Reviewed, UniProtKB/Swiss-Prot P0C0F4 (UDG_STRPY)

Names and origin

Protein names

Recommended name:
    UDP-glucose 6-dehydrogenase
      Short name=UDP-Glc dehydrogenase
      Short name=UDP-GlcDH
      Short name=UDPGDH
    EC=1.1.1.22

Gene names

Name:

hasB

Organism

Streptococcus pyogenes

Taxonomic identifier

1314 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis.
Catalytic activity	UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.
Pathway	Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1.
Sequence similarities	Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=20 µM for UDP-glucose KM=65 µM for NAD

Ontologies

Keywords
Biological process	Capsule biogenesis/degradation
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 402

402

UDP-glucose 6-dehydrogenase

PRO_0000074054

Regions

Nucleotide binding

2 – 19

18

NAD

Region

142 – 145

4

Substrate binding

Region

249 – 253

5

Substrate binding

Sites

Active site

260

1

Nucleophile

Binding site

29

1

NAD

Binding site

34

1

NAD

Binding site

83

1

NAD

Binding site

118

1

NAD; via amide nitrogen

Binding site

145

1

NAD

Binding site

204

1

Substrate

Binding site

257

1

Substrate; via amide nitrogen

Binding site

263

1

NAD

Binding site

319

1

Substrate; via carbonyl oxygen

Binding site

320

1

Substrate

Binding site

327

1

NAD

Binding site

402

1

Substrate

Experimental info

Mutagenesis

118

1

T → A: Increases Km for substrate 3-fold. Increases Km for NAD 6-fold. Reduces catalytic activity 160-fold

Mutagenesis

141

1

E → Q: Increases Km for substrate 3-fold. Increases Km for NAD 2-fold. Reduces catalytic activity about 10-fold

Mutagenesis

145

1

E → Q: Increases Km for substrate 6-fold. Increases Km for NAD 3-fold. Reduces catalytic activity about 10-fold

Mutagenesis

260

1

C → A or S: Loss of activity

Secondary structure

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402

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 19

10

Turn

20 – 22

3

Beta strand

23 – 28

6

Helix

32 – 39

8

Helix

48 – 56

9

Beta strand

61 – 65

5

Helix

67 – 73

7

Beta strand

75 – 79

5

Turn

87 – 90

4

Helix

95 – 107

13

Beta strand

112 – 115

4

Helix

123 – 131

9

Beta strand

136 – 138

3

Helix

150 – 153

4

Beta strand

158 – 161

4

Helix

168 – 184

17

Beta strand

186 – 188

3

Beta strand

192 – 195

4

Helix

197 – 227

31

Helix

232 – 240

9

Turn

243 – 245

3

Beta strand

247 – 249

3

Helix

260 – 271

12

Turn

272 – 274

3

Helix

279 – 303

25

Beta strand

311 – 315

5

Helix

330 – 339

10

Beta strand

344 – 348

5

Beta strand

361 – 363

3

Helix

367 – 373

7

Beta strand

375 – 378

4

Helix

384 – 392

9

Sequences

	Sequence		Length	Mass (Da)
	P0C0F4-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: DD1869D659F4CA58	FASTA	402	45,483
	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

References

[1]	"Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity." Dougherty B.A., van de Rijn I. J. Biol. Chem. 268:7118-7124(1993) [PubMed: 8463246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WF50.
[2]	"Active site residues and mechanism of UDP-glucose dehydrogenase." Ge X., Penney L.C., van de Rijn I., Tanner M.E. Eur. J. Biochem. 271:14-22(2004) [PubMed: 14686915] [Abstract] Cited for: MUTAGENESIS OF THR-118; GLU-141; GLU-145 AND CYS-260.
[3]	"The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation." Campbell R.E., Mosimann S.C., van De Rijn I., Tanner M.E., Strynadka N.C. Biochemistry 39:7012-7023(2000) [PubMed: 10841783] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, MUTAGENESIS OF CYS-260.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L08444 Genomic DNA. Translation: AAA26899.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DLI	X-ray	2.31	A	1-402	[»]
1DLJ	X-ray	1.80	A	1-402	[»]
1LTY	model	-	A	1-402	[»]

ModBase

Search...

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]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.

PANTHER

PTHR11374. UDPG_MGDP_DH_Creg. 1 hit.

Pfam

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

ProtoNet

Search...

Entry information

Entry name

UDG_STRPY

Accession

Primary (citable) accession number: P0C0F4
Secondary accession number(s): Q07172

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	November 25, 2008
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)