ID   HLDD_BURCM              Reviewed;         330 AA.
AC   Q0BH85;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Bamb_0929;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
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., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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.
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; CP000440; ABI86488.1; -; Genomic_DNA.
DR   RefSeq; YP_772822.1; -.
DR   GeneID; 4310396; -.
DR   GenomeReviews; CP000440_GR; Bamb_0929.
DR   KEGG; bam:Bamb_0929; -.
DR   NMPDR; fig|339670.3.peg.1992; -.
DR   OMA; Q0BH85; FGPNEYH.
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    330       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_1000069344.
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   330 AA;  37060 MW;  A6520F2CF111D8CC CRC64;
     MTVIVTGAAG FIGANIVKAL NERGESRIIA VDNLTRADKF RNLVDCEIDD YLDKTEFVER
     FTRGDFGKVR AVFHEGACSD TMETDGRYMM DNNFRYSRAV LDACLAQGAQ FLYASSAAIY
     GGSTRFVEER EVEAPLNVYG YSKFLFDQVI RRVLPSAKSQ IAGFRYFNVY GPRETHKGRM
     ASVAFHNFNQ FRAEGKVKLF GEYNGYAPGE QTRDFVSVED VAKVNLFFFD HPEKSGIFNL
     GTGRAQPFND IASTVVNTLR ALDNLPPLTL AQQVEQGLIE YVAFPDALRG KYQCFTQADQ
     TKLRSAGYDA PFLTVQEGVD RYVRWLSGQV
//