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UniProtKB/Swiss-Prot entry P0C0F4

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

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Entry information
Entry name UDG_STRPY
Primary accession number P0C0F4
Secondary accession number Q07172
Integrated into Swiss-Prot on September 13, 2005
Sequence was last modified on September 13, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 23)
Name and origin of the protein
Protein name UDP-glucose 6-dehydrogenase
Synonyms UDP-Glc dehydrogenase
UDP-GlcDH
UDPGDH
EC 1.1.1.22
Gene name
Name: hasB
From
Streptococcus pyogenes [TaxID: 1314] 
Taxonomy Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=WF50;
PubMed=8463246 [NCBI, ExPASy, EBI, Israel, Japan]
Dougherty B.A., van de Rijn I.;
"Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity.";
J. Biol. Chem. 268:7118-7124(1993).
[2]
 MUTAGENESIS OF THR-118; GLU-141; GLU-145 AND CYS-260.
DOI=10.1046/j.1432-1033.2003.03876.x; PubMed=14686915 [NCBI, ExPASy, EBI, Israel, Japan]
Ge X., Penney L.C., van de Rijn I., Tanner M.E.;
"Active site residues and mechanism of UDP-glucose dehydrogenase.";
Eur. J. Biochem. 271:14-22(2004).
[3]
 X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, AND MUTAGENESIS OF CYS-260.
DOI=10.1021/bi000181h; PubMed=10841783 [NCBI, ExPASy, EBI, Israel, Japan]
Campbell R.E., Mosimann S.C., van De Rijn I., Tanner M.E., Strynadka N.C.;
"The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.";
Biochemistry 39:7012-7023(2000).
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
L08444; AAA26899.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1DLI; X-ray; 2.31 A; A=1-402.[ExPASy / RCSB / EBI]
1DLJ; X-ray; 1.80 A; A=1-402.[ExPASy / RCSB / EBI]
1LTY; Model; -; A=1-402.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DLI; -.
1DLJ; -.
1LTY; -.
ModBase P0C0F4.
Ontologies
GO
GO:0003979; Molecular function: UDP-glucose 6-dehydrogenase activity (inferred from electronic annotation from EC).
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.
BLOCKS P0C0F4.
Other
ProtoNet P0C0F4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Capsule biogenesis/degradation; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   402  402     UDP-glucose 6-dehydrogenase. PRO_0000074054
NP_BIND   2    19  18     NAD. 
REGION   142   145  4     Substrate binding. 
REGION   249   253  5     Substrate binding. 
ACT_SITE   260   260        Nucleophile. 
BINDING   29    29        NAD. 
BINDING   34    34        NAD. 
BINDING   83    83        NAD. 
BINDING   118   118        NAD; via amide nitrogen. 
BINDING   145   145        NAD. 
BINDING   204   204        Substrate. 
BINDING   257   257        Substrate; via amide nitrogen. 
BINDING   263   263        NAD. 
BINDING   319   319        Substrate; via carbonyl oxygen. 
BINDING   320   320        Substrate. 
BINDING   327   327        NAD. 
BINDING   402   402        Substrate. 
MUTAGEN   118   118        T->A: Increases Km for substrate 3-fold. Increases Km for NAD 6-fold. Reduces catalytic activity 160-fold. 
MUTAGEN   141   141        E->Q: Increases Km for substrate 3-fold. Increases Km for NAD 2-fold. Reduces catalytic activity about 10-fold. 
MUTAGEN   145   145        E->Q: Increases Km for substrate 6-fold. Increases Km for NAD 3-fold. Reduces catalytic activity about 10-fold. 
MUTAGEN   260   260        C->A,S: Loss of activity. 
STRAND   2     6  5      
HELIX   10    19  10      
TURN   20    22  3      
STRAND   23    28  6      
HELIX   32    39  8      
HELIX   48    56  9      
STRAND   61    65  5      
HELIX   67    73  7      
STRAND   75    79  5      
TURN   87    90  4      
HELIX   95   107  13      
STRAND   112   115  4      
HELIX   123   131  9      
STRAND   136   138  3      
HELIX   150   153  4      
STRAND   158   161  4      
HELIX   168   184  17      
STRAND   186   188  3      
STRAND   192   195  4      
HELIX   197   227  31      
HELIX   232   240  9      
TURN   243   245  3      
STRAND   247   249  3      
HELIX   260   271  12      
TURN   272   274  3      
HELIX   279   303  25      
STRAND   311   315  5      
HELIX   330   339  10      
STRAND   344   348  5      
STRAND   361   363  3      
HELIX   367   373  7      
STRAND   375   378  4      
HELIX   384   392  9      
Sequence information
Length: 402 AA [This is the length of the unprocessed precursor] Molecular weight: 45483 Da [This is the MW of the unprocessed precursor] CRC64: DD1869D659F4CA58 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI EYYLKSKQLS 

        70         80         90        100        110        120 
IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV IKEVLSVNSH ATLIIKSTIP 

       130        140        150        160        170        180 
IGFITEMRQK FQTDRIIFSP EFLRESKALY DNLYPSRIIV SCEENDSPKV KADAEKFALL 

       190        200        210        220        230        240 
LKSAAKKNNV PVLIMGASEA EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMIIQGIS 

       250        260        270        280        290        300 
YDDRIGMHYN NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN 

       310        320        330        340        350        360 
VLKEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP MLNKLESEDQ 

       370        380        390        400 
SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG RD
P0C0F4 in FASTA format

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