ID   HLDD_RHOFD              Reviewed;         340 AA.
AC   Q21Y60;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Rfer_1561;
OS   Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
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., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM
RT   15236.";
RL   Submitted (FEB-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; CP000267; ABD69293.1; -; Genomic_DNA.
DR   RefSeq; YP_522824.1; -.
DR   GeneID; 3963268; -.
DR   GenomeReviews; CP000267_GR; Rfer_1561.
DR   KEGG; rfr:Rfer_1561; -.
DR   NMPDR; fig|338969.3.peg.3307; -.
DR   HOGENOM; Q21Y60; -.
DR   OMA; Q21Y60; FGPNEYH.
DR   BioCyc; RFER338969:RFER_1561-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    340       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255739.
FT   NP_BIND      12     13       NADP (By similarity).
FT   NP_BIND      33     34       NADP (By similarity).
FT   NP_BIND      76     80       NADP (By similarity).
FT   REGION      209    212       Substrate binding (By similarity).
FT   ACT_SITE    140    140       Proton acceptor (By similarity).
FT   ACT_SITE    186    186       Proton acceptor (By similarity).
FT   BINDING      40     40       NADP (By similarity).
FT   BINDING      93     93       NADP (By similarity).
FT   BINDING     144    144       NADP (By similarity).
FT   BINDING     177    177       Substrate (By similarity).
FT   BINDING     178    178       NADP; via amide nitrogen (By similarity).
FT   BINDING     186    186       NADP (By similarity).
FT   BINDING     188    188       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     195    195       Substrate (By similarity).
FT   BINDING     222    222       Substrate (By similarity).
FT   BINDING     301    301       Substrate (By similarity).
SQ   SEQUENCE   340 AA;  37384 MW;  83857F2D20C7B210 CRC64;
     MTRIVVTGAA GFIGSNIIQG LNARGLNDII AIDDLTQGDK FRNLAHLKIS DYVDASVFYD
     LFANGAYGQI EAVFHEGACS DTMESNGKYM MDNNYATSVN LFQACQKRGA RLLYASSAAT
     YGGSDTFRED PAFERPLNVY GYSKLLFDQR MRRECGNDFR RSVAGKTGQV VGFRYFNVYG
     PHEQHKGRMA SVAFHQFHQF QAEGKVKLFA DYGGYAAGAQ MRDFIFIDDV VAVNLWFFDH
     PGVSGIFNLG TGRAQPFNDV ASSVVNALRG LSGQTALGLE ALTEAGLIEY IPFPDALRGK
     YQSYTQADLS ALRATGCDHP FADVQTGVSN YVQWLAQQDS
//