ID   HLDD_RALME              Reviewed;         331 AA.
AC   Q1LQG2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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; OrderedLocusNames=Rmet_0728;
OS   Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A.,
RA   Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of the chromosome of Ralstonia metallidurans
RT   CH34.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP000352; ABF07614.1; -; Genomic_DNA.
DR   RefSeq; YP_582883.1; -.
DR   GeneID; 4037519; -.
DR   GenomeReviews; CP000352_GR; Rmet_0728.
DR   KEGG; rme:Rmet_0728; -.
DR   HOGENOM; Q1LQG2; -.
DR   OMA; Q1LQG2; FGPNEYH.
DR   BioCyc; RMET266264:RMET_0728-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    331       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255738.
FT   NP_BIND      11     12       NADP (By similarity).
FT   NP_BIND      32     33       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      39     39       NADP (By similarity).
FT   BINDING      54     54       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     213    213       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
SQ   SEQUENCE   331 AA;  37354 MW;  7D72B08B70E48514 CRC64;
     MTIIVTGAAG FIGSNIVKGL NERGETNIIA VDNLTRAEKF NNLVDCEIAD YLDKTDFVAR
     FARGDFGNVR AVFHEGACSD TMETDGRYMM ENNYRYTLAL LEACLEQGAQ FLYASSAATY
     GASTMFREDR DYEKPLNVYG YSKFLFDQVV RRRLPSAHSQ IVGFRYFNVY GPREFHKGRM
     ASVAFHHFNQ FRAEGTVKLF GEYNGYAPGT QSRDFVSVED VVKVNLYFLD HPEKSGIFNL
     GTGRSQPFND IAVSVVNALR ESEGKPALSL DEMVQEGLVE YVKFPDALRG KYQCFTQSDV
     SRLRGAGYSD QFLTVQEGVS RYCKWLLERS A
//