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Q2UCU3

- BGALA_ASPOR

UniProt

Q2UCU3 - BGALA_ASPOR

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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: 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)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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

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        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

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007161 Genomic DNA. Translation: BAE60622.1 .
RefSeqi XP_001727461.1. XM_001727409.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 59 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