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Protein

Probable beta-galactosidase A

Gene

lacA

Organism
Penicillium sp.
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei96Substrate1
Binding sitei140Substrate1
Binding sitei141Substrate; via amide nitrogen1
Binding sitei142Substrate1
Binding sitei199Substrate1
Active sitei200Proton donorSequence analysis1
Binding sitei261Substrate1
Active sitei299NucleophileSequence analysis1
Binding sitei365Substrate1

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.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_500007246020 – 1011Probable beta-galactosidase AAdd BLAST992

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi205 ↔ 2061 Publication
Disulfide bondi267 ↔ 3161 Publication
Glycosylationi374N-linked (GlcNAc...)1 Publication1
Glycosylationi456N-linked (GlcNAc...)1 Publication1
Glycosylationi625N-linked (GlcNAc...)1 Publication1
Glycosylationi707N-linked (GlcNAc...)1 Publication1
Glycosylationi763N-linked (GlcNAc...)1 Publication1
Glycosylationi780N-linked (GlcNAc...)1 Publication1
Glycosylationi917N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

11011
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 – 66Combined sources5
Helixi69 – 71Combined sources3
Helixi75 – 77Combined sources3
Helixi78 – 86Combined sources9
Turni87 – 89Combined sources3
Beta strandi92 – 96Combined sources5
Helixi99 – 102Combined sources4
Helixi113 – 115Combined sources3
Helixi118 – 127Combined sources10
Beta strandi130 – 134Combined sources5
Helixi144 – 147Combined sources4
Helixi150 – 154Combined sources5
Helixi164 – 183Combined sources20
Helixi186 – 188Combined sources3
Beta strandi190 – 195Combined sources6
Helixi214 – 226Combined sources13
Beta strandi237 – 241Combined sources5
Beta strandi257 – 260Combined sources4
Helixi282 – 289Combined sources8
Beta strandi296 – 303Combined sources8
Helixi313 – 319Combined sources7
Helixi322 – 333Combined sources12
Turni334 – 336Combined sources3
Beta strandi338 – 343Combined sources6
Helixi378 – 391Combined sources14
Helixi394 – 397Combined sources4
Beta strandi399 – 401Combined sources3
Beta strandi405 – 411Combined sources7
Beta strandi415 – 421Combined sources7
Beta strandi429 – 437Combined sources9
Beta strandi444 – 446Combined sources3
Beta strandi448 – 452Combined sources5
Beta strandi455 – 459Combined sources5
Beta strandi461 – 464Combined sources4
Beta strandi466 – 468Combined sources3
Beta strandi474 – 482Combined sources9
Beta strandi485 – 500Combined sources16
Beta strandi503 – 510Combined sources8
Beta strandi515 – 521Combined sources7
Beta strandi527 – 531Combined sources5
Beta strandi537 – 541Combined sources5
Beta strandi544 – 550Combined sources7
Beta strandi556 – 560Combined sources5
Beta strandi563 – 569Combined sources7
Helixi570 – 573Combined sources4
Beta strandi583 – 586Combined sources4
Helixi593 – 597Combined sources5
Beta strandi601 – 603Combined sources3
Beta strandi605 – 614Combined sources10
Beta strandi617 – 626Combined sources10
Beta strandi628 – 634Combined sources7
Beta strandi641 – 644Combined sources4
Beta strandi647 – 649Combined sources3
Beta strandi659 – 663Combined sources5
Helixi675 – 677Combined sources3
Beta strandi681 – 685Combined sources5
Helixi687 – 689Combined sources3
Beta strandi698 – 700Combined sources3
Beta strandi714 – 717Combined sources4
Helixi721 – 724Combined sources4
Beta strandi731 – 738Combined sources8
Beta strandi745 – 751Combined sources7
Beta strandi758 – 762Combined sources5
Beta strandi765 – 770Combined sources6
Beta strandi777 – 784Combined sources8
Beta strandi793 – 800Combined sources8
Helixi815 – 817Combined sources3
Beta strandi821 – 827Combined sources7
Helixi832 – 834Combined sources3
Beta strandi836 – 842Combined sources7
Turni843 – 846Combined sources4
Turni851 – 853Combined sources3
Beta strandi855 – 857Combined sources3
Helixi862 – 865Combined sources4
Turni866 – 869Combined sources4
Beta strandi870 – 872Combined sources3
Turni883 – 885Combined sources3
Beta strandi887 – 900Combined sources14
Beta strandi911 – 915Combined sources5
Beta strandi925 – 931Combined sources7
Beta strandi934 – 940Combined sources7
Turni941 – 943Combined sources3
Beta strandi948 – 951Combined sources4
Beta strandi960 – 970Combined sources11
Beta strandi981 – 985Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TG7X-ray1.90A41-1011[»]
1XC6X-ray2.10A41-1011[»]
ProteinModelPortaliQ700S9.
SMRiQ700S9.
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.
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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TG7X-ray1.90A41-1011[»]
1XC6X-ray2.10A41-1011[»]
ProteinModelPortaliQ700S9.
SMRiQ700S9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ700S9.

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_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 2, 2016
This is version 62 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

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.