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B5CY92

- PORB_BACPM

UniProt

B5CY92 - PORB_BACPM

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Protein
Beta-porphyranase B
Gene
BACPLE_01689
Organism
Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone.1 Publication

Catalytic activityi

Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721Substrate By similarity
Binding sitei76 – 761Substrate By similarity
Active sitei173 – 1731Nucleophile By similarity
Binding sitei173 – 1731Substrate By similarity
Active sitei178 – 1781Proton donor By similarity
Binding sitei178 – 1781Substrate By similarity
Binding sitei284 – 2841Substrate By similarity

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-porphyranase B (EC:3.2.1.178)
Alternative name(s):
Glycosyl hydrolase 86 family protein B
Short name:
GH16B
Gene namesi
ORF Names:BACPLE_01689
OrganismiBacteroides plebeius (strain DSM 17135 / JCM 12973 / M2)
Taxonomic identifieri484018 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 321301Beta-porphyranase B
PRO_0000422025Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 315
Helixi32 – 354
Beta strandi43 – 475
Helixi49 – 513
Beta strandi57 – 593
Turni62 – 643
Beta strandi65 – 684
Beta strandi70 – 723
Beta strandi79 – 813
Helixi83 – 853
Beta strandi86 – 894
Beta strandi92 – 965
Beta strandi98 – 1047
Helixi106 – 1083
Beta strandi110 – 1189
Beta strandi120 – 1245
Beta strandi130 – 1389
Beta strandi141 – 1444
Beta strandi146 – 1516
Beta strandi155 – 1639
Beta strandi165 – 17915
Turni192 – 1954
Helixi196 – 1983
Beta strandi201 – 21010
Beta strandi216 – 2183
Beta strandi222 – 2243
Turni233 – 2353
Beta strandi238 – 2469
Beta strandi249 – 2546
Beta strandi257 – 2626
Beta strandi277 – 2826
Turni295 – 2984
Turni301 – 3044
Beta strandi305 – 31814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AWDX-ray2.40A/B21-321[»]
ProteinModelPortaliB5CY92.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B5CY92-1 [UniParc]FASTAAdd to Basket

« Hide

MRKTVLYLSA ASLFLSSYTL KNDKEYSLAE EHIKNLPEAP EGYKWVVNED    50
YTDEFNGKRL NAAKWHAKSP YWTNGRPPAT FKAENVSVKK GCLRIINTVL 100
SPTEGLDGKP GDKYRLAGGA VASVKNQAHY GYYETRMKAS LTTMSSTFWL 150
SNRPVMKEIM KGGKKIKTWS SQELDIIETM GIIRSVNPDN PWNKTWNMQM 200
NSNTHYWYQE QGGKRTDNTA KRSDVVSYMT DPSAEDFHTY GCWWVDANTV 250
KFYYDGKYMY TIKPTTKYTD TPFDRPMFIH IVTETYDWEK QVPTAEDLKD 300
KDKSTTYYDW VRAYKLVPIE E 321
Length:321
Mass (Da):37,253
Last modified:October 14, 2008 - v1
Checksum:i56EAC9B6C773F4FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
ABQC02000019 Genomic DNA. Translation: EDY95423.1.

Genome annotation databases

EnsemblBacteriaiEDY95423; EDY95423; BACPLE_01689.
PATRICi30481052. VBIBacPle58056_1655.

Cross-referencesi

Web resourcesi

Protein Spotlight

A gut's tale - Issue 158 of March 2014

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
ABQC02000019 Genomic DNA. Translation: EDY95423.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AWD X-ray 2.40 A/B 21-321 [» ]
ProteinModelPortali B5CY92.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EDY95423 ; EDY95423 ; BACPLE_01689 .
PATRICi 30481052. VBIBacPle58056_1655.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view ]
Pfami PF00722. Glyco_hydro_16. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Draft genome sequence of Bacteroides plebeius (DSM 17135)."
    Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D., Gordon J.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17135 / JCM 12973 / M2.
  2. "Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota."
    Hehemann J.H., Correc G., Barbeyron T., Helbert W., Czjzek M., Michel G.
    Nature 464:908-912(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
    Strain: DSM 17135 / JCM 12973 / M2.
  3. "Bacteria of the human gut microbiome catabolize red seaweed glycans with carbohydrate-active enzyme updates from extrinsic microbes."
    Hehemann J.H., Kelly A.G., Pudlo N.A., Martens E.C., Boraston A.B.
    Proc. Natl. Acad. Sci. U.S.A. 109:19786-19791(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 21-321, FUNCTION, CATALYTIC ACTIVITY.
    Strain: DSM 17135 / JCM 12973 / M2.

Entry informationi

Entry nameiPORB_BACPM
AccessioniPrimary (citable) accession number: B5CY92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Gut bacteria supply the human body with energy from dietary polysaccharides through glycosidases that are absent in the human genome. Beta-porphyranases, which are active on sulfated polysaccharides from marine red algae of the genus Porphyra, are present in marine bacteria. They are absent from metagenome data of gut bacteria, except from the genome of the gut bacterium B.plebeius isolated from Japanese individuals. Seaweeds make an important contribution to the diet in Japan and Porphyra (nori) is the most important nutritional seaweed used to prepare sushi, suggesting that seaweeds with associated marine bacteria have been the route by which genes coding for beta-porphyranases have been transferred in human gut B.plebeius genome (1 Publication and 1 Publication).

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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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