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P11759 (ALGD_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GDP-mannose 6-dehydrogenase

Short name=GMD
EC=1.1.1.132
Gene names
Name:algD
Ordered Locus Names:PA3540
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics.

Catalytic activity

GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH.

Enzyme regulation

The enzyme can be inhibited by GMP, ATP, GDP-D-glucose and maltose.

Pathway

Glycan biosynthesis; alginate biosynthesis.

Subunit structure

Homotetramer Potential. According to Ref.6, this enzyme exists as a homotetramer, but results obtained in Ref.3 and Ref.5 indicate that it is a homohexamer. Ref.3

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436GDP-mannose 6-dehydrogenase
PRO_0000074067

Regions

Nucleotide binding7 – 126NAD
Region157 – 1615Substrate binding
Region210 – 2178Substrate binding
Region256 – 26510Substrate binding

Sites

Active site2681Nucleophile
Binding site301NAD
Binding site351NAD
Binding site861NAD
Binding site1051NAD
Binding site1241NAD; via amide nitrogen
Binding site2251Substrate
Binding site2711NAD
Binding site3241Substrate
Binding site3311NAD

Experimental info

Sequence conflict3491L → F in CAA68425. Ref.1

Secondary structure

............................................................................... 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11759 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: B6F3DC2B70B04463

FASTA43647,600
        10         20         30         40         50         60 
MRISIFGLGY VGAVCAGCLS ARGHEVIGVD VSSTKIDLIN QGKSPIVEPG LEALLQQGRQ 

        70         80         90        100        110        120 
TGRLSGTTDF KKAVLDSDVS FICVGTPSKK NGDLDLGYIE TVCREIGFAI REKSERHTVV 

       130        140        150        160        170        180 
VRSTVLPGTV NNVVIPLIED CSGKKAGVDF GVGTNPEFLR ESTAIKDYDF PPMTVIGELD 

       190        200        210        220        230        240 
KQTGDLLEEI YRELDAPIIR KTVEVAEMIK YTCNVWHAAK VTFANEIGNI AKAVGVDGRE 

       250        260        270        280        290        300 
VMDVICQDHK LNLSRYYMRP GFAFGGSCLP KDVRALTYRA SQLDVEHPML GSLMRSNSNQ 

       310        320        330        340        350        360 
VQKAFDLITS HDTRKVGLLG LSFKAGTDDL RESPLVELAE MLIGKGYELR IFDRNVEYAR 

       370        380        390        400        410        420 
VHGANKEYIE SKIPHVSSLL VSDLDEVVAS SDVLVLGNGD ELFVDLVNKT PSGKKLVDLV 

       430 
GFMPHTTTAQ AEGICW 

« Hide

References

« Hide 'large scale' references
[1]"Pseudomonas aeruginosa infection in cystic fibrosis: nucleotide sequence and transcriptional regulation of the algD gene."
Deretic V., Gill J.F., Chakrabarty A.M.
Nucleic Acids Res. 15:4567-4581(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 8830.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa."
Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M.
J. Biol. Chem. 264:9380-9385(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11, SUBUNIT, INHIBITION.
[4]"Characterization of guanosine diphospho-D-mannose dehydrogenase from Pseudomonas aeruginosa. Structural analysis by limited proteolysis."
Roychoudhury S., Chakrabarty K., Ho Y.-K., Chakrabarty A.M.
J. Biol. Chem. 267:990-996(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11; 280-289 AND 297-306.
[5]"Sequence of the alg8 and alg44 genes involved in the synthesis of alginate by Pseudomonas aeruginosa."
Maharaj R., May T.B., Wang S.-K., Chakrabarty A.M.
Gene 136:267-269(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 425-435.
Strain: 8830.
[6]"Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase."
Naught L.E., Gilbert S., Imhoff R., Snook C., Beamer L., Tipton P.
Biochemistry 41:9637-9645(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[7]"Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa."
Snook C.F., Tipton P.A., Beamer L.J.
Biochemistry 42:4658-4668(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NAD AND PRODUCT.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Slime with a design - Issue 37 of August 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00337 Genomic DNA. Translation: CAA68425.1.
AE004091 Genomic DNA. Translation: AAG06928.1.
L22611 Genomic DNA. Translation: AAC36874.1.
PIRH83203.
DEPSGD. S07391.
RefSeqNP_252230.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFZX-ray2.80A/B/C/D1-436[»]
1MUUX-ray2.02A/B/C/D1-436[»]
1MV8X-ray1.55A/B/C/D1-436[»]
ProteinModelPortalP11759.
SMRP11759. Positions 1-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06928; AAG06928; PA3540.
GeneID879004.
KEGGpae:PA3540.
PATRIC19841693. VBIPseAer58763_3704.

Organism-specific databases

PseudoCAPPA3540.

Phylogenomic databases

eggNOGCOG1004.
HOGENOMHOG000153773.
KOK00066.
OMAGDLELDY.
OrthoDBEOG6ZSP7N.
PhylomeDBP11759.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14396.
UniPathwayUPA00286.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR028358. GDPman_DH.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]
PANTHERPTHR11374. PTHR11374. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500135. GDPman_DH. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11759.

Entry information

Entry nameALGD_PSEAE
AccessionPrimary (citable) accession number: P11759
Secondary accession number(s): Q9HY71
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways