ID HLDD_HAES1 Reviewed; 309 AA. AC Q0I569; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase; DE EC=5.1.3.20; DE AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase; DE Short=ADP-glyceromanno-heptose 6-epimerase; DE Short=ADP-hep 6-epimerase; DE Short=AGME; GN Name=hldD; Synonyms=rfaD; OrderedLocusNames=HS_1613; OS Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17172329; DOI=10.1128/JB.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) RT strain 129Pt and comparison to Haemophilus ducreyi 35000HP and RT Haemophilus influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). CC -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero- CC beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an CC epimerization at carbon 6 of the heptose (By similarity). CC -!- CATALYTIC ACTIVITY: ADP-D-glycero-D-manno-heptose = ADP-L-glycero- CC D-manno-heptose. CC -!- COFACTOR: Binds 1 NADP(+) per subunit (By similarity). CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. CC -!- SUBUNIT: Homopentamer (By similarity). CC -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a CC smaller C-terminal substrate-binding domain (By similarity). CC -!- SIMILARITY: Belongs to the sugar epimerase family. HldD subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000436; ABI25881.1; -; Genomic_DNA. DR RefSeq; YP_719818.1; -. DR SMR; Q0I569; 1-306. DR GeneID; 4241140; -. DR GenomeReviews; CP000436_GR; HS_1613. DR KEGG; hso:HS_1613; -. DR HOGENOM; Q0I569; -. DR OMA; Q0I569; FGPNEYH. DR BioCyc; HSOM205914:HS_1613-MON; -. DR GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:HAMAP. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:HAMAP. DR GO; GO:0044237; P:cellular metabolic process; IEA:InterPro. DR HAMAP; MF_01601; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR011912; Heptose_epim. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR10366:SF29; Heptose_epim; 1. DR Pfam; PF01370; Epimerase; 1. DR TIGRFAMs; TIGR02197; heptose_epim; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; NADP. FT CHAIN 1 309 ADP-L-glycero-D-manno-heptose-6- FT epimerase. FT /FTId=PRO_0000323479. FT NP_BIND 10 11 NADP (By similarity). FT NP_BIND 31 32 NADP (By similarity). FT NP_BIND 75 79 NADP (By similarity). FT REGION 200 203 Substrate binding (By similarity). FT ACT_SITE 139 139 Proton acceptor (By similarity). FT ACT_SITE 177 177 Proton acceptor (By similarity). FT BINDING 38 38 NADP (By similarity). FT BINDING 53 53 NADP (By similarity). FT BINDING 92 92 NADP (By similarity). FT BINDING 143 143 NADP (By similarity). FT BINDING 168 168 Substrate (By similarity). FT BINDING 169 169 NADP; via amide nitrogen (By similarity). FT BINDING 177 177 NADP (By similarity). FT BINDING 179 179 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 186 186 Substrate (By similarity). FT BINDING 208 208 Substrate (By similarity). FT BINDING 271 271 Substrate (By similarity). SQ SEQUENCE 309 AA; 34866 MW; 790866DF9509FF7E CRC64; MIIVTGGAGL IGSNIIAALN DMGRRDILVV DNLTDGTKFV NLVDLDIADY CDKEDFIASI IAGDDFGDID AIFHQGACSA TTEWNGKYLM QNNYEYSKEL LHYCLLREIP FFYASSAATY GDKTDFIEER QFEGPLNVYG YSKFLFDEYV RQILPQATSP VCGFKYFNVY GPREQHKGSM ASVAFHLNNQ MLKGENPKLF AGSEHFLRDF VYVGDVAKVN LWAWQHGISG IYNCGTGRAE SFEQVARAVL NYHGKGEIET IPFPEHLKSR YQEYTQANLT KLRAAGYQAE FKSVAEGVAE YMQWLNRKS //