Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q84HQ2 (Q84HQ2_BIFAD) Unreviewed, UniProtKB/TrEMBL

Last modified July 27, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
EC=2.4.1.7 EMBL AAO33821.1
Gene names
Name:sucP EMBL AAO33821.1
OrganismBifidobacterium adolescentis EMBL AAO33821.1
Taxonomic identifier1680 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region50 – 534Sucrose binding PDB 2GDU
Region190 – 1923Sucrose binding PDB 2GDU
Region289 – 2902Sucrose binding PDB 2GDU
Region342 – 3454Sucrose binding PDB 2GDU

Sites

Binding site881Sucrose PDB 2GDU
Binding site1561Sucrose PDB 2GDU
Binding site3991Sucrose PDB 2GDU

Amino acid modifications

Modified residue3561Cysteine sulfinic acid (-SO2H) PDB 2GDU PDB 1R7A

Sequences

Sequence LengthMass (Da)Tools
Q84HQ2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 10705FE3182E5754

FASTA50456,190
        10         20         30         40         50         60 
MKNKVQLITY ADRLGDGTIK SMTDILRTRF DGVYDGVHIL PFFTPFDGAD AGFDPIDHTK 

        70         80         90        100        110        120 
VDERLGSWDD VAELSKTHNI MVDAIVNHMS WESKQFQDVL AKGEESEYYP MFLTMSSVFP 

       130        140        150        160        170        180 
NGATEEDLAG IYRPRPGLPF THYKFAGKTR LVWVSFTPQQ VDIDTDSDKG WEYLMSIFDQ 

       190        200        210        220        230        240 
MAASHVSYIR LDAVGYGAKE AGTSCFMTPK TFKLISRLRE EGVKRGLEIL IEVHSYYKKQ 

       250        260        270        280        290        300 
VEIASKVDRV YDFALPPLLL HALSTGHVEP VAHWTDIRPN NAVTVLDTHD GIGVIDIGSD 

       310        320        330        340        350        360 
QLDRSLKGLV PDEDVDNLVN TIHANTHGES QAATGAAASN LDLYQVNSTY YSALGCNDQH 

       370        380        390        400        410        420 
YIAARAVQFF LPGVPQVYYV GALAGKNDME LLRKTNNGRD INRHYYSTAE IDENLKRPVV 

       430        440        450        460        470        480 
KALNALAKFR NELDAFDGTF SYTTDDDTSI SFTWRGETSQ ATLTFEPKRG LGVDNTTPVA 

       490        500 
MLEWEDSAGD HRSDDLIANP PVVA 

« Hide

References

[1]"Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083."
van den Broek L.A., van Boxtel E.L., Kievit R.P., Verhoef R., Beldman G., Voragen A.G.
Appl. Microbiol. Biotechnol. 65:219-227(2004) [PubMed: 14740189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 20083 EMBL AAO33821.1.
[2]"Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis."
Sprogoe D., van den Broek L.A., Mirza O., Kastrup J.S., Voragen A.G., Gajhede M., Skov L.K.
Biochemistry 43:1156-1162(2004) [PubMed: 14756551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 20083 EMBL AAO33821.1.
[3]Van den Broek L.A.M., Van Boxtel E.L., Beldman G., Voragen A.G.J.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 20083 EMBL AAO33821.1.
[4]"Structural rearrangements of Sucrose Phosphorylase from Bifidobacterium adolescentis during sucrose conversion."
Mirza O., Skov L.K., Sprogoe D., Van den Broek L.A.M., Voragen A.G.J., Katsrup J.S., Gajhede M.
Submitted (MAR-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[5]"Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion."
Mirza O., Skov L.K., Sprogoe D., van den Broek L.A., Beldman G., Kastrup J.S., Gajhede M.
J. Biol. Chem. 281:35576-35584(2006) [PubMed: 16990265] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SUCROSE, SULFINATION AT CYS-356.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF543301 Genomic DNA. Translation: AAO33821.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R7AX-ray1.77A/B1-504[»]
2GDUX-ray2.10A/B1-504[»]
2GDVX-ray2.00A/B1-504[»]
ProteinModelPortalQ84HQ2.
SMRQ84HQ2. Positions 1-504.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBQ84HQ2.

Enzyme and pathway databases

BRENDA2.4.1.7. 1589.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR015325. Suc_Porlyase_C.
IPR016377. Sucrose_phosphorylase.
IPR022527. Sucrose_phosphorylase_GftA.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09244. DUF1964. 1 hit.
[Graphical view]
PIRSFPIRSF003059. Sucrose_phosphorylase. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR03852. Sucrose_gtfA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ84HQ2_BIFAD
AccessionPrimary (citable) accession number: Q84HQ2
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 27, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)