GMD1_ARATH
ID GMD1_ARATH Reviewed; 361 AA.
AC Q9SNY3; Q058I8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=GDP-mannose 4,6 dehydratase 1;
DE EC=4.2.1.47;
DE AltName: Full=GDP-D-mannose dehydratase 1;
DE Short=GMD 1;
GN Name=GMD1; OrderedLocusNames=At5g66280; ORFNames=K1L20.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Bonin C.P., Reiter W.-D.;
RT "The GMD1 gene of Arabidopsis thaliana encodes an isoform of GDP-D-mannose
RT 4,6-dehydratase that is expressed in roots and pollen.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12805618; DOI=10.1104/pp.103.022368;
RA Bonin C.P., Freshour G., Hahn M.G., Vanzin G.F., Reiter W.D.;
RT "The GMD1 and GMD2 genes of Arabidopsis encode isoforms of GDP-D-mannose
RT 4,6-dehydratase with cell type-specific expression patterns.";
RL Plant Physiol. 132:883-892(2003).
CC -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC deoxy-D-mannose. {ECO:0000269|PubMed:12805618}.
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:12805618};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots,stipules and pollen just before
CC anthesis. Primarily localized to the root meristem and columella root
CC cap. Not expressed in emerging lateral roots.
CC {ECO:0000269|PubMed:12805618}.
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; AF195140; AAF07199.1; -; mRNA.
DR EMBL; AB022211; BAB10707.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98194.1; -; Genomic_DNA.
DR EMBL; BT029230; ABJ98562.1; -; mRNA.
DR RefSeq; NP_201429.1; NM_126026.3.
DR AlphaFoldDB; Q9SNY3; -.
DR SMR; Q9SNY3; -.
DR BioGRID; 22002; 6.
DR IntAct; Q9SNY3; 2.
DR STRING; 3702.AT5G66280.1; -.
DR iPTMnet; Q9SNY3; -.
DR PaxDb; Q9SNY3; -.
DR PRIDE; Q9SNY3; -.
DR ProteomicsDB; 248434; -.
DR EnsemblPlants; AT5G66280.1; AT5G66280.1; AT5G66280.
DR GeneID; 836760; -.
DR Gramene; AT5G66280.1; AT5G66280.1; AT5G66280.
DR KEGG; ath:AT5G66280; -.
DR Araport; AT5G66280; -.
DR TAIR; locus:2155036; AT5G66280.
DR eggNOG; KOG1372; Eukaryota.
DR HOGENOM; CLU_007383_14_0_1; -.
DR InParanoid; Q9SNY3; -.
DR OMA; TDCLYLG; -.
DR OrthoDB; 877551at2759; -.
DR PhylomeDB; Q9SNY3; -.
DR BioCyc; ARA:AT5G66280-MON; -.
DR BRENDA; 4.2.1.47; 399.
DR UniPathway; UPA00128; UER00190.
DR PRO; PR:Q9SNY3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SNY3; differential.
DR Genevisible; Q9SNY3; AT.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IBA:GO_Central.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IBA:GO_Central.
DR GO; GO:0019673; P:GDP-mannose metabolic process; IBA:GO_Central.
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..361
FT /note="GDP-mannose 4,6 dehydratase 1"
FT /id="PRO_0000201710"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 23..28
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 79..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 101..105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 361 AA; 40850 MW; 3ADC7AE7394FAD81 CRC64;
MASRSLNGDS DIVKPRKIAL VTGITGQDGS YLTEFLLEKG YEVHGLIRRS SNFNTQRLNH
IYVDPHNVNK ALMKLHYGDL SDASSLRRWL DVIKPDEVYN LAAQSHVAVS FEIPDYTADV
VATGALRLLE AVRSHNIDNG RAIKYYQAGS SEMFGSTPPP QSETTPFHPR SPYAASKCAA
HWYTVNYREA YGLYACNGIL FNHESPRRGE NFVTRKITRA LGRIKVGLQT KLFLGNIQAS
RDWGFAGDYV EAMWLMLQQE KPDDYVVATE ESHTVKEFLD VSFGYVGLNW KDHVEIDKRY
FRPTEVDNLK GDASKAKEML GWKPKVGFEK LVKMMVDEDL ELAKREKVLA DAGYMDAQQQ
P
