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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ629057 Genomic DNA. Translation: CAF32457.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ629057 Genomic DNA. Translation: CAF32457.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 56 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