GMDS_CRIGR
ID GMDS_CRIGR Reviewed; 372 AA.
AC Q8K3X3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GDP-mannose 4,6 dehydratase;
DE EC=4.2.1.47 {ECO:0000250|UniProtKB:O60547};
DE AltName: Full=GDP-D-mannose dehydratase;
DE Short=GMD;
GN Name=GMDS; Synonyms=GMD;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Becker D.J., Smith P.L., Petryniak B., Kelly R.J., Myers J.T., Wu B.,
RA Wang P.G., Lowe J.B.;
RT "Glycan-dependent regulation of GDP-mannose 4,6-dehydratase activity.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC deoxy-D-mannose. {ECO:0000250|UniProtKB:O60547}.
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:0000250|UniProtKB:O60547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23821;
CC Evidence={ECO:0000250|UniProtKB:O60547};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:O60547};
CC -!- ACTIVITY REGULATION: Inhibited by GDP-fucose.
CC {ECO:0000250|UniProtKB:O60547}.
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:0000250|UniProtKB:O60547}.
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; AF525364; AAM91925.1; -; mRNA.
DR RefSeq; NP_001233625.1; NM_001246696.1.
DR AlphaFoldDB; Q8K3X3; -.
DR SMR; Q8K3X3; -.
DR STRING; 10029.NP_001233625.1; -.
DR Ensembl; ENSCGRT00001017103; ENSCGRP00001012868; ENSCGRG00001014163.
DR GeneID; 100689436; -.
DR KEGG; cge:100689436; -.
DR CTD; 2762; -.
DR eggNOG; KOG1372; Eukaryota.
DR GeneTree; ENSGT00440000033640; -.
DR OrthoDB; 877551at2759; -.
DR BRENDA; 4.2.1.47; 1309.
DR UniPathway; UPA00128; UER00190.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070401; F:NADP+ binding; ISS:UniProtKB.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019673; P:GDP-mannose metabolic process; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; ISS: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 2: Evidence at transcript level;
KW Acetylation; Lyase; NADP; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT CHAIN 2..372
FT /note="GDP-mannose 4,6 dehydratase"
FT /id="PRO_0000201704"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000250"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 30..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 55..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 86..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 108..112
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60547"
SQ SEQUENCE 372 AA; 41974 MW; D4E256DF97230D2E CRC64;
MAHAPASCPS SRNSGDGDKG KPRKVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF
NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL
AEYTADVDGV GTLRLLDAIK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG
AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL
GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFM HIGKTIVWEG
KNENEVGRCK ETGKIHVTVD LKYYRPTEVD FLQGDCSKAQ QKLNWKPRVA FDELVREMVQ
ADVELMRTNP NA
