ID   HLDD_POLSJ              Reviewed;         335 AA.
AC   Q12CM2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Bpro_1784;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591;
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Richardson P.;
RT   "Complete sequence of chromosome of Polaromonas sp. JS666.";
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; CP000316; ABE43720.1; -; Genomic_DNA.
DR   RefSeq; YP_548618.1; -.
DR   GeneID; 4015569; -.
DR   GenomeReviews; CP000316_GR; Bpro_1784.
DR   KEGG; pol:Bpro_1784; -.
DR   NMPDR; fig|296591.1.peg.2822; -.
DR   HOGENOM; Q12CM2; -.
DR   OMA; Q12CM2; FGPNEYH.
DR   BioCyc; PSP296591:BPRO_1784-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    335       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255736.
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      204    207       Substrate binding (By similarity).
FT   ACT_SITE    139    139       Proton acceptor (By similarity).
FT   ACT_SITE    181    181       Proton acceptor (By similarity).
FT   BINDING      39     39       NADP (By similarity).
FT   BINDING      92     92       NADP (By similarity).
FT   BINDING     143    143       NADP (By similarity).
FT   BINDING     172    172       Substrate (By similarity).
FT   BINDING     173    173       NADP; via amide nitrogen (By similarity).
FT   BINDING     181    181       NADP (By similarity).
FT   BINDING     183    183       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   BINDING     217    217       Substrate (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
SQ   SEQUENCE   335 AA;  36962 MW;  E406A44F92E1A782 CRC64;
     MKIVVTGAAG FIGSNLVKGL NDRGIDDIIA VDDLTHGDKF RNLADLQIAD YIDADDFYDL
     FAEGAFGQVE AVFHEGACSD TMELDGKYMM DNNYTLSCEL FHACQEQGTR LLYASSAATY
     GGSDTFSESP EFERPLNVYG YSKLLFDQRM RRELGARFEN AATQVAGFRY FNVYGPREQH
     KGRMASVAFH QFNQFQAEGK VKLFGDYGGY QAGGQMRDFV FIDDVVAVNL WFLDHPEKSG
     IFNLGTGRAQ PFNDVALAVV NTLRQSQNAA AMSLEDAVRG GLIDYITFPP ALVGKYQSYT
     QADLQALRAA GCQHAFADVQ TGVAAYMQWL ASAKI
//