ID GMDS_DICDI Reviewed; 356 AA. AC Q1ZXF7; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=GDP-mannose 4,6 dehydratase; DE EC=4.2.1.47; DE AltName: Full=GDP-D-mannose dehydratase; DE Short=GMD; GN Name=gmd; ORFNames=DDB_G0284553; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Conversion of GDP-D-mannose to GDP-4-keto-6-D- CC deoxymannose. CC -!- CATALYTIC ACTIVITY: GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose CC + H(2)O. CC -!- COFACTOR: NADP (By similarity). CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis CC via de novo pathway; GDP-L-fucose from GDP-D-mannose: step 1/2. CC -!- SIMILARITY: Belongs to the GDP-mannose 4,6-dehydratase family. 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; AAFI02000066; EAS66860.1; -; Genomic_DNA. DR RefSeq; XP_001134543.1; -. DR GeneID; 4238151; -. DR KEGG; ddi:DDB_0231676; -. DR dictyBase; DDB_G0284553; gmd. DR BRENDA; 4.2.1.47; 424. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:EC. DR GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR006368; GDP_Man_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR10366:SF32; GDP_mann_dehyd; 1. DR Pfam; PF01370; Epimerase; 1. DR TIGRFAMs; TIGR01472; gmd; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; NADP. FT CHAIN 1 356 GDP-mannose 4,6 dehydratase. FT /FTId=PRO_0000327628. FT ACT_SITE 138 138 By similarity. FT ACT_SITE 140 140 Nucleophile (By similarity). FT ACT_SITE 162 162 Nucleophile (By similarity). FT BINDING 166 166 NADP (By similarity). SQ SEQUENCE 356 AA; 41061 MW; 9DB1B513B28E16CA CRC64; MSEERKVALI TGITGQDGSY LTEFLISKGY YVHGIIQKIF HHFNTIVKNI YIKIDMLKEK ESLTLHYGDL TDASNLHSIV SKVNPTEIYN LGAQSHVKVS FDMSEYTGDV DGLGCLRLLD AIRSCGMEKK VKYYQASTSE LYGKVQEIPQ SETTPFYPRS PYAVAKQYAY WIVVNYREAY DMYACNGILF NHESPRRGPT FVTRKITRFV AGIACGRDEI LYLGNINAKR DWGHARDYVE AMWLMLQQEK PEDFVIATGE THSVREFVEK SFKEIDIIIK WRGEAEKEEG YCEKTGKVYV KIDEKYYRPT EVDLLLGNPN KAKKLLQWQI KTSFGELVKE MVAKDIEYIK NGDKYN //