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Protein

GDP-mannose 6-dehydrogenase

Gene

algD

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 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: alginate biosynthesis

This protein is involved in the pathway alginate biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway alginate biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei30NAD1 Publication1
Binding sitei35NAD1 Publication1
Binding sitei86NAD1 Publication1
Binding sitei105NAD1 Publication1
Binding sitei124NAD; via amide nitrogen1 Publication1
Binding sitei225Substrate1 Publication1
Active sitei268Nucleophile1 Publication1
Binding sitei271NAD1 Publication1
Binding sitei324Substrate1 Publication1
Binding sitei331NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 12NAD1 Publication6

GO - Molecular functioni

  • GDP-mannose 6-dehydrogenase activity Source: PseudoCAP
  • NAD binding Source: PseudoCAP

GO - Biological processi

  • alginic acid biosynthetic process Source: PseudoCAP
  • cellular response to cell envelope stress Source: PseudoCAP
  • response to osmotic stress Source: PseudoCAP
  • single-species biofilm formation Source: PseudoCAP

Keywordsi

Molecular functionOxidoreductase
Biological processAlginate biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14396
PAER208964:G1FZ6-3608-MONOMER
BRENDAi1.1.1.132 5087
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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3540

Pathology & Biotechi

Chemistry databases

DrugBankiDB02772 Sucrose

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000740671 – 436GDP-mannose 6-dehydrogenaseAdd BLAST436

Proteomic databases

PaxDbiP11759
PRIDEiP11759

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.Curated2 Publications

Protein-protein interaction databases

STRINGi208964.PA3540

Structurei

Secondary structure

1436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi12 – 21Combined sources10
Beta strandi25 – 29Combined sources5
Helixi33 – 40Combined sources8
Helixi51 – 60Combined sources10
Beta strandi64 – 68Combined sources5
Helixi70 – 75Combined sources6
Beta strandi78 – 82Combined sources5
Beta strandi92 – 94Combined sources3
Helixi97 – 110Combined sources14
Beta strandi118 – 121Combined sources4
Helixi129 – 132Combined sources4
Helixi134 – 142Combined sources9
Turni147 – 149Combined sources3
Beta strandi150 – 154Combined sources5
Helixi164 – 169Combined sources6
Beta strandi174 – 180Combined sources7
Helixi181 – 191Combined sources11
Beta strandi194 – 196Combined sources3
Beta strandi198 – 202Combined sources5
Helixi203 – 233Combined sources31
Helixi238 – 245Combined sources8
Turni249 – 253Combined sources5
Beta strandi266 – 268Combined sources3
Helixi269 – 282Combined sources14
Helixi290 – 292Combined sources3
Helixi293 – 308Combined sources16
Beta strandi315 – 319Combined sources5
Beta strandi322 – 324Combined sources3
Helixi334 – 344Combined sources11
Beta strandi348 – 352Combined sources5
Helixi354 – 359Combined sources6
Beta strandi362 – 364Combined sources3
Helixi366 – 371Combined sources6
Helixi374 – 377Combined sources4
Helixi384 – 390Combined sources7
Beta strandi392 – 396Combined sources5
Helixi401 – 403Combined sources3
Helixi404 – 408Combined sources5
Beta strandi415 – 421Combined sources7
Beta strandi424 – 426Combined sources3
Beta strandi429 – 434Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11759

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 161Substrate binding1 Publication5
Regioni210 – 217Substrate binding1 Publication8
Regioni256 – 265Substrate binding1 Publication10

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6Y Bacteria
COG1004 LUCA
HOGENOMiHOG000153773
InParanoidiP11759
KOiK00066
OMAiIICVQTP
PhylomeDBiP11759

Family and domain databases

InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR028358 GDPman_DH
IPR036291 NAD(P)-bd_dom_sf
IPR017476 UDP-Glc/GDP-Man
IPR014027 UDP-Glc/GDP-Man_DH_C
IPR036220 UDP-Glc/GDP-Man_DH_C_sf
IPR014026 UDP-Glc/GDP-Man_DH_dimer
IPR001732 UDP-Glc/GDP-Man_DH_N
PfamiView protein in Pfam
PF00984 UDPG_MGDP_dh, 1 hit
PF03720 UDPG_MGDP_dh_C, 1 hit
PF03721 UDPG_MGDP_dh_N, 1 hit
PIRSFiPIRSF500135 GDPman_DH, 1 hit
PIRSF000124 UDPglc_GDPman_dh, 1 hit
SMARTiView protein in SMART
SM00984 UDPG_MGDP_dh_C, 1 hit
SUPFAMiSSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 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)DescriptionActionsGraphical viewLength
Sequence conflicti349L → F in CAA68425 (PubMed:3108855).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_003110461.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG06928; AAG06928; PA3540
GeneIDi879004
KEGGipae:PA3540
PATRICifig|208964.12.peg.3704

Similar proteinsi

Entry informationi

Entry nameiALGD_PSEAE
AccessioniPrimary (citable) accession number: P11759
Secondary accession number(s): Q9HY71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 11, 2001
Last modified: May 23, 2018
This is version 162 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, Direct protein sequencing, Reference proteome

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