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P11546

- LACG_LACLL

UniProt

P11546 - LACG_LACLL

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Protein

6-phospho-beta-galactosidase

Gene
lacG
Organism
Lactococcus lactis subsp. lactis (Streptococcus lactis)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

A 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donor
Active sitei375 – 3751Nucleophile

GO - Molecular functioni

  1. 6-phospho-beta-galactosidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. lactose catabolic process via tagatose-6-phosphate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

SABIO-RKP11546.
UniPathwayiUPA00542; UER00605.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phospho-beta-galactosidase (EC:3.2.1.85)
Alternative name(s):
Beta-D-phosphogalactoside galactohydrolase
Short name:
PGALase
P-beta-Gal
Short name:
PBG
Gene namesi
Name:lacG
Encoded oniPlasmid pUCL131 Publication
Plasmid pLP7121 Publication
OrganismiLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifieri1360 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4684686-phospho-beta-galactosidaseUniRule annotationPRO_0000063883Add
BLAST

Expressioni

Inductioni

By lactose. The operon consists of lacABCDFEGX.1 Publication

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145
Helixi17 – 204
Helixi26 – 283
Helixi34 – 396
Beta strandi41 – 433
Beta strandi46 – 483
Helixi52 – 6514
Beta strandi70 – 745
Helixi77 – 804
Beta strandi84 – 874
Helixi90 – 10617
Beta strandi109 – 1179
Helixi121 – 1255
Helixi128 – 1303
Helixi133 – 14816
Beta strandi154 – 1596
Helixi161 – 1699
Beta strandi174 – 1763
Helixi182 – 20524
Beta strandi209 – 2179
Beta strandi221 – 2255
Helixi229 – 24214
Helixi244 – 2518
Helixi257 – 27014
Helixi278 – 28710
Turni288 – 2903
Beta strandi293 – 2975
Beta strandi302 – 3054
Beta strandi312 – 3143
Beta strandi325 – 3284
Turni329 – 3313
Beta strandi332 – 3343
Beta strandi338 – 3403
Helixi352 – 36413
Helixi366 – 3683
Beta strandi371 – 3755
Helixi392 – 41019
Beta strandi415 – 4217
Turni429 – 4313
Helixi432 – 4343
Beta strandi439 – 4424
Turni444 – 4463
Beta strandi449 – 4513
Helixi453 – 46412

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBGX-ray2.30A/B1-468[»]
2PBGX-ray2.50A1-468[»]
3PBGX-ray2.70A/B1-468[»]
4PBGX-ray2.50A/B1-468[»]
ProteinModelPortaliP11546.
SMRiP11546. Positions 1-468.

Miscellaneous databases

EvolutionaryTraceiP11546.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
HAMAPiMF_01574. LacG.
InterProiIPR005928. 6P-beta-galactosidase.
IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR01233. lacG. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11546-1 [UniParc]FASTAAdd to Basket

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MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS    50
DFYHKYPVDL ELAEEYGVNG IRISIAWSRI FPTGYGEVNE KGVEFYHKLF 100
AECHKRHVEP FVTLHHFDTP EALHSNGDFL NRENIEHFID YAAFCFEEFP 150
EVNYWTTFNE IGPIGDGQYL VGKFPPGIKY DLAKVFQSHH NMMVSHARAV 200
KLYKDKGYKG EIGVVHALPT KYPYDPENPA DVRAAELEDI IHNKFILDAT 250
YLGHYSDKTM EGVNHILAEN GGELDLRDED FQALDAAKDL NDFLGINYYM 300
SDWMQAFDGE TEIIHNGKGE KGSSKYQIKG VGRRVAPDYV PRTDWDWIIY 350
PEGLYDQIMR VKNDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ 400
HLEVLSDAIA DGANVKGYFI WSLMDVFSWS NGYEKRYGLF YVDFDTQERY 450
PKKSAHWYKK LAETQVIE 468
Length:468
Mass (Da):54,072
Last modified:August 1, 1992 - v2
Checksum:i5ACFC9BB81DF0E90
GO

Sequence cautioni

The sequence AAA26949.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA42986.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti383 – 3831E → Q in AAA25173. 1 Publication
Sequence conflicti387 – 3871N → K in AAA25173. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28357 Genomic DNA. Translation: AAA25173.1.
M60447 Genomic DNA. Translation: AAA25183.1.
M19454 Genomic DNA. Translation: AAA26949.1. Different initiation.
X60456 Genomic DNA. Translation: CAA42986.1. Different initiation.
PIRiA37168. GLSOPL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28357 Genomic DNA. Translation: AAA25173.1 .
M60447 Genomic DNA. Translation: AAA25183.1 .
M19454 Genomic DNA. Translation: AAA26949.1 . Different initiation.
X60456 Genomic DNA. Translation: CAA42986.1 . Different initiation.
PIRi A37168. GLSOPL.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PBG X-ray 2.30 A/B 1-468 [» ]
2PBG X-ray 2.50 A 1-468 [» ]
3PBG X-ray 2.70 A/B 1-468 [» ]
4PBG X-ray 2.50 A/B 1-468 [» ]
ProteinModelPortali P11546.
SMRi P11546. Positions 1-468.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00542 ; UER00605 .
SABIO-RK P11546.

Miscellaneous databases

EvolutionaryTracei P11546.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
HAMAPi MF_01574. LacG.
InterProi IPR005928. 6P-beta-galactosidase.
IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR01233. lacG. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and structural analysis of the phospho-beta-galactosidase gene from Streptococcus lactis Z268."
    Boizet B., Villeval D., Slos P., Novel M., Novel G., Mercenier A.
    Gene 62:249-261(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: L13 / Z268.
    Plasmid: pUCL13
  2. "Structure and expression of the Lactococcus lactis gene for phospho-beta-galactosidase (lacG) in Escherichia coli and L. lactis."
    de Vos W.M., Gasson M.J.
    J. Gen. Microbiol. 135:1833-1846(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: 712.
    Plasmid: pLP712
  3. "Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis."
    de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.
    J. Biol. Chem. 265:22554-22560(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, INDUCTION.
    Strain: MG1820.
  4. "Nonidentity between plasmid and chromosomal copies of ISS1-like sequences in Lactococcus lactis subsp. lactis CNRZ270 and their possible role in chromosomal integration of plasmid genes."
    Huang D.C., Novel M., Huang X.F., Novel G.
    Gene 118:39-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-468.
    Strain: Z270.
  5. "The three-dimensional structure of 6-phospho-beta-galactosidase from Lactococcus lactis."
    Wiesmann C., Beste G., Hengstenberg W., Schulz G.E.
    Structure 3:961-968(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  6. "Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis."
    Wiesmann C., Hengstenberg W., Schulz G.E.
    J. Mol. Biol. 269:851-860(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiLACG_LACLL
AccessioniPrimary (citable) accession number: P11546
Secondary accession number(s): Q79AQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This gene was sequenced from pMG820, a laboratory-derived deletion of the naturally occurring plasmid pLP712.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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