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B2T625 (HLDD_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ADP-L-glycero-D-manno-heptose-6-epimerase

EC=5.1.3.20
Alternative name(s):
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Short name=ADP-glyceromanno-heptose 6-epimerase
Short name=ADP-hep 6-epimerase
Short name=AGME
Gene names
Name:hldD
Ordered Locus Names:Bphyt_2995
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose By similarity. HAMAP-Rule MF_01601

Catalytic activity

ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose. HAMAP-Rule MF_01601

Cofactor

Binds 1 NADP+ per subunit By similarity.

Pathway

Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. HAMAP-Rule MF_01601

Subunit structure

Homopentamer By similarity.

Domain

Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain By similarity. HAMAP-Rule MF_01601

Sequence similarities

Belongs to the sugar epimerase family. HldD subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330ADP-L-glycero-D-manno-heptose-6-epimerase HAMAP-Rule MF_01601
PRO_1000190400

Regions

Nucleotide binding11 – 122NADP By similarity
Nucleotide binding32 – 332NADP By similarity
Nucleotide binding75 – 795NADP By similarity
Region200 – 2034Substrate binding By similarity

Sites

Active site1391Proton acceptor By similarity
Active site1771Proton acceptor By similarity
Binding site391NADP By similarity
Binding site541NADP By similarity
Binding site921NADP By similarity
Binding site1431NADP By similarity
Binding site1681Substrate By similarity
Binding site1691NADP; via amide nitrogen By similarity
Binding site1771NADP By similarity
Binding site1791Substrate; via carbonyl oxygen By similarity
Binding site1861Substrate By similarity
Binding site2131Substrate By similarity
Binding site2921Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2T625 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 53972ABD4068592F

FASTA33037,414
        10         20         30         40         50         60 
MTLIVTGAAG FIGSNLVKAL NERGEQRIIA VDNLTRADKF KNLVDCEIDD YLDKTEFVER 

        70         80         90        100        110        120 
FRRGDFGKVR AIFHEGACSD TMETDGRYMM DNNFRYSRDV LDVCLAQNIQ FLYASSAATY 

       130        140        150        160        170        180 
GGSSRFVEER EVEQPLNVYG YSKFLFDQVI RRVLPTAKSQ IAGFRYFNVY GPRETHKARM 

       190        200        210        220        230        240 
ASVAFHNFNQ FRAEGKVKLF GEYNGYAAGE QTRDFVSVED VVKVNLFFFD NPDKSGIFNL 

       250        260        270        280        290        300 
GSGRAQPFND IASTVVNTLR SLNNEPALSL ADQVQRGLIE YIPFPDALRG KYQCFTQADQ 

       310        320        330 
SKLRAAGYDA PFLSVQEGVD RYVRWLFGQV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD17389.1.
RefSeqYP_001896613.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2T625.
SMRB2T625. Positions 3-326.
ModBaseSearch...

Protein-protein interaction databases

STRING398527.Bphyt_2995.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD17389; ACD17389; Bphyt_2995.
GeneID6283544.
KEGGbpy:Bphyt_2995.
PATRIC19216420. VBIBurPhy117947_6964.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0451.
HOGENOMHOG000167987.
KOK03274.
OMAAVNLWFW.
ProtClustDBCLSK896740.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-3033-MONOMER.
UniPathwayUPA00356; UER00440.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01601. Heptose_epimerase.
InterProIPR001509. Epimerase_deHydtase.
IPR011912. Heptose_epim.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR10366:SF29. PTHR10366:SF29. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR02197. heptose_epim. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHLDD_BURPP
AccessionPrimary (citable) accession number: B2T625
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families