ID   HLDD_BURPS     STANDARD;      PRT;   330 AA.
AC   Q9WWX6; Q63S12;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   07-MAR-2006, entry version 23.
DE   ADP-L-glycero-D-manno-heptose-6-epimerase (EC 5.1.3.20) (ADP-L-
DE   glycero-beta-D-manno-heptose-6-epimerase) (ADP-glyceromanno-heptose
DE   6-epimerase) (ADP-hep 6-epimerase) (AGME).
GN   Name=hldD; Synonyms=gmhD; OrderedLocusNames=BPSL2509;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1026b;
RX   MEDLINE=20011168; PubMed=10543742;
RA   Burtnick M.N., Woods D.E.;
RT   "Isolation of polymyxin B-susceptible mutants of Burkholderia
RT   pseudomallei and molecular characterization of genetic loci involved
RT   in polymyxin B resistance.";
RL   Antimicrob. Agents Chemother. 43:2648-2656(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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   -!- 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; AF159428; AAD43346.1; -; Genomic_DNA.
DR   EMBL; BX571965; CAH36516.1; -; Genomic_DNA.
DR   HSSP; P17963; 1EQ2.
DR   GenomeReviews; BX571965_GR; BPSL2509.
DR   HAMAP; MF_01601; -; 1.
DR   InterPro; IPR001509; Epimerase_Dh.
DR   InterPro; IPR011912; Heptose_epim.
DR   PANTHER; PTHR10366:SF34; Heptose_epim; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   TIGRFAMs; TIGR02197; heptose_epim; 1.
KW   Carbohydrate metabolism; Complete proteome; Isomerase; NADP.
FT   CHAIN         1    330       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000205790.
FT   NP_BIND       7     13       ADP (By similarity).
FT   ACT_SITE    116    116       By similarity.
FT   ACT_SITE    139    139       By similarity.
FT   ACT_SITE    143    143       By similarity.
FT   CONFLICT     64     64       G -> S (in Ref. 1).
FT   CONFLICT    242    242       T -> A (in Ref. 1).
FT   CONFLICT    302    302       T -> K (in Ref. 1).
SQ   SEQUENCE   330 AA;  37019 MW;  3DBF6A129000E524 CRC64;
     MTLIVTGAAG FIGANIVKAL NERGETRIIA VDNLTRADKF KNLVDCEIDD YLDKTEFVER
     FARGDFGKVR AVFHEGACSD TMETDGRYMM DNNFRYSRAV LDACLAQGTQ FLYASSAAIY
     GGSSRFVEAR EFEAPLNVYG YSKFLFDQVI RRVMPSAKSQ IAGFRYFNVY GPRESHKGRM
     ASVAFHNFNQ FRAEGKVKLF GEYNGYGPGE QTRDFVSVED VAKVNLHFFD HPQKSGIFNL
     GTGRAQPFND IATTVVNTLR ALEGQPALTL AEQVEQGLVE YVPFPDALRG KYQCFTQADQ
     TTLRAAGYDA PFLTVQEGVD RYVRWLFGQL
//