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P11759

- ALGD_PSEAE

UniProt

P11759 - ALGD_PSEAE

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Protein

GDP-mannose 6-dehydrogenase

Gene

algD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301NAD1 Publication
Binding sitei35 – 351NAD1 Publication
Binding sitei86 – 861NAD1 Publication
Binding sitei105 – 1051NAD1 Publication
Binding sitei124 – 1241NAD; via amide nitrogen1 Publication
Binding sitei225 – 2251Substrate
Active sitei268 – 2681Nucleophile
Binding sitei271 – 2711NAD1 Publication
Binding sitei324 – 3241Substrate
Binding sitei331 – 3311NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NAD1 Publication

GO - Molecular functioni

  1. GDP-mannose 6-dehydrogenase activity Source: PseudoCAP
  2. NAD binding Source: PseudoCAP

GO - Biological processi

  1. alginic acid biosynthetic process Source: PseudoCAP
  2. biofilm formation Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Alginate biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14396.
UniPathwayiUPA00286.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose 6-dehydrogenase (EC:1.1.1.132)
Short name:
GMD
Gene namesi
Name:algD
Ordered Locus Names:PA3540
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA3540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436GDP-mannose 6-dehydrogenasePRO_0000074067Add
BLAST

Interactioni

Subunit structurei

Homotetramer (Potential). According to PubMed:12135385, this enzyme exists as a homotetramer, but results obtained in PubMed:2470755 and PubMed:8294014 indicate that it is a homohexamer.2 PublicationsCurated

Protein-protein interaction databases

STRINGi208964.PA3540.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi12 – 2110
Beta strandi25 – 295
Helixi33 – 408
Helixi51 – 6010
Beta strandi64 – 685
Helixi70 – 756
Beta strandi78 – 825
Beta strandi92 – 943
Helixi97 – 11014
Beta strandi118 – 1214
Helixi129 – 1324
Helixi134 – 1429
Turni147 – 1493
Beta strandi150 – 1545
Helixi164 – 1696
Beta strandi174 – 1807
Helixi181 – 19111
Beta strandi194 – 1963
Beta strandi198 – 2025
Helixi203 – 23331
Helixi238 – 2458
Turni249 – 2535
Beta strandi266 – 2683
Helixi269 – 28214
Helixi290 – 2923
Helixi293 – 30816
Beta strandi315 – 3195
Beta strandi322 – 3243
Helixi334 – 34411
Beta strandi348 – 3525
Helixi354 – 3596
Beta strandi362 – 3643
Helixi366 – 3716
Helixi374 – 3774
Helixi384 – 3907
Beta strandi392 – 3965
Helixi401 – 4033
Helixi404 – 4085
Beta strandi415 – 4217
Beta strandi424 – 4263
Beta strandi429 – 4346

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFZX-ray2.80A/B/C/D1-436[»]
1MUUX-ray2.02A/B/C/D1-436[»]
1MV8X-ray1.55A/B/C/D1-436[»]
ProteinModelPortaliP11759.
SMRiP11759. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11759.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1615Substrate binding
Regioni210 – 2178Substrate binding
Regioni256 – 26510Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1004.
HOGENOMiHOG000153773.
InParanoidiP11759.
KOiK00066.
OMAiGDLELDY.
OrthoDBiEOG6ZSP7N.
PhylomeDBiP11759.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR008927. 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]
PANTHERiPTHR11374. PTHR11374. 1 hit.
PfamiPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF500135. GDPman_DH. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

Sequencei

Sequence statusi: Complete.

P11759-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRISIFGLGY VGAVCAGCLS ARGHEVIGVD VSSTKIDLIN QGKSPIVEPG
60 70 80 90 100
LEALLQQGRQ TGRLSGTTDF KKAVLDSDVS FICVGTPSKK NGDLDLGYIE
110 120 130 140 150
TVCREIGFAI REKSERHTVV VRSTVLPGTV NNVVIPLIED CSGKKAGVDF
160 170 180 190 200
GVGTNPEFLR ESTAIKDYDF PPMTVIGELD KQTGDLLEEI YRELDAPIIR
210 220 230 240 250
KTVEVAEMIK YTCNVWHAAK VTFANEIGNI AKAVGVDGRE VMDVICQDHK
260 270 280 290 300
LNLSRYYMRP GFAFGGSCLP KDVRALTYRA SQLDVEHPML GSLMRSNSNQ
310 320 330 340 350
VQKAFDLITS HDTRKVGLLG LSFKAGTDDL RESPLVELAE MLIGKGYELR
360 370 380 390 400
IFDRNVEYAR VHGANKEYIE SKIPHVSSLL VSDLDEVVAS SDVLVLGNGD
410 420 430
ELFVDLVNKT PSGKKLVDLV GFMPHTTTAQ AEGICW
Length:436
Mass (Da):47,600
Last modified:January 11, 2001 - v2
Checksum:iB6F3DC2B70B04463
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti349 – 3491L → F in CAA68425. (PubMed:3108855)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00337 Genomic DNA. Translation: CAA68425.1.
AE004091 Genomic DNA. Translation: AAG06928.1.
L22611 Genomic DNA. Translation: AAC36874.1.
PIRiH83203.
S07391. DEPSGD.
RefSeqiNP_252230.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06928; AAG06928; PA3540.
GeneIDi879004.
KEGGipae:PA3540.
PATRICi19841693. VBIPseAer58763_3704.

Cross-referencesi

Web resourcesi

Protein Spotlight

Slime with a design - Issue 37 of August 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00337 Genomic DNA. Translation: CAA68425.1 .
AE004091 Genomic DNA. Translation: AAG06928.1 .
L22611 Genomic DNA. Translation: AAC36874.1 .
PIRi H83203.
S07391. DEPSGD.
RefSeqi NP_252230.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MFZ X-ray 2.80 A/B/C/D 1-436 [» ]
1MUU X-ray 2.02 A/B/C/D 1-436 [» ]
1MV8 X-ray 1.55 A/B/C/D 1-436 [» ]
ProteinModelPortali P11759.
SMRi P11759. Positions 1-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA3540.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG06928 ; AAG06928 ; PA3540 .
GeneIDi 879004.
KEGGi pae:PA3540.
PATRICi 19841693. VBIPseAer58763_3704.

Organism-specific databases

PseudoCAPi PA3540.

Phylogenomic databases

eggNOGi COG1004.
HOGENOMi HOG000153773.
InParanoidi P11759.
KOi K00066.
OMAi GDLELDY.
OrthoDBi EOG6ZSP7N.
PhylomeDBi P11759.

Enzyme and pathway databases

UniPathwayi UPA00286 .
BioCyci MetaCyc:MONOMER-14396.

Miscellaneous databases

EvolutionaryTracei P11759.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR008927. 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 ]
PANTHERi PTHR11374. PTHR11374. 1 hit.
Pfami PF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF500135. GDPman_DH. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTi SM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsi TIGR03026. NDP-sugDHase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiALGD_PSEAE
AccessioniPrimary (citable) accession number: P11759
Secondary accession number(s): Q9HY71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 11, 2001
Last modified: October 29, 2014
This is version 138 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, Direct protein sequencing, 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3