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B5CY96

- PORA_BACPM

UniProt

B5CY96 - PORA_BACPM

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Protein

Beta-porphyranase A

Gene

BACPLE_01693

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 sitei53 – 531Substrate
Binding sitei87 – 871Substrate
Binding sitei114 – 1141Substrate
Binding sitei156 – 1561Substrate
Binding sitei237 – 2371Substrate
Binding sitei324 – 3241Substrate
Binding sitei331 – 3311Substrate
Binding sitei342 – 3421Substrate

GO - Molecular functioni

  1. hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-porphyranase A (EC:3.2.1.178)
Alternative name(s):
Glycosyl hydrolase 86 family protein A
Short name:
GH86A
Gene namesi
ORF Names:BACPLE_01693
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 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 728706Beta-porphyranase APRO_0000422034Add
BLAST

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 389Combined sources
Helixi46 – 483Combined sources
Beta strandi50 – 534Combined sources
Helixi60 – 6910Combined sources
Beta strandi75 – 773Combined sources
Helixi80 – 889Combined sources
Beta strandi105 – 1128Combined sources
Turni117 – 1193Combined sources
Helixi126 – 13813Combined sources
Beta strandi141 – 1488Combined sources
Beta strandi150 – 1523Combined sources
Helixi154 – 1563Combined sources
Helixi166 – 18520Combined sources
Turni188 – 1936Combined sources
Beta strandi195 – 2028Combined sources
Turni206 – 2116Combined sources
Helixi212 – 2165Combined sources
Helixi218 – 2258Combined sources
Helixi226 – 2283Combined sources
Beta strandi230 – 24011Combined sources
Helixi252 – 26918Combined sources
Beta strandi275 – 28410Combined sources
Turni294 – 2996Combined sources
Helixi300 – 31213Combined sources
Helixi313 – 3175Combined sources
Beta strandi318 – 3247Combined sources
Helixi330 – 3323Combined sources
Helixi335 – 3373Combined sources
Beta strandi346 – 3505Combined sources
Turni355 – 3573Combined sources
Beta strandi360 – 3623Combined sources
Helixi366 – 3727Combined sources
Beta strandi377 – 38610Combined sources
Beta strandi389 – 3968Combined sources
Beta strandi399 – 4068Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi412 – 4176Combined sources
Turni419 – 4246Combined sources
Beta strandi425 – 43612Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 45011Combined sources
Beta strandi453 – 4575Combined sources
Beta strandi461 – 4699Combined sources
Beta strandi476 – 4849Combined sources
Beta strandi489 – 4913Combined sources
Beta strandi498 – 5058Combined sources
Beta strandi509 – 52113Combined sources
Beta strandi529 – 5324Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi551 – 56212Combined sources
Helixi564 – 5663Combined sources
Beta strandi569 – 5779Combined sources
Beta strandi583 – 59614Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AW7X-ray1.33A30-598[»]
ProteinModelPortaliB5CY96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini599 – 701103CBM-cenCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 782Substrate binding
Regioni151 – 1522Substrate binding

Sequence similaritiesi

Belongs to the glycosyl hydrolase 86 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

B5CY96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYKYIFLLS AFTLGVPPGI YCQGRNEVVV DYNTRRFLSG VSELDRSKYF
60 70 80 90 100
NIHSTSDDDK DVGKFLADYQ VGLGRKFWGP YSYAYNKTHE VGKYPQMKPY
110 120 130 140 150
SGNISVKRYI ATEHPYVQHI QGGIDVQAAG AWSAEYYSNS ELVPEFFEPL
160 170 180 190 200
NEPFVHANDA GFTVQGQAMR ELMVDFYASI GKHIHNNPRL NGKMKVIGYA
210 220 230 240 250
AAYPAWEDGN FNYWNTRMKM FIDRAGAYMD GFSVHLYDGI NVTGTDTKRS
260 270 280 290 300
GSNSEAVLDM VEAYSYIKFG HVKPLAISEF GGIDNSKPDD SYDDISSVRS
310 320 330 340 350
VSSFNHFLFN LMERQDNLFI SIPFVSDKAE WHITAANNYT SYSAALFIPD
360 370 380 390 400
NPQNLKNTTW RLNDKKYFFE LWKNVKGERV DITSSNPDIQ VQAFKDGGRL
410 420 430 440 450
YIALDNLDDN PQTVYLNNKN SWKDVSNVTK RSLYVNYNAG IEYTEQNVPS
460 470 480 490 500
MPESISIVPN QTIVLVADVS SSAFTNSIIR NKYYSSEYLK PISAGSSLSF
510 520 530 540 550
PFTGIESGSG RASLRMSIGR PVSASKKPVV KINGTAVSVP DNWKGYGQSN
560 570 580 590 600
RNIFFGMIEV PFDIQLLKNG DNNVDITFSD GGGHVSSMIL QVEKYTVSTL
610 620 630 640 650
QNGTFSEGLS AWQPLGNYGT VCVQTDNAGN NVACISGHAG LMQRVDMESG
660 670 680 690 700
RTYRFSADVK TEGACKLKVM LQDMSTGTVY TEEFSSPGNY KAVSFDFNST
710 720
VKKVVCAIVC ERQNDAAWID NIVLLPQN
Length:728
Mass (Da):81,281
Last modified:October 14, 2008 - v1
Checksum:i192BD9484B946F0E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
ABQC02000019 Genomic DNA. Translation: EDY95427.1.

Genome annotation databases

EnsemblBacteriaiEDY95427; EDY95427; BACPLE_01693.
PATRICi30481056. VBIBacPle58056_1657.

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: EDY95427.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AW7 X-ray 1.33 A 30-598 [» ]
ProteinModelPortali B5CY96.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EDY95427 ; EDY95427 ; BACPLE_01693 .
PATRICi 30481056. VBIBacPle58056_1657.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02018. CBM_4_9. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 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. "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 (1.33 ANGSTROMS) OF 30-598 IN COMPLEX WITH PORPHYRAN-AGAROSE-OLIGOSACCHARIDE, FUNCTION, CATALYTIC ACTIVITY.
    Strain: DSM 17135 / JCM 12973 / M2.

Entry informationi

Entry nameiPORA_BACPM
AccessioniPrimary (citable) accession number: B5CY96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 22 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 (PubMed:23150581).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