Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei313Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi32R → E: Lack of activity. 1 Publication1
Mutagenesisi166N → A: Strong decrease in activity. 1 Publication1
Mutagenesisi210R → E: Lack of activity. 1 Publication1
Mutagenesisi358R → E: Lack of activity. 1 Publication1
Mutagenesisi362Y → F: Strong decrease in activity. 1 Publication1
Mutagenesisi362Y → N: Lack of activity. 1 Publication1
Mutagenesisi364F → N: Decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004240701 – 7511,3-beta-galactosyl-N-acetylhexosamine phosphorylaseAdd BLAST751

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1751
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi16 – 26Combined sources11
Beta strandi29 – 32Combined sources4
Helixi43 – 46Combined sources4
Beta strandi49 – 54Combined sources6
Helixi61 – 64Combined sources4
Helixi68 – 70Combined sources3
Beta strandi73 – 77Combined sources5
Beta strandi84 – 93Combined sources10
Turni98 – 100Combined sources3
Beta strandi101 – 103Combined sources3
Helixi109 – 112Combined sources4
Beta strandi114 – 117Combined sources4
Turni118 – 121Combined sources4
Beta strandi122 – 124Combined sources3
Helixi126 – 128Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi133 – 142Combined sources10
Beta strandi148 – 157Combined sources10
Helixi161 – 169Combined sources9
Helixi186 – 201Combined sources16
Beta strandi208 – 212Combined sources5
Beta strandi219 – 222Combined sources4
Beta strandi226 – 232Combined sources7
Helixi237 – 239Combined sources3
Helixi242 – 252Combined sources11
Helixi259 – 262Combined sources4
Helixi263 – 265Combined sources3
Turni266 – 268Combined sources3
Helixi276 – 302Combined sources27
Beta strandi306 – 314Combined sources9
Turni316 – 318Combined sources3
Helixi325 – 328Combined sources4
Beta strandi332 – 339Combined sources8
Helixi340 – 347Combined sources8
Beta strandi351 – 361Combined sources11
Turni365 – 367Combined sources3
Helixi375 – 391Combined sources17
Beta strandi395 – 398Combined sources4
Helixi403 – 407Combined sources5
Helixi410 – 430Combined sources21
Beta strandi439 – 447Combined sources9
Helixi448 – 451Combined sources4
Turni452 – 456Combined sources5
Turni465 – 467Combined sources3
Helixi468 – 478Combined sources11
Beta strandi480 – 488Combined sources9
Helixi489 – 495Combined sources7
Beta strandi503 – 508Combined sources6
Turni513 – 515Combined sources3
Helixi517 – 521Combined sources5
Helixi523 – 534Combined sources12
Beta strandi538 – 544Combined sources7
Beta strandi547 – 552Combined sources6
Beta strandi555 – 557Combined sources3
Helixi560 – 563Combined sources4
Beta strandi564 – 567Combined sources4
Turni587 – 591Combined sources5
Helixi596 – 605Combined sources10
Turni612 – 614Combined sources3
Beta strandi619 – 621Combined sources3
Beta strandi635 – 639Combined sources5
Beta strandi642 – 646Combined sources5
Helixi648 – 650Combined sources3
Beta strandi653 – 659Combined sources7
Beta strandi662 – 668Combined sources7
Helixi674 – 687Combined sources14
Helixi691 – 694Combined sources4
Beta strandi698 – 701Combined sources4
Beta strandi704 – 709Combined sources6
Turni710 – 713Combined sources4
Beta strandi714 – 719Combined sources6
Beta strandi721 – 723Combined sources3
Beta strandi725 – 730Combined sources6
Beta strandi736 – 741Combined sources6
Beta strandi746 – 749Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
SMRiE8MF13.
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
PDB 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[»]
SMRiE8MF13.
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

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: November 2, 2016
This is version 28 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.