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UniProtKB/Swiss-Prot entry P11759


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALGD_PSEAE
Primary accession number P11759
Secondary accession number Q9HY71
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name GDP-mannose 6-dehydrogenase
Synonyms GMD
EC 1.1.1.132
Gene name
Name: algD
OrderedLocusNames: PA3540
From
Pseudomonas aeruginosa [TaxID: 287] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=8830;
DOI=10.1093/nar/15.11.4567; PubMed=3108855 [NCBI, ExPASy, EBI, Israel, Japan]
Deretic V., Gill J.F., Chakrabarty A.M.;
"Pseudomonas aeruginosa infection in cystic fibrosis: nucleotide sequence and transcriptional regulation of the algD gene.";
Nucleic Acids Res. 15:4567-4581(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).
[3]
PROTEIN SEQUENCE OF 1-11, SUBUNIT, AND INHIBITION.
PubMed=2470755 [NCBI, ExPASy, EBI, Israel, Japan]
Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M.;
"Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa.";
J. Biol. Chem. 264:9380-9385(1989).
[4]
PROTEIN SEQUENCE OF 1-11; 280-289 AND 297-306.
PubMed=1370473 [NCBI, ExPASy, EBI, Israel, Japan]
Roychoudhury S., Chakrabarty K., Ho Y.-K., Chakrabarty A.M.;
"Characterization of guanosine diphospho-D-mannose dehydrogenase from Pseudomonas aeruginosa. Structural analysis by limited proteolysis.";
J. Biol. Chem. 267:990-996(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 425-435.
STRAIN=8830;
DOI=10.1016/0378-1119(93)90477-K; PubMed=8294014 [NCBI, ExPASy, EBI, Israel, Japan]
Maharaj R., May T.B., Wang S.-K., Chakrabarty A.M.;
"Sequence of the alg8 and alg44 genes involved in the synthesis of alginate by Pseudomonas aeruginosa.";
Gene 136:267-269(1993).
[6]
CHARACTERIZATION.
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1021/bi025862m; PubMed=12135385 [NCBI, ExPASy, EBI, Israel, Japan]
Naught L.E., Gilbert S., Imhoff R., Snook C., Beamer L., Tipton P.;
"Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase.";
Biochemistry 41:9637-9645(2002).
[7]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NAD AND PRODUCT.
DOI=10.1021/bi027328k; PubMed=12705829 [NCBI, ExPASy, EBI, Israel, Japan]
Snook C.F., Tipton P.A., Beamer L.J.;
"Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa.";
Biochemistry 42:4658-4668(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00337; CAA68425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG06928.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L22611; AAC36874.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H83203; H83203.
S07391; DEPSGD.
RefSeq NP_252230.1; -.
3D structure databases
PDB
1MFZ; X-ray; 2.80 A; A/B/C/D=1-436.[ExPASy / RCSB / EBI]
1MUU; X-ray; 2.00 A; A/B/C/D=1-436.[ExPASy / RCSB / EBI]
1MV8; X-ray; 1.55 A; A/B/C/D=1-436.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MFZ; -.
1MUU; -.
1MV8; -.
ModBase P11759.
Enzyme and pathway databases
BioCyc PAER208964:PA3540-MON; -.
Organism-specific databases
PseudoCAP PA3540; -.
Ontologies
GO
GO:0047919; Molecular function: GDP-mannose 6-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0042121; Biological process: alginic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.
PANTHER PTHR11374; UDPG_MGDP_DH_Creg; 1.
Pfam PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GeneID 879004; -.
GenomeReviews AE004091_GR; PA3540.
KEGG pae:PA3540; -.
Phylogenomic databases
HOGENOM P11759; -.
Genome annotation databases
CMR P11759; PA3540.
Other
ProtoNet P11759.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alginate biosynthesis; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   436  436     GDP-mannose 6-dehydrogenase. PRO_0000074067
NP_BIND   7    12  6     NAD. 
REGION   157   161  5     Substrate binding. 
REGION   210   217  8     Substrate binding. 
REGION   256   265  10     Substrate binding. 
ACT_SITE   268   268        Nucleophile. 
BINDING   30    30        NAD. 
BINDING   35    35        NAD. 
BINDING   86    86        NAD. 
BINDING   105   105        NAD. 
BINDING   124   124        NAD; via amide nitrogen. 
BINDING   225   225        Substrate. 
BINDING   271   271        NAD. 
BINDING   324   324        Substrate. 
BINDING   331   331        NAD. 
CONFLICT   349   349        L -> F (in Ref. 1; CAA68425). 
STRAND   2     6  5      
HELIX   12    21  10      
STRAND   25    29  5      
HELIX   33    40  8      
HELIX   51    60  10      
STRAND   64    68  5      
HELIX   70    75  6      
STRAND   78    82  5      
STRAND   92    94  3      
HELIX   97   112  16      
STRAND   118   121  4      
HELIX   129   132  4      
HELIX   134   142  9      
TURN   147   149  3      
STRAND   150   154  5      
HELIX   164   169  6      
STRAND   174   180  7      
HELIX   181   191  11      
STRAND   194   196  3      
STRAND   198   201  4      
HELIX   203   234  32      
HELIX   238   245  8      
TURN   249   253  5      
STRAND   266   268  3      
HELIX   269   282  14      
HELIX   290   292  3      
HELIX   293   308  16      
STRAND   315   319  5      
STRAND   322   324  3      
HELIX   334   344  11      
STRAND   348   352  5      
HELIX   354   361  8      
HELIX   366   371  6      
HELIX   374   377  4      
HELIX   384   390  7      
STRAND   392   396  5      
HELIX   401   403  3      
HELIX   404   408  5      
STRAND   415   421  7      
STRAND   429   434  6      
Sequence information
Length: 436 AA [This is the length of the unprocessed precursor] Molecular weight: 47600 Da [This is the MW of the unprocessed precursor] CRC64: B6F3DC2B70B04463 [This is a checksum on the sequence]
        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 

P11759 in FASTA format

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View entry in raw text format (no links)
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