P11759 (ALGD_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GDP-mannose 6-dehydrogenase
Short name=GMD
EC=1.1.1.132

Gene names

Name:	algD
Ordered Locus Names:	PA3540

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Alginate biosynthesis
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alginic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	GDP-mannose 6-dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 436

436

GDP-mannose 6-dehydrogenase

PRO_0000074067

Regions

Nucleotide binding

7 – 12

6

NAD

Region

157 – 161

5

Substrate binding

Region

210 – 217

8

Substrate binding

Region

256 – 265

10

Substrate binding

Sites

Active site

268

1

Nucleophile

Binding site

30

1

NAD

Binding site

35

1

NAD

Binding site

86

1

NAD

Binding site

105

1

NAD

Binding site

124

1

NAD; via amide nitrogen

Binding site

225

1

Substrate

Binding site

271

1

NAD

Binding site

324

1

Substrate

Binding site

331

1

NAD

Experimental info

Sequence conflict

349

1

L → F in CAA68425. Ref.1

Secondary structure

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436

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

12 – 21

10

Beta strand

25 – 29

5

Helix

33 – 40

8

Helix

51 – 60

10

Beta strand

64 – 68

5

Helix

70 – 75

6

Beta strand

78 – 82

5

Beta strand

92 – 94

3

Helix

97 – 110

14

Beta strand

118 – 121

4

Helix

129 – 132

4

Helix

134 – 142

9

Turn

147 – 149

3

Beta strand

150 – 154

5

Helix

164 – 169

6

Beta strand

174 – 180

7

Helix

181 – 191

11

Beta strand

194 – 196

3

Beta strand

198 – 202

5

Helix

203 – 233

31

Helix

238 – 245

8

Turn

249 – 253

5

Beta strand

266 – 268

3

Helix

269 – 282

14

Helix

290 – 292

3

Helix

293 – 308

16

Beta strand

315 – 319

5

Beta strand

322 – 324

3

Helix

334 – 344

11

Beta strand

348 – 352

5

Helix

354 – 359

6

Beta strand

362 – 364

3

Helix

366 – 371

6

Helix

374 – 377

4

Helix

384 – 390

7

Beta strand

392 – 396

5

Helix

401 – 403

3

Helix

404 – 408

5

Beta strand

415 – 421

7

Beta strand

424 – 426

3

Beta strand

429 – 434

6

Sequences

	Sequence		Length	Mass (Da)
	P11759 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: B6F3DC2B70B04463	FASTA	436	47,600
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

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.

PIR

H83203.
DEPSGD. S07391.

RefSeq

NP_252230.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P11759.

SMR

P11759. Positions 1-436.

ModBase

Search...

Protein-protein interaction databases

STRING

208964.PA3540.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

879004.

KEGG

pae:PA3540.

PATRIC

19841693. VBIPseAer58763_3704.

Organism-specific databases

PseudoCAP

PA3540.

Phylogenomic databases

eggNOG

COG1004.

HOGENOM

HOG000153773.

KO

K00066.

OMA

VCREIGY.

ProtClustDB

CLSK868056.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14396.

UniPathway

UPA00286.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]

Pfam

PF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000124. UDPglc_GDPman_dh. 1 hit.

SMART

SM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.
SSF52413. UDP-Glc/GDP-Man_DH_C. 1 hit.

TIGRFAMs

TIGR03026. NDP-sugDHase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P11759.

Entry information

Entry name

ALGD_PSEAE

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program