ID HLDD_BURPS STANDARD; PRT; 330 AA. AC Q9WWX6; Q63S12; DT 01-FEB-2005 (Rel. 46, Created) DT 01-FEB-2005 (Rel. 46, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) 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 6- DE 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. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE. 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. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; AF159428; AAD43346.1; -. DR EMBL; BX571965; CAH36516.1; -. DR HSSP; P17963; 1EQ2. DR HAMAP; MF_01601; -; 1. KW Carbohydrate metabolism; Complete proteome; Isomerase; NADP. 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 //