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Q2UCU3

- BGALA_ASPOR

UniProt

Q2UCU3 - BGALA_ASPOR

Protein

Probable beta-galactosidase A

Gene

lacA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961SubstrateBy similarity
    Binding sitei140 – 1401SubstrateBy similarity
    Binding sitei141 – 1411Substrate; via amide nitrogenBy similarity
    Binding sitei142 – 1421SubstrateBy similarity
    Binding sitei199 – 1991SubstrateBy similarity
    Active sitei200 – 2001Proton donorSequence Analysis
    Binding sitei260 – 2601SubstrateBy similarity
    Active sitei298 – 2981NucleophileSequence Analysis
    Binding sitei364 – 3641SubstrateBy similarity

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    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
    ProteomesiUP000006564: Chromosome 4

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 1005987Probable beta-galactosidase APRO_0000395218Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi205 ↔ 206By similarity
    Disulfide bondi266 ↔ 315By similarity
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi760 – 7601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi777 – 7771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi805 – 8051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    Secondary structure

    1
    1005
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 485
    Beta strandi53 – 553
    Beta strandi58 – 603
    Beta strandi62 – 676
    Helixi69 – 713
    Helixi75 – 773
    Helixi78 – 8710
    Beta strandi92 – 965
    Helixi99 – 1024
    Helixi113 – 1153
    Helixi118 – 12710
    Beta strandi130 – 1378
    Helixi144 – 1474
    Helixi150 – 1545
    Helixi164 – 1696
    Helixi171 – 18313
    Helixi186 – 1883
    Beta strandi190 – 20011
    Helixi213 – 22412
    Turni225 – 2273
    Beta strandi236 – 2405
    Beta strandi257 – 2593
    Helixi281 – 2888
    Beta strandi295 – 3028
    Helixi312 – 3187
    Helixi321 – 33212
    Turni333 – 3353
    Beta strandi337 – 3459
    Helixi350 – 3523
    Helixi377 – 39014
    Helixi393 – 3953
    Beta strandi404 – 4107
    Beta strandi412 – 4209
    Beta strandi422 – 4243
    Beta strandi426 – 4349
    Beta strandi440 – 4434
    Beta strandi445 – 4495
    Beta strandi452 – 4609
    Beta strandi463 – 4686
    Beta strandi471 – 4799
    Beta strandi482 – 49716
    Beta strandi500 – 5078
    Beta strandi512 – 5187
    Beta strandi524 – 5285
    Beta strandi534 – 5385
    Beta strandi541 – 5477
    Beta strandi553 – 5575
    Beta strandi560 – 5667
    Helixi567 – 5704
    Beta strandi580 – 5834
    Helixi590 – 5945
    Beta strandi598 – 6003
    Beta strandi602 – 61110
    Beta strandi614 – 62310
    Beta strandi625 – 6317
    Beta strandi638 – 6414
    Beta strandi644 – 6463
    Beta strandi656 – 6605
    Helixi672 – 6743
    Beta strandi678 – 6825
    Helixi684 – 6863
    Beta strandi695 – 6973
    Beta strandi706 – 7083
    Beta strandi711 – 7144
    Helixi718 – 7214
    Beta strandi728 – 7358
    Beta strandi742 – 7487
    Beta strandi755 – 7595
    Beta strandi762 – 7676
    Beta strandi774 – 7818
    Beta strandi790 – 7978
    Turni808 – 8103
    Helixi812 – 8143
    Beta strandi818 – 8247
    Helixi829 – 8313
    Beta strandi833 – 8397
    Turni840 – 8434
    Turni848 – 8503
    Beta strandi852 – 8543
    Helixi859 – 8635
    Turni864 – 8663
    Beta strandi867 – 8693
    Beta strandi875 – 8773
    Turni880 – 8823
    Beta strandi884 – 89916
    Beta strandi908 – 9125
    Beta strandi918 – 9258
    Beta strandi928 – 9347
    Turni935 – 9373
    Beta strandi942 – 9454
    Beta strandi953 – 96412
    Beta strandi975 – 9795

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IUGX-ray2.60A1-1005[»]
    ProteinModelPortaliQ2UCU3.
    SMRiQ2UCU3. Positions 41-1005.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi175 – 18410Poly-Ala

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiHNAPGTG.
    OrthoDBiEOG7ZGXBD.

    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.
    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

    MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD     50
    KSLFINGERI MLFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA 100
    LLEGKPGDYR AEGIFALEPF FDAAKEAGIY LIARPGSYIN AEVSGGGFPG 150
    WLQRVNGTLR SSDEPFLKAT DNYIANAAAA VAKAQITNGG PVILYQPENE 200
    YSGGCCGVKY PDADYMQYVM DQARKADIVV PFISNDASPS GHNAPGSGTG 250
    AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ 300
    AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW 350
    GNLGHPGGYT SYDYGSPITE TRNVTREKYS DIKLLANFVK ASPSYLTATP 400
    RNLTTGVYTD TSDLAVTPLI GDSPGSFFVV RHTDYSSQES TSYKLKLPTS 450
    AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS GTNIIYSTAE VFTWKKFDGN 500
    KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS SVIIGWDVSS 550
    TRRIVQVGDL RVFLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK 600
    AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTGAKNLF VNGEKASHTV 650
    DKNGIWSSEV KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSADL 700
    PKTKNTHRPL DTPTSLYSSD YGFHTGYLIY RGHFVANGKE SEFFIRTQGG 750
    SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY KLSQLESGKN YVITVVIDNL 800
    GLDENWTVGE ETMKNPRGIL SYKLSGQDAS AITWKLTGNL GGEDYQDKVR 850
    GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL 900
    PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL 950
    NYRGTNYVAL SLWALESDGA KLGSFELSYT TPVLTGYGNV ESPEQPKYEQ 1000
    RKGAY 1005
    Length:1,005
    Mass (Da):109,870
    Last modified:January 24, 2006 - v1
    Checksum:iBAD290D2FA9EB003
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007161 Genomic DNA. Translation: BAE60622.1.
    RefSeqiXP_001727461.1. XM_001727409.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00006026; CADAORAP00005912; CADAORAG00006026.
    GeneIDi5987935.
    KEGGiaor:AOR_1_770194.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007161 Genomic DNA. Translation: BAE60622.1 .
    RefSeqi XP_001727461.1. XM_001727409.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IUG X-ray 2.60 A 1-1005 [» ]
    ProteinModelPortali Q2UCU3.
    SMRi Q2UCU3. Positions 41-1005.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00006026 ; CADAORAP00005912 ; CADAORAG00006026 .
    GeneIDi 5987935.
    KEGGi aor:AOR_1_770194.

    Phylogenomic databases

    OMAi HNAPGTG.
    OrthoDBi EOG7ZGXBD.

    Family and domain databases

    Gene3Di 2.102.20.10. 1 hit.
    2.60.120.260. 2 hits.
    2.60.390.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR018954. Betagal_dom2.
    IPR025972. BetaGal_dom3.
    IPR025300. BetaGal_jelly_roll_dom.
    IPR008979. Galactose-bd-like.
    IPR019801. Glyco_hydro_35_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR001944. Glycoside_Hdrlase_35.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF10435. BetaGal_dom2. 1 hit.
    PF13363. BetaGal_dom3. 1 hit.
    PF13364. BetaGal_dom4_5. 2 hits.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SMARTi SM01029. BetaGal_dom2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF117100. SSF117100. 1 hit.
    SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    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: October 1, 2014
    This is version 57 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

    External Data

    Dasty 3