined sources3
Beta strandi602 – 611Combined sources10
Beta strandi614 – 623Combined sources10
Beta strandi625 – 631Combined sources7
Beta strandi638 – 641Combined sources4
Beta strandi644 – 646Combined sources3
Beta strandi656 – 660Combined sources5
Helixi672 – 674Combined sources3
Beta strandi678 – 682Combined sources5
Helixi684 – 686Combined sources3
Beta strandi695 – 697Combined sources3
Beta strandi706 – 708Combined sources3
Beta strandi711 – 714Combined sources4
Helixi718 – 721Combined sources4
Beta strandi728 – 735Combined sources8
Beta strandi742 – 748Combined sources7
Beta strandi755 – 759Combined sources5
Beta strandi762 – 767Combined sources6
Beta strandi774 – 781Combined sources8
Beta strandi790 – 797Combined sources8
Turni808 – 810Combined sources3
Helixi812 – 814Combined sources3
Beta strandi818 – 824Combined sources7
Helixi829 – 831Combined sources3
Beta strandi833 – 839Combined sources7
Turni840 – 843Combined sources4
Turni848 – 850Combined sources3
Beta strandi852 – 854Combined sources3
Helixi859 – 863Combined sources5
Turni864 – 866Combined sources3
Beta strandi867 – 869Combined sources3
Beta strandi875 – 877Combined sources3
Turni880 – 882Combined sources3
Beta strandi884 – 899Combined sources16
Beta strandi908 – 912Combined sources5
Beta strandi918 – 925Combined sources8
Beta strandi928 – 934Combined sources7
Turni935 – 937Combined sources3
Beta strandi942 – 945Combined sources4
Beta strandi953 – 964Combined sources12
Beta strandi975 – 979Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IUGX-ray2.60A1-1005[»]
ProteinModelPortaliQ2UCU3.
SMRiQ2UCU3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi175 – 184Poly-Ala10

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

OMAiHNAPGTG.
OrthoDBiEOG092C0SLI.

Family and domain databases

Gene3Di2.102.20.10. 1 hit.
2.60.120.260. 2 hits.
2.60.390.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR018954. Betagal_dom2.
IPR025972. BetaGal_dom3.
IPR025300. BetaGal_jelly_roll_dom.
IPR008979. Galactose-bd-like.
IPR031330. Gly_Hdrlase_35_cat.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF10435. BetaGal_dom2. 1 hit.
PF13363. BetaGal_dom3. 1 hit.
PF13364. BetaGal_dom4_5. 2 hits.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSiPR00742. GLHYDRLASE35.
SMARTiSM01029. BetaGal_dom2. 1 hit.
[Graphical view]
SUPFAMiSSF117100. SSF117100. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2UCU3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD
60 70 80 90 100
KSLFINGERI MLFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA
110 120 130 140 150
LLEGKPGDYR AEGIFALEPF FDAAKEAGIY LIARPGSYIN AEVSGGGFPG
160 170 180 190 200
WLQRVNGTLR SSDEPFLKAT DNYIANAAAA VAKAQITNGG PVILYQPENE
210 220 230 240 250
YSGGCCGVKY PDADYMQYVM DQARKADIVV PFISNDASPS GHNAPGSGTG
260 270 280 290 300
AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ
310 320 330 340 350
AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW
360 370 380 390 400
GNLGHPGGYT SYDYGSPITE TRNVTREKYS DIKLLANFVK ASPSYLTATP
410 420 430 440 450
RNLTTGVYTD TSDLAVTPLI GDSPGSFFVV RHTDYSSQES TSYKLKLPTS
460 470 480 490 500
AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS GTNIIYSTAE VFTWKKFDGN
510 520 530 540 550
KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS SVIIGWDVSS
560 570 580 590 600
TRRIVQVGDL RVFLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK
610 620 630 640 650
AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTGAKNLF VNGEKASHTV
660 670 680 690 700
DKNGIWSSEV KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSADL
710 720 730 740 750
PKTKNTHRPL DTPTSLYSSD YGFHTGYLIY RGHFVANGKE SEFFIRTQGG
760 770 780 790 800
SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY KLSQLESGKN YVITVVIDNL
810 820 830 840 850
GLDENWTVGE ETMKNPRGIL SYKLSGQDAS AITWKLTGNL GGEDYQDKVR
860 870 880 890 900
GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL
910 920 930 940 950
PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL
960 970 980 990 1000
NYRGTNYVAL SLWALESDGA KLGSFELSYT TPVLTGYGNV ESPEQPKYEQ

RKGAY
Length:1,005
Mass (Da):109,870
Last modified:January 24, 2006 - v1
Checksum:iBAD290D2FA9EB003
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007161 Genomic DNA. Translation: BAE60622.1.
RefSeqiXP_001727461.1. XM_001727409.1.

Genome annotation databases

EnsemblFungiiBAE60622; BAE60622; AO090012000445.
GeneIDi5987935.
KEGGiaor:AOR_1_770194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007161 Genomic DNA. Translation: BAE60622.1.
RefSeqiXP_001727461.1. XM_001727409.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IUGX-ray2.60A1-1005[»]
ProteinModelPortaliQ2UCU3.
SMRiQ2UCU3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.
mycoCLAPiLAC35A_ASPOR.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE60622; BAE60622; AO090012000445.
GeneIDi5987935.
KEGGiaor:AOR_1_770194.

Phylogenomic databases

OMAiHNAPGTG.
OrthoDBiEOG092C0SLI.

Family and domain databases

Gene3Di2.102.20.10. 1 hit.
2.60.120.260. 2 hits.
2.60.390.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR018954. Betagal_dom2.
IPR025972. BetaGal_dom3.
IPR025300. BetaGal_jelly_roll_dom.
IPR008979. Galactose-bd-like.
IPR031330. Gly_Hdrlase_35_cat.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF10435. BetaGal_dom2. 1 hit.
PF13363. BetaGal_dom3. 1 hit.
PF13364. BetaGal_dom4_5. 2 hits.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSiPR00742. GLHYDRLASE35.
SMARTiSM01029. BetaGal_dom2. 1 hit.
[Graphical view]
SUPFAMiSSF117100. SSF117100. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBGALA_ASPOR
AccessioniPrimary (citable) accession number: Q2UCU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.