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Protein

GDP-mannose 4,6-dehydratase

Gene

gmd

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.UniRule annotation1 Publication

Catalytic activityi

GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O.UniRule annotation1 Publication

Cofactori

NADP+UniRule annotation1 Publication

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei36NADPUniRule annotation1 Publication1
Active sitei126UniRule annotation1
Active sitei128NucleophileUniRule annotation1
Active sitei150NucleophileUniRule annotation1
Binding sitei154NADPUniRule annotation1 Publication1
Binding sitei180NADPUniRule annotation1 Publication1
Binding sitei185NADPUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 14NADPUniRule annotation1 Publication4
Nucleotide bindingi59 – 60NADPUniRule annotation1 Publication2
Nucleotide bindingi81 – 85NADPUniRule annotation1 Publication5

GO - Molecular functioni

GO - Biological processi

  • GDP-D-rhamnose biosynthetic process Source: PseudoCAP
  • GDP-mannose metabolic process Source: InterPro
  • lipopolysaccharide biosynthetic process Source: PseudoCAP
  • O antigen biosynthetic process Source: PseudoCAP

Keywordsi

Molecular functionLyase
Biological processLipopolysaccharide biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12848
PAER208964:G1FZ6-5581-MONOMER
BRENDAi4.2.1.47 5087
UniPathwayiUPA00030

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose 4,6-dehydrataseUniRule annotation (EC:4.2.1.47UniRule annotation)
Alternative name(s):
GDP-D-mannose dehydrataseUniRule annotation
Gene namesi
Name:gmdUniRule annotation
Synonyms:gca
Ordered Locus Names:PA5453
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5453

Pathology & Biotechi

Chemistry databases

DrugBankiDB04315 Guanosine-5'-Diphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017151 – 323GDP-mannose 4,6-dehydrataseAdd BLAST323

Proteomic databases

PaxDbiQ51366

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5453

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Turni9 – 11Combined sources3
Helixi13 – 24Combined sources12
Beta strandi28 – 33Combined sources6
Helixi42 – 46Combined sources5
Helixi50 – 52Combined sources3
Beta strandi53 – 57Combined sources5
Helixi63 – 73Combined sources11
Beta strandi76 – 80Combined sources5
Helixi87 – 90Combined sources4
Helixi94 – 101Combined sources8
Helixi103 – 115Combined sources13
Beta strandi119 – 126Combined sources8
Helixi127 – 130Combined sources4
Beta strandi134 – 138Combined sources5
Helixi149 – 168Combined sources20
Beta strandi172 – 177Combined sources6
Helixi190 – 202Combined sources13
Beta strandi209 – 212Combined sources4
Beta strandi217 – 219Combined sources3
Helixi223 – 235Combined sources13
Beta strandi236 – 238Combined sources3
Beta strandi242 – 244Combined sources3
Beta strandi249 – 251Combined sources3
Helixi252 – 261Combined sources10
Turni262 – 264Combined sources3
Helixi267 – 269Combined sources3
Beta strandi271 – 273Combined sources3
Helixi275 – 277Combined sources3
Helixi291 – 297Combined sources7
Helixi305 – 322Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RPNX-ray2.15A/B/C/D1-323[»]
ProteinModelPortaliQ51366
SMRiQ51366
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51366

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C0K Bacteria
COG1089 LUCA
HOGENOMiHOG000168003
InParanoidiQ51366
KOiK01711
OMAiTDCLYLG
PhylomeDBiQ51366

Family and domain databases

HAMAPiMF_00955 GDP_Man_dehydratase, 1 hit
InterProiView protein in InterPro
IPR006368 GDP_Man_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR43715 PTHR43715, 1 hit
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01472 gmd, 1 hit

Sequencei

Sequence statusi: Complete.

Q51366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRSALVTGI TGQDGAYLAK LLLEKGYRVH GLVARRSSDT RWRLRELGIE
60 70 80 90 100
GDIQYEDGDM ADACSVQRAV IKAQPQEVYN LAAQSFVGAS WNQPVTTGVV
110 120 130 140 150
DGLGVTHLLE AIRQFSPETR FYQASTSEMF GLIQAERQDE NTPFYPRSPY
160 170 180 190 200
GVAKLYGHWI TVNYRESFGL HASSGILFNH ESPLRGIEFV TRKVTDAVAR
210 220 230 240 250
IKLGKQQELR LGNVDAKRDW GFAGDYVEAM WLMLQQDKAD DYVVATGVTT
260 270 280 290 300
TVRDMCQIAF EHVGLDYRDF LKIDPAFFRP AEVDVLLGNP AKAQRVLGWK
310 320
PRTSLDELIR MMVEADLRRV SRE
Length:323
Mass (Da):36,399
Last modified:December 8, 2000 - v2
Checksum:i6C2BCC27D00D97E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153A → V in AAC44117 (PubMed:8548534).Curated1
Sequence conflicti167S → N in AAC44117 (PubMed:8548534).Curated1
Sequence conflicti216A → V in AAC44117 (PubMed:8548534).Curated1
Sequence conflicti223A → G in AAC44117 (PubMed:8548534).Curated1
Sequence conflicti247G → V in AAC44117 (PubMed:8548534).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18320 Genomic DNA Translation: AAC44117.1
AE004091 Genomic DNA Translation: AAG08838.1
PIRiG82964
RefSeqiNP_254140.1, NC_002516.2
WP_003096890.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG08838; AAG08838; PA5453
GeneIDi883089
KEGGipae:PA5453
PATRICifig|208964.12.peg.5716

Similar proteinsi

Entry informationi

Entry nameiGM4D_PSEAE
AccessioniPrimary (citable) accession number: Q51366
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: May 23, 2018
This is version 127 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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