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Q700S9

- BGALA_PENSQ

UniProt

Q700S9 - BGALA_PENSQ

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Protein

Probable beta-galactosidase A

Gene

lacA

Organism
Penicillium sp.
Status
Reviewed - Annotation score: 4 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 – 961Substrate
Binding sitei140 – 1401Substrate
Binding sitei141 – 1411Substrate; via amide nitrogen
Binding sitei142 – 1421Substrate
Binding sitei199 – 1991Substrate
Active sitei200 – 2001Proton donorSequence Analysis
Binding sitei261 – 2611Substrate
Active sitei299 – 2991NucleophileSequence Analysis
Binding sitei365 – 3651Substrate

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

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-galactosidase A (EC:3.2.1.23)
Alternative name(s):
Lactase A
Gene namesi
Name:lacA
OrganismiPenicillium sp.
Taxonomic identifieri5081 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 1011992Probable beta-galactosidase APRO_5000072460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi205 ↔ 2061 Publication
Disulfide bondi267 ↔ 3161 Publication
Glycosylationi374 – 3741N-linked (GlcNAc...)1 Publication
Glycosylationi456 – 4561N-linked (GlcNAc...)1 Publication
Glycosylationi625 – 6251N-linked (GlcNAc...)1 Publication
Glycosylationi707 – 7071N-linked (GlcNAc...)1 Publication
Glycosylationi763 – 7631N-linked (GlcNAc...)1 Publication
Glycosylationi780 – 7801N-linked (GlcNAc...)1 Publication
Glycosylationi917 – 9171N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
1011
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 485
Beta strandi53 – 553
Beta strandi58 – 603
Beta strandi62 – 665
Helixi69 – 713
Helixi75 – 773
Helixi78 – 869
Turni87 – 893
Beta strandi92 – 965
Helixi99 – 1024
Helixi113 – 1153
Helixi118 – 12710
Beta strandi130 – 1345
Helixi144 – 1474
Helixi150 – 1545
Helixi164 – 18320
Helixi186 – 1883
Beta strandi190 – 1956
Helixi214 – 22613
Beta strandi237 – 2415
Beta strandi257 – 2604
Helixi282 – 2898
Beta strandi296 – 3038
Helixi313 – 3197
Helixi322 – 33312
Turni334 – 3363
Beta strandi338 – 3436
Helixi378 – 39114
Helixi394 – 3974
Beta strandi399 – 4013
Beta strandi405 – 4117
Beta strandi415 – 4217
Beta strandi429 – 4379
Beta strandi444 – 4463
Beta strandi448 – 4525
Beta strandi455 – 4595
Beta strandi461 – 4644
Beta strandi466 – 4683
Beta strandi474 – 4829
Beta strandi485 – 50016
Beta strandi503 – 5108
Beta strandi515 – 5217
Beta strandi527 – 5315
Beta strandi537 – 5415
Beta strandi544 – 5507
Beta strandi556 – 5605
Beta strandi563 – 5697
Helixi570 – 5734
Beta strandi583 – 5864
Helixi593 – 5975
Beta strandi601 – 6033
Beta strandi605 – 61410
Beta strandi617 – 62610
Beta strandi628 – 6347
Beta strandi641 – 6444
Beta strandi647 – 6493
Beta strandi659 – 6635
Helixi675 – 6773
Beta strandi681 – 6855
Helixi687 – 6893
Beta strandi698 – 7003
Beta strandi714 – 7174
Helixi721 – 7244
Beta strandi731 – 7388
Beta strandi745 – 7517
Beta strandi758 – 7625
Beta strandi765 – 7706
Beta strandi777 – 7848
Beta strandi793 – 8008
Helixi815 – 8173
Beta strandi821 – 8277
Helixi832 – 8343
Beta strandi836 – 8427
Turni843 – 8464
Turni851 – 8533
Beta strandi855 – 8573
Helixi862 – 8654
Turni866 – 8694
Beta strandi870 – 8723
Turni883 – 8853
Beta strandi887 – 90014
Beta strandi911 – 9155
Beta strandi925 – 9317
Beta strandi934 – 9407
Turni941 – 9433
Beta strandi948 – 9514
Beta strandi960 – 97011
Beta strandi981 – 9855

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TG7X-ray1.90A41-1011[»]
1XC6X-ray2.10A41-1011[»]
ProteinModelPortaliQ700S9.
SMRiQ700S9. Positions 41-1011.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ700S9.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Keywords - Domaini

Signal

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.

Q700S9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLSSWVVA ALAAQAAGAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE
60 70 80 90 100
HSIFVNGERL MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA
110 120 130 140 150
LLEGNPGHYS AEGIFDLQPF FDAAKEAGIY LLARPGPYIN AEVSGGGFPG
160 170 180 190 200
WLQRVDGILR TSDEAYLKAT DNYASNIAAT IAKAQITNGG PIILYQPENE
210 220 230 240 250
YSGACCGYNG FPDGSYMQYI EDHARDAGIV VPFISNDAWA AGHNAPGTGA
260 270 280 290 300
GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFHTSHEQQS PSTPYSLVEF
310 320 330 340 350
QGGAFDPWGG VGFAKCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN
360 370 380 390 400
WGNLGHPGGY TSYDYGSAIS ESRNITREKY SELKLLGNFA KVSPGYLVAN
410 420 430 440 450
PGDLSTSTYT NTADLTVTPL LGSNSSASSF FVIRHSDYSS QASVEYKLTV
460 470 480 490 500
PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY DVAGTNILYS TAEVFTWKKF
510 520 530 540 550
NNEKVLVLYG GPGEHHEFAV SGASSSSVVE GSSSGISSKK VGKALVVAWD
560 570 580 590 600
VSTARRIVQV GSLKVFLLDR NSAYNYWVPQ VPTKGTAPGY SNQETTASSI
610 620 630 640 650
IVKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK NLVINGKKTQ
660 670 680 690 700
TKVDKNGIWS ASVAYTAPKV QLPSLKSLKW KSVDTLPEAK NTYDDSAWTS
710 720 730 740 750
ADHAYTNNSA HSLQTPTSLF ASDYGYHTGA LLFRGHFTAN GKEKTFFVQT
760 770 780 790 800
KGGTAYGHSI WINETYVGSW AGTSINDNNN ATYTLPTLQS GKNYVITVVI
810 820 830 840 850
DNMGLDEDWT IGSEDMKNPR GIIQYSLSGQ EASAISWKLT GNLGGENYRD
860 870 880 890 900
TVRGPLNEGG LYAERQGFHQ PQPPTQKWDS SSPFTGLTKP GIRFYSTSFD
910 920 930 940 950
LDLPSGYDIP LYFNFGNSTS TPAAYRVQLY VNGYQYGKYV NNIGPQTSFP
960 970 980 990 1000
VPEGILNYHG TNWLALSLWA QEDNGAKLDS FELINTTPVL TSLGEVKSVN
1010
QPKYQARKGA Y
Length:1,011
Mass (Da):109,750
Last modified:July 5, 2004 - v1
Checksum:iA8A5BD48354F791A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ629057 Genomic DNA. Translation: CAF32457.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ629057 Genomic DNA. Translation: CAF32457.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TG7 X-ray 1.90 A 41-1011 [» ]
1XC6 X-ray 2.10 A 41-1011 [» ]
ProteinModelPortali Q700S9.
SMRi Q700S9. Positions 41-1011.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH35. Glycoside Hydrolase Family 35.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q700S9.

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. "Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose."
    Rojas A.L., Nagem R.A., Neustroev K.N., Arand M., Adamska M., Eneyskaya E.V., Kulminskaya A.A., Garratt R.C., Golubev A.M., Polikarpov I.
    J. Mol. Biol. 343:1281-1292(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-1011 IN COMPLEX WITH GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-374; ASN-456; ASN-625; ASN-707; ASN-763; ASN-780 AND ASN-917.

Entry informationi

Entry nameiBGALA_PENSQ
AccessioniPrimary (citable) accession number: Q700S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 55 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

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