ID   HLDD_SHEFN              Reviewed;         317 AA.
AC   Q07W60;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Sfri_3929;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
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   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
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.
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DR   EMBL; CP000447; ABI73754.1; -; Genomic_DNA.
DR   RefSeq; YP_752593.1; -.
DR   GeneID; 4280820; -.
DR   GenomeReviews; CP000447_GR; Sfri_3929.
DR   KEGG; sfr:Sfri_3929; -.
DR   NMPDR; fig|318167.10.peg.3747; -.
DR   HOGENOM; Q07W60; -.
DR   OMA; Q07W60; 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    317       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_1000069367.
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      198    201       Substrate binding (By similarity).
FT   ACT_SITE    139    139       Proton acceptor (By similarity).
FT   ACT_SITE    175    175       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     166    166       Substrate (By similarity).
FT   BINDING     167    167       NADP; via amide nitrogen (By similarity).
FT   BINDING     175    175       NADP (By similarity).
FT   BINDING     177    177       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     184    184       Substrate (By similarity).
FT   BINDING     211    211       Substrate (By similarity).
FT   BINDING     275    275       Substrate (By similarity).
SQ   SEQUENCE   317 AA;  35735 MW;  43BB16220B4E2652 CRC64;
     MIVVTGAAGF IGSNLVKQLN AMGRNDIIAV DDLTDGTQMF NLADCEIADY LDKDDFIKQI
     KAGDFDNKLE VIFHQGACSS TTEWDGKFMM ANNFEYSKTL LHYSQANNCQ FIYASSASVY
     GGSEKFIEQR ELEKPLNVYA YSKFLFDQYV RQQKLTGQVA GLRYFNVYGP REQHKGGMAS
     VAFHFNNQIN TNGVCRLFEG VDGYENGQQL RDFVFVEDVV KVNLWLWQNP SVSGIYNCGT
     GQAQSFNDVA NAVIAYHGKG HIEYIPFPDK LKGAYQSYTQ ADLTQLRAAG YQGEFKTVEQ
     AVPEYLDWLK TQHFIGQ
//