GMD2_CAEEL
ID GMD2_CAEEL Reviewed; 382 AA.
AC O45583; Q1H8X4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GDP-mannose 4,6 dehydratase 2;
DE EC=4.2.1.47;
DE AltName: Full=GDP-D-mannose dehydratase;
DE Short=GMD;
GN Name=gmd-2; ORFNames=F56H6.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-382, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND DEVELOPMENTAL STAGE.
RX PubMed=16650000; DOI=10.1111/j.1742-4658.2006.05239.x;
RA Rhomberg S., Fuchsluger C., Rendic D., Paschinger K., Jantsch V., Kosma P.,
RA Wilson I.B.H.;
RT "Reconstitution in vitro of the GDP-fucose biosynthetic pathways of
RT Caenorhabditis elegans and Drosophila melanogaster.";
RL FEBS J. 273:2244-2256(2006).
CC -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC deoxy-D-mannose. {ECO:0000269|PubMed:16650000}.
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:0000269|PubMed:16650000};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 16-23 degrees Celsius.
CC {ECO:0000269|PubMed:16650000};
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:16650000}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:16650000}.
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; Z81553; CAB04494.1; -; Genomic_DNA.
DR EMBL; AM231685; CAJ77754.1; -; mRNA.
DR PIR; T22798; T22798.
DR RefSeq; NP_493106.1; NM_060705.1.
DR AlphaFoldDB; O45583; -.
DR SMR; O45583; -.
DR BioGRID; 51157; 1.
DR STRING; 6239.F56H6.5; -.
DR EPD; O45583; -.
DR PaxDb; O45583; -.
DR PeptideAtlas; O45583; -.
DR EnsemblMetazoa; F56H6.5.1; F56H6.5.1; WBGene00010166.
DR GeneID; 186416; -.
DR KEGG; cel:CELE_F56H6.5; -.
DR UCSC; F56H6.5; c. elegans.
DR CTD; 186416; -.
DR WormBase; F56H6.5; CE16133; WBGene00010166; gmd-2.
DR eggNOG; KOG1372; Eukaryota.
DR GeneTree; ENSGT00440000033640; -.
DR HOGENOM; CLU_007383_14_0_1; -.
DR InParanoid; O45583; -.
DR OMA; LEKGYEX; -.
DR OrthoDB; 877551at2759; -.
DR PhylomeDB; O45583; -.
DR UniPathway; UPA00128; UER00190.
DR PRO; PR:O45583; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00010166; Expressed in pharyngeal muscle cell (C elegans) and 1 other tissue.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IDA:UniProtKB.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IBA:GO_Central.
DR GO; GO:0042350; P:GDP-L-fucose biosynthetic process; IDA:WormBase.
DR GO; GO:0019673; P:GDP-mannose metabolic process; IDA:UniProtKB.
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 Lyase; NADP; Reference proteome.
FT CHAIN 1..382
FT /note="GDP-mannose 4,6 dehydratase 2"
FT /id="PRO_0000201709"
FT ACT_SITE 166
FT /evidence="ECO:0000250"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 40..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 43071 MW; 1A3437F87872B457 CRC64;
MEARNAEGLE SCIEKIQEVK LSSFAELKAF RERKVALITG ITGQDGSYLA ELLLSKGYKV
HGIIRRSSSF NTARIEHLYG NPVTHNGSAS FSLHYGDMTD SSCLIKLIST IEPTEIYHLA
AQSHVKVSFD LPEYTAEVDA VGTLRLLDAI HACRLTEKVR FYQASTSELY GKVQEIPQSE
LTPFYPRSPY AVAKMYGYWI VVNYREAYKM FACNGILFNH ESPRRGETFV TRKITRSVAK
ISLRQQEHIE LGNLSALRDW GHAKEYVEAM WRILQQDTPD DFVIATGKQF SVREFCNLAF
AEIGEQLVWE GEGVDEVGKN QDGVVRVKVS PKYYRPTEVE TLLGNPAKAR KTLGWEPKIT
VPELVKEMVA SDIALMEADP MA
