ID A0A183BCR7_9TREM Unreviewed; 60 AA.
AC A0A183BCR7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011989};
DE EC=4.2.1.47 {ECO:0000256|ARBA:ARBA00011989};
DE AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|ARBA:ARBA00031085};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001704601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0001704601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937};
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:0000256|ARBA:ARBA00004912}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-mannose 4,6-dehydratase subfamily.
CC {ECO:0000256|ARBA:ARBA00009263}.
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DR AlphaFoldDB; A0A183BCR7; -.
DR WBParaSite; ECPE_0001704601-mRNA-1; ECPE_0001704601-mRNA-1; ECPE_0001704601.
DR UniPathway; UPA00128; UER00190.
DR Proteomes; UP000050740; Unplaced.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 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:SF1; GDP-MANNOSE 4,6 DEHYDRATASE; 1.
DR PANTHER; PTHR43715; GDP-MANNOSE 4,6-DEHYDRATASE; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..59
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 60 AA; 6908 MW; 443F129627D12AAE CRC64;
LELGNLNAER DWGFAGDYVR AMWLMLQQDK PEDFVIASGE KHSVREFTNL AFSHVGIQLR
//