UniProt Accession

 HLDD_ECOLI; P67910; P17963; Q2M7T3 

Genbank Protein ID

 M33577; X54492; U00039; U00096; AP009048 

Genbank Nucleotide ID

 AAA24525.1; CAA38364.1; AAB18596.1; AAC76643.1; BAE77673.1 

Protein Name

 ADP-L-glycero-D-manno-heptose-6-epimerase 

Protein Synonyms/Alias

 ADP-L-glycero-beta-D-manno-heptose-6-epimerase; ADP-glyceromanno-heptose 6-epimerase; ADP-hep 6-epimerase; AGME 

Gene Name

 hldD 

Gene Synonyms/Alias

 htrM; rfaD; waaD; b3619; JW3594 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
22	IVKALNDKGITDILV	acetylation	[1]
34	ILVVDNLKDGTKFVN	acetylation	[1]
135	IESREYEKPLNVYGY	acetylation	[1]
208	FEGSENFKRDFVYVG	acetylation	[1]
255	DATLAYHKKGQIEYI	acetylation	[1]
256	ATLAYHKKGQIEYIP	acetylation	[1]
267	EYIPFPDKLKGRYQA	acetylation	[1, 2, 3]
269	IPFPDKLKGRYQAFT	acetylation	[1]
290	LRAAGYDKPFKTVAE	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 10 11 NADP.
 NP_BIND 31 32 NADP.
 NP_BIND 75 79 NADP.
 REGION 201 204 Substrate binding.
 ACT_SITE 140 140 Proton acceptor.
 ACT_SITE 178 178 Proton acceptor.
 BINDING 38 38 NADP.
 BINDING 53 53 NADP.
 BINDING 92 92 NADP.
 BINDING 144 144 NADP.
 BINDING 169 169 Substrate.
 BINDING 170 170 NADP; via amide nitrogen.
 BINDING 178 178 NADP.
 BINDING 180 180 Substrate; via carbonyl oxygen.
 BINDING 187 187 Substrate.
 BINDING 209 209 Substrate.
 BINDING 272 272 Substrate.
 MOD_RES 267 267 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Isomerase; Lipopolysaccharide biosynthesis; NAD; NADP; Reference proteome; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 310 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IDA:EcoCyc.
 GO:0070401; F:NADP+ binding; IDA:EcoCyc.
 GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW. 

Interpro

 IPR001509; Epimerase_deHydtase.
 IPR011912; Heptose_epim.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF01370; Epimerase 

SMART

  

PROSITE

  

PRINTS