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Q2L2R8 (HLDD_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BAV1359
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length332 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 MF_01601

Catalytic activity

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

Cofactor

Binds 1 NADP+ per subunit By similarity. HAMAP MF_01601

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 MF_01601

Subunit structure

Homopentamer By similarity. HAMAP MF_01601

Domain

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

Sequence similarities

Belongs to the sugar epimerase family. HldD subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandNADP
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionADP-glyceromanno-heptose 6-epimerase activity

Inferred from electronic annotation. Source: EC

NADP binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332ADP-L-glycero-D-manno-heptose-6-epimerase HAMAP MF_01601
PRO_0000255719

Regions

Nucleotide binding10 – 112NADP By similarity
Nucleotide binding31 – 322NADP By similarity
Nucleotide binding74 – 785NADP By similarity
Region199 – 2024Substrate binding By similarity

Sites

Active site1381Proton acceptor By similarity
Active site1761Proton acceptor By similarity
Binding site381NADP By similarity
Binding site911NADP By similarity
Binding site1421NADP By similarity
Binding site1671Substrate By similarity
Binding site1681NADP; via amide nitrogen By similarity
Binding site1761NADP By similarity
Binding site1781Substrate; via carbonyl oxygen By similarity
Binding site1851Substrate By similarity
Binding site2121Substrate By similarity
Binding site2911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L2R8 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 1D2F969EE3D35EDE

FASTA33237,090
        10         20         30         40         50         60 
MIVVTGAAGF IGSNLVRGLN RRGIYDIIAI DDLTEGDKFR NLVDCRIADY MHHEDARALL 

        70         80         90        100        110        120 
KAGQFPRVRA VLHQGACSDT TERNGQYMMD NNYRVTLEWF EYCQANRVPL IYASSAAVYG 

       130        140        150        160        170        180 
ASTVYVEDPA NEGPLNVYGY SKLLFDQVLR TRMDKLTAQV VGLRYFNVYG PHEQHKGRMA 

       190        200        210        220        230        240 
SVAFHNMNQF LAEGHVRLFS GWDGYADGGQ SRDFISVEDV VDVNLHFLDH PGTSGIFNCG 

       250        260        270        280        290        300 
TGRAQPFNDV AAAVVNTLRA EQGEAPLSLD ELVSQGLIRY IPFPDDLKGR YQSFTQANVD 

       310        320        330 
ALRAAGYTAV MRDVQTGVSE YVRYWRSRKS LA 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48968.1.
RefSeqYP_785881.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L2R8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2L2R8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267183.
GenomeReviewsGene locus BAV1359 in contig AM167904_GR.
KEGGbav:BAV1359.
PATRIC21128910. VBIBorAvi43433_1378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG755066.
OMARRDFIYV.
ProtClustDBCLSK920182.

Enzyme and pathway databases

BioCycABAU360910:BAV1359-MONOMER.

Family and domain databases

HAMAPMF_01601. Heptose_epimerase.
[Tree]
InterProIPR001509. Epimerase_deHydtase.
IPR011912. Heptose_epim.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK03274.
PANTHERPTHR10366:SF29. Heptose_epim. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR02197. Heptose_epim. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHLDD_BORA1
AccessionPrimary (citable) accession number: Q2L2R8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 40 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