Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361NADPUniRule annotation1 Publication
Active sitei126 – 1261UniRule annotation
Active sitei128 – 1281NucleophileUniRule annotation
Active sitei150 – 1501NucleophileUniRule annotation
Binding sitei154 – 1541NADPUniRule annotation1 Publication
Binding sitei180 – 1801NADPUniRule annotation1 Publication
Binding sitei185 – 1851NADPUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADPUniRule annotation1 Publication
Nucleotide bindingi59 – 602NADPUniRule annotation1 Publication
Nucleotide bindingi81 – 855NADPUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

  • GDP-mannose metabolic process Source: InterPro
  • lipopolysaccharide biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12848.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323GDP-mannose 4,6-dehydratasePRO_0000201715Add
BLAST

Proteomic databases

PaxDbiQ51366.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5453.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Turni9 – 113Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 336Combined sources
Helixi42 – 465Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 575Combined sources
Helixi63 – 7311Combined sources
Beta strandi76 – 805Combined sources
Helixi87 – 904Combined sources
Helixi94 – 1018Combined sources
Helixi103 – 11513Combined sources
Beta strandi119 – 1268Combined sources
Helixi127 – 1304Combined sources
Beta strandi134 – 1385Combined sources
Helixi149 – 16820Combined sources
Beta strandi172 – 1776Combined sources
Helixi190 – 20213Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi217 – 2193Combined sources
Helixi223 – 23513Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi249 – 2513Combined sources
Helixi252 – 26110Combined sources
Turni262 – 2643Combined sources
Helixi267 – 2693Combined sources
Beta strandi271 – 2733Combined sources
Helixi275 – 2773Combined sources
Helixi291 – 2977Combined sources
Helixi305 – 32218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPNX-ray2.15A/B/C/D1-323[»]
ProteinModelPortaliQ51366.
SMRiQ51366. Positions 2-323.
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.
OMAiDYQHRTG.
PhylomeDBiQ51366.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00955. GDP_Man_dehydratase. 1 hit.
InterProiIPR006368. GDP_Man_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531A → V in AAC44117 (PubMed:8548534).Curated
Sequence conflicti167 – 1671S → N in AAC44117 (PubMed:8548534).Curated
Sequence conflicti216 – 2161A → V in AAC44117 (PubMed:8548534).Curated
Sequence conflicti223 – 2231A → G in AAC44117 (PubMed:8548534).Curated
Sequence conflicti247 – 2471G → V in AAC44117 (PubMed:8548534).Curated

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. NZ_ASJY01000837.1.

Genome annotation databases

EnsemblBacteriaiAAG08838; AAG08838; PA5453.
GeneIDi883089.
KEGGipae:PA5453.
PATRICi19845789. VBIPseAer58763_5716.

Cross-referencesi

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. NZ_ASJY01000837.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPNX-ray2.15A/B/C/D1-323[»]
ProteinModelPortaliQ51366.
SMRiQ51366. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5453.

Proteomic databases

PaxDbiQ51366.

Protocols and materials databases

DNASUi883089.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08838; AAG08838; PA5453.
GeneIDi883089.
KEGGipae:PA5453.
PATRICi19845789. VBIPseAer58763_5716.

Organism-specific databases

PseudoCAPiPA5453.

Phylogenomic databases

eggNOGiENOG4105C0K. Bacteria.
COG1089. LUCA.
HOGENOMiHOG000168003.
InParanoidiQ51366.
KOiK01711.
OMAiDYQHRTG.
PhylomeDBiQ51366.

Enzyme and pathway databases

UniPathwayiUPA00030.
BioCyciMetaCyc:MONOMER-12848.
BRENDAi4.2.1.47. 5087.

Miscellaneous databases

EvolutionaryTraceiQ51366.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00955. GDP_Man_dehydratase. 1 hit.
InterProiIPR006368. GDP_Man_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01472. gmd. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGM4D_PSEAE
AccessioniPrimary (citable) accession number: Q51366
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: September 7, 2016
This is version 115 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.