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Q1R4X2 (HLDD_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:UTI89_C4164
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length310 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
   PTMAcetylation
   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 – 310310ADP-L-glycero-D-manno-heptose-6-epimerase HAMAP MF_01601
PRO_0000255729

Regions

Nucleotide binding10 – 112NADP By similarity
Nucleotide binding31 – 322NADP By similarity
Nucleotide binding75 – 795NADP By similarity
Region201 – 2044Substrate binding By similarity

Sites

Active site1401Proton acceptor By similarity
Active site1781Proton acceptor By similarity
Binding site381NADP By similarity
Binding site531NADP By similarity
Binding site921NADP By similarity
Binding site1441NADP By similarity
Binding site1691Substrate By similarity
Binding site1701NADP; via amide nitrogen By similarity
Binding site1781NADP By similarity
Binding site1801Substrate; via carbonyl oxygen By similarity
Binding site1871Substrate By similarity
Binding site2091Substrate By similarity
Binding site2721Substrate By similarity

Amino acid modifications

Modified residue2671N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1R4X2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 499122A87C041522

FASTA31034,894
        10         20         30         40         50         60 
MIIVTGGAGF IGSNIVKALN DKGITDILVV DNLKDGTKFV NLVDLDIADY MDKEDFLIQI 

        70         80         90        100        110        120 
MAGEEFGDVE AIFHEGACSS TTEWDGKYMM DNNYQYSKEL LHYCLEREIP FLYASSAATY 

       130        140        150        160        170        180 
GGRTSDFIES REYEKPLNVY GYSKFLFDEY VRQILPEANS QIVGFRYFNV YGPREGHKGS 

       190        200        210        220        230        240 
MASVAFHLNT QLNNGESPKL FEGSENFKRD FVYVGDVADV NLWFLENGVS GIFNLGTGRA 

       250        260        270        280        290        300 
ESFQAVADAT LAYHKKGQIE YIPFPDKLKG RYQAFTQADL TNLRAAGYDK PFKTVAEGVT 

       310 
EYMAWLNRDA

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000243 Genomic DNA. Translation: ABE09592.1.
RefSeqYP_543123.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R4X2.
SMRQ1R4X2. Positions 1-307.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R4X2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000067620; EBESCP00000065098; EBESCG00000066667.
GeneID3989625.
GenomeReviewsGene locus UTI89_C4164 in contig CP000243_GR.
KEGGeci:UTI89_C4164.
PATRIC18457750. VBIEscCol42261_4072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0451.
GeneTreeEBGT00050000008810.
HOGENOMHBG755066.
OMARRDFIYV.
ProtClustDBPRK11150.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C4164-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_ECOUT
AccessionPrimary (citable) accession number: Q1R4X2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 43 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

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