ID   HLDD_BORA1              Reviewed;         332 AA.
AC   Q2L2R8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=BAV1359;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48968.1; -; Genomic_DNA.
DR   RefSeq; YP_785881.1; -.
DR   GeneID; 6267183; -.
DR   GenomeReviews; AM167904_GR; BAV1359.
DR   KEGG; bav:BAV1359; -.
DR   HOGENOM; Q2L2R8; -.
DR   OMA; Q2L2R8; 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    332       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255719.
FT   NP_BIND      10     11       NADP (By similarity).
FT   NP_BIND      31     32       NADP (By similarity).
FT   NP_BIND      74     78       NADP (By similarity).
FT   REGION      199    202       Substrate binding (By similarity).
FT   ACT_SITE    138    138       Proton acceptor (By similarity).
FT   ACT_SITE    176    176       Proton acceptor (By similarity).
FT   BINDING      38     38       NADP (By similarity).
FT   BINDING      91     91       NADP (By similarity).
FT   BINDING     142    142       NADP (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     168    168       NADP; via amide nitrogen (By similarity).
FT   BINDING     176    176       NADP (By similarity).
FT   BINDING     178    178       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     185    185       Substrate (By similarity).
FT   BINDING     212    212       Substrate (By similarity).
FT   BINDING     291    291       Substrate (By similarity).
SQ   SEQUENCE   332 AA;  37090 MW;  1D2F969EE3D35EDE CRC64;
     MIVVTGAAGF IGSNLVRGLN RRGIYDIIAI DDLTEGDKFR NLVDCRIADY MHHEDARALL
     KAGQFPRVRA VLHQGACSDT TERNGQYMMD NNYRVTLEWF EYCQANRVPL IYASSAAVYG
     ASTVYVEDPA NEGPLNVYGY SKLLFDQVLR TRMDKLTAQV VGLRYFNVYG PHEQHKGRMA
     SVAFHNMNQF LAEGHVRLFS GWDGYADGGQ SRDFISVEDV VDVNLHFLDH PGTSGIFNCG
     TGRAQPFNDV AAAVVNTLRA EQGEAPLSLD ELVSQGLIRY IPFPDDLKGR YQSFTQANVD
     ALRAAGYTAV MRDVQTGVSE YVRYWRSRKS LA
//