GMDS_DICDI
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 03-AUG-2022, entry version 95.
DE RecName: Full=GDP-mannose 4,6 dehydratase;
DE EC=4.2.1.47 {ECO:0000305|PubMed:19614564};
DE AltName: Full=GDP-D-mannose dehydratase {ECO:0000303|PubMed:19614564};
DE Short=GMD {ECO:0000303|PubMed:19614564};
GN Name=gmd; ORFNames=DDB_G0284553;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=HL250;
RX PubMed=19614564; DOI=10.1042/bj20090786;
RA Schiller B., Hykollari A., Voglmeir J., Poltl G., Hummel K.,
RA Razzazi-Fazeli E., Geyer R., Wilson I.B.H.;
RT "Development of Dictyostelium discoideum is associated with alteration of
RT fucosylated N-glycan structures.";
RL Biochem. J. 423:41-52(2009).
RN [2]
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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 62-98; 131-159; 218-229; 271-280; 306-321 AND 324-344,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Participates in the synthesis of GDP-L-fucose, catalyzing the
CC conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-4-
CC dehydro-alpha-D-rhamnose) which is further catalyzed by GDP-L-fucose
CC synthase (ger) (PubMed:19614564). GDP-L-fucose is important for the
CC synthesis of fucosylated N-glycans which are expressed on the cell
CC surface (PubMed:19614564). {ECO:0000269|PubMed:19614564,
CC ECO:0000303|PubMed:19614564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:57964; EC=4.2.1.47;
CC Evidence={ECO:0000305|PubMed:19614564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23821;
CC Evidence={ECO:0000305|PubMed:19614564};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC {ECO:0000269|PubMed:19614564}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000066; EAS66860.1; -; Genomic_DNA.
DR RefSeq; XP_001134543.1; XM_001134543.1.
DR AlphaFoldDB; Q1ZXF7; -.
DR SMR; Q1ZXF7; -.
DR STRING; 44689.DDB0231676; -.
DR PaxDb; Q1ZXF7; -.
DR EnsemblProtists; EAS66860; EAS66860; DDB_G0284553.
DR GeneID; 8624624; -.
DR KEGG; ddi:DDB_G0284553; -.
DR dictyBase; DDB_G0284553; gmd.
DR eggNOG; KOG1372; Eukaryota.
DR HOGENOM; CLU_007383_14_1_1; -.
DR InParanoid; Q1ZXF7; -.
DR OMA; TDCLYLG; -.
DR PhylomeDB; Q1ZXF7; -.
DR Reactome; R-DDI-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00128; UER00190.
DR PRO; PR:Q1ZXF7; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IDA:dictyBase.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IMP:dictyBase.
DR GO; GO:0019673; P:GDP-mannose metabolic process; IDA:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
DR HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR InterPro; IPR006368; GDP_Man_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43715; PTHR43715; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01472; gmd; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; NADP; Reference proteome.
FT CHAIN 1..356
FT /note="GDP-mannose 4,6 dehydratase"
FT /id="PRO_0000327628"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VARIANT 108
FT /note="G -> D (in strain: HL250; loss of activity)"
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
