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Protein

1,3-beta-galactosyl-N-acetylhexosamine phosphorylase

Gene

lnpA

Organism
Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.3 Publications

Catalytic activityi

Beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei313 – 3131Proton donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciBLON565042:GIWN-1685-MONOMER.
BRENDAi2.4.1.211. 851.

Protein family/group databases

CAZyiGH112. Glycoside Hydrolase Family 112.

Names & Taxonomyi

Protein namesi
Recommended name:
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC:2.4.1.211)
Alternative name(s):
Galacto-N-biose/lacto-N-biose I phosphorylase
Short name:
GLNBP
Gene namesi
Name:lnpA
Synonyms:lnbp
Ordered Locus Names:BLLJ_1623
OrganismiBifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Taxonomic identifieri565042 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium
Proteomesi
  • UP000007255 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321R → E: Lack of activity. 1 Publication
Mutagenesisi166 – 1661N → A: Strong decrease in activity. 1 Publication
Mutagenesisi210 – 2101R → E: Lack of activity. 1 Publication
Mutagenesisi358 – 3581R → E: Lack of activity. 1 Publication
Mutagenesisi362 – 3621Y → F: Strong decrease in activity. 1 Publication
Mutagenesisi362 – 3621Y → N: Lack of activity. 1 Publication
Mutagenesisi364 – 3641F → N: Decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7517511,3-beta-galactosyl-N-acetylhexosamine phosphorylasePRO_0000424070Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
751
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi16 – 2611Combined sources
Beta strandi29 – 324Combined sources
Helixi43 – 464Combined sources
Beta strandi49 – 546Combined sources
Helixi61 – 644Combined sources
Helixi68 – 703Combined sources
Beta strandi73 – 775Combined sources
Beta strandi84 – 9310Combined sources
Turni98 – 1003Combined sources
Beta strandi101 – 1033Combined sources
Helixi109 – 1124Combined sources
Beta strandi114 – 1174Combined sources
Turni118 – 1214Combined sources
Beta strandi122 – 1243Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi148 – 15710Combined sources
Helixi161 – 1699Combined sources
Helixi186 – 20116Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi226 – 2327Combined sources
Helixi237 – 2393Combined sources
Helixi242 – 25211Combined sources
Helixi259 – 2624Combined sources
Helixi263 – 2653Combined sources
Turni266 – 2683Combined sources
Helixi276 – 30227Combined sources
Beta strandi306 – 3149Combined sources
Turni316 – 3183Combined sources
Helixi325 – 3284Combined sources
Beta strandi332 – 3398Combined sources
Helixi340 – 3478Combined sources
Beta strandi351 – 36111Combined sources
Turni365 – 3673Combined sources
Helixi375 – 39117Combined sources
Beta strandi395 – 3984Combined sources
Helixi403 – 4075Combined sources
Helixi410 – 43021Combined sources
Beta strandi439 – 4479Combined sources
Helixi448 – 4514Combined sources
Turni452 – 4565Combined sources
Turni465 – 4673Combined sources
Helixi468 – 47811Combined sources
Beta strandi480 – 4889Combined sources
Helixi489 – 4957Combined sources
Beta strandi503 – 5086Combined sources
Turni513 – 5153Combined sources
Helixi517 – 5215Combined sources
Helixi523 – 53412Combined sources
Beta strandi538 – 5447Combined sources
Beta strandi547 – 5526Combined sources
Beta strandi555 – 5573Combined sources
Helixi560 – 5634Combined sources
Beta strandi564 – 5674Combined sources
Turni587 – 5915Combined sources
Helixi596 – 60510Combined sources
Turni612 – 6143Combined sources
Beta strandi619 – 6213Combined sources
Beta strandi635 – 6395Combined sources
Beta strandi642 – 6465Combined sources
Helixi648 – 6503Combined sources
Beta strandi653 – 6597Combined sources
Beta strandi662 – 6687Combined sources
Helixi674 – 68714Combined sources
Helixi691 – 6944Combined sources
Beta strandi698 – 7014Combined sources
Beta strandi704 – 7096Combined sources
Turni710 – 7134Combined sources
Beta strandi714 – 7196Combined sources
Beta strandi721 – 7233Combined sources
Beta strandi725 – 7306Combined sources
Beta strandi736 – 7416Combined sources
Beta strandi746 – 7494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZUSX-ray2.11A/B/C/D1-751[»]
2ZUTX-ray1.90A/B/C/D1-751[»]
2ZUUX-ray2.30A/B/C/D1-751[»]
2ZUVX-ray1.85A/B1-751[»]
2ZUWX-ray2.11A/B/C/D1-751[»]
3WFZX-ray2.60A/B/C/D1-751[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycoside hydrolase 112 family.Curated

Phylogenomic databases

HOGENOMiHOG000015674.
KOiK15533.
OMAiPMHEYTV.

Family and domain databases

InterProiIPR029062. Class_I_gatase-like.
IPR012711. Lacto-N-biose_phosphorylase.
[Graphical view]
PfamiPF09508. Lact_bio_phlase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 2 hits.
TIGRFAMsiTIGR02336. TIGR02336. 1 hit.

Sequencei

Sequence statusi: Complete.

E8MF13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSTGRFTLP SEENFAEKTK ELAELWGADA IRNSDGTHLD EAVLALGKKI
60 70 80 90 100
YNAYFPTRAH NEWITLHMDE TPQVYLLTDR ILAESDTVDI PLMESFFAEQ
110 120 130 140 150
LKPNRDADPH KYWEVVDRTT GEVVDSANWT LDADEDTVHV SGVAAWHEYT
160 170 180 190 200
VSFLAYIIWD PVEMYNHLTN DWGDKEHEIP FDIYHPATRK FVFDTFEQWL
210 220 230 240 250
KDSPQTDVVR FTTFFYQFTL LFDEKRREKV VDWFGCACTV SPRALDDFEA
260 270 280 290 300
KYGYRLRPED FVDGGAYNSA WRVPRKAQRD WIDFLSGFVR ENVKQLADMS
310 320 330 340 350
HAAGKEAMMF LGDQWIGTEP YKDGFDELGL DAVVGSIGDG TTTRMIADIP
360 370 380 390 400
GVKYTEGRFL PYFFPDTFYE GNDPSIEGLD NWRKARRAIL RSPISRMGYG
410 420 430 440 450
GYLSLAAKFP KFVDTVTHIA NEFRDIHDRT GGVAAEGELN VAILNSWGKM
460 470 480 490 500
RSWMAFTVAH ALPNKQTYSY YGILESLSGM RVNVRFISFD DVLAHGIDSD
510 520 530 540 550
IDVIINGGPV DTAFTGGDVW TNPKLVETVR AWVRGGGAFV GVGEPSSAPR
560 570 580 590 600
FQTGRFFQLA DVIGVDEERY QTLSVDKYFP PVVPDHFITA DVPVDPAARE
610 620 630 640 650
AWEQAGYRIP LSGCGGGQSI KPLGGIDFGE PVLNTYPVNE NVTLLRADGG
660 670 680 690 700
QVQLATNDYG KGRGVYISGL PYSAANARLL ERVLFYASHN EDKYAAWSSS
710 720 730 740 750
NPECEVAHFP EQGLYCVINN TDQPQKTTVT LADGTTEDFD LPDSGIAWRE

A
Length:751
Mass (Da):84,327
Last modified:April 5, 2011 - v1
Checksum:iE2C4E2471C6761EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB181926 Genomic DNA. Translation: BAD80751.1.
AB303839 Genomic DNA. Translation: BAF73924.1.
AP010888 Genomic DNA. Translation: BAJ67290.1.
RefSeqiWP_007056738.1. NC_015067.1.

Genome annotation databases

EnsemblBacteriaiBAJ67290; BAJ67290; BLLJ_1623.
KEGGiblm:BLLJ_1623.
PATRICi46891734. VBIBifLon48544_1679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB181926 Genomic DNA. Translation: BAD80751.1.
AB303839 Genomic DNA. Translation: BAF73924.1.
AP010888 Genomic DNA. Translation: BAJ67290.1.
RefSeqiWP_007056738.1. NC_015067.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZUSX-ray2.11A/B/C/D1-751[»]
2ZUTX-ray1.90A/B/C/D1-751[»]
2ZUUX-ray2.30A/B/C/D1-751[»]
2ZUVX-ray1.85A/B1-751[»]
2ZUWX-ray2.11A/B/C/D1-751[»]
3WFZX-ray2.60A/B/C/D1-751[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH112. Glycoside Hydrolase Family 112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAJ67290; BAJ67290; BLLJ_1623.
KEGGiblm:BLLJ_1623.
PATRICi46891734. VBIBifLon48544_1679.

Phylogenomic databases

HOGENOMiHOG000015674.
KOiK15533.
OMAiPMHEYTV.

Enzyme and pathway databases

BioCyciBLON565042:GIWN-1685-MONOMER.
BRENDAi2.4.1.211. 851.

Family and domain databases

InterProiIPR029062. Class_I_gatase-like.
IPR012711. Lacto-N-biose_phosphorylase.
[Graphical view]
PfamiPF09508. Lact_bio_phlase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 2 hits.
TIGRFAMsiTIGR02336. TIGR02336. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLNPA_BIFL2
AccessioniPrimary (citable) accession number: E8MF13
Secondary accession number(s): Q5NU17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: April 5, 2011
Last modified: September 7, 2016
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.