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P0C0F4

- UDG_STRPY

UniProt

P0C0F4 - UDG_STRPY

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Protein

UDP-glucose 6-dehydrogenase

Gene

hasB

Organism
Streptococcus pyogenes
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis.

Catalytic activityi

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

Kineticsi

  1. KM=20 µM for UDP-glucose
  2. KM=65 µM for NAD

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291NAD1 Publication
Binding sitei34 – 341NAD1 Publication
Binding sitei83 – 831NAD1 Publication
Binding sitei118 – 1181NAD; via amide nitrogen1 Publication
Binding sitei145 – 1451NAD1 Publication
Binding sitei204 – 2041Substrate1 Publication
Binding sitei257 – 2571Substrate; via amide nitrogen1 Publication
Active sitei260 – 2601Nucleophile
Binding sitei263 – 2631NAD1 Publication
Binding sitei319 – 3191Substrate; via carbonyl oxygen1 Publication
Binding sitei320 – 3201Substrate1 Publication
Binding sitei327 – 3271NAD1 Publication
Binding sitei402 – 4021Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2 – 1918NAD1 PublicationAdd
BLAST

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. UDP-glucose 6-dehydrogenase activity Source: CACAO

GO - Biological processi

  1. polysaccharide biosynthetic process Source: InterPro
  2. UDP-glucuronate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Capsule biogenesis/degradation

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP0C0F4.
UniPathwayiUPA00038; UER00491.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose 6-dehydrogenase (EC:1.1.1.22)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
Gene namesi
Name:hasB
OrganismiStreptococcus pyogenes
Taxonomic identifieri1314 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi118 – 1181T → A: Increases Km for substrate 3-fold. Increases Km for NAD 6-fold. Reduces catalytic activity 160-fold. 1 Publication
Mutagenesisi141 – 1411E → Q: Increases Km for substrate 3-fold. Increases Km for NAD 2-fold. Reduces catalytic activity about 10-fold. 1 Publication
Mutagenesisi145 – 1451E → Q: Increases Km for substrate 6-fold. Increases Km for NAD 3-fold. Reduces catalytic activity about 10-fold. 1 Publication
Mutagenesisi260 – 2601C → A or S: Loss of activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402UDP-glucose 6-dehydrogenasePRO_0000074054Add
BLAST

Structurei

Secondary structure

1
402
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 1910
Turni20 – 223
Beta strandi23 – 286
Helixi32 – 398
Helixi48 – 569
Beta strandi61 – 655
Helixi67 – 737
Beta strandi75 – 795
Turni87 – 904
Helixi95 – 10713
Beta strandi112 – 1154
Helixi123 – 1308
Beta strandi136 – 1383
Helixi150 – 1534
Beta strandi158 – 1614
Helixi168 – 18417
Beta strandi186 – 1883
Beta strandi192 – 1954
Helixi197 – 22731
Helixi232 – 2409
Turni243 – 2453
Beta strandi247 – 2493
Helixi260 – 27213
Helixi279 – 30224
Beta strandi311 – 3155
Helixi330 – 33910
Beta strandi344 – 3485
Beta strandi361 – 3633
Helixi367 – 3737
Beta strandi375 – 3784
Helixi384 – 3929

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLIX-ray2.31A1-402[»]
1DLJX-ray1.80A1-402[»]
1LTYmodel-A1-402[»]
ProteinModelPortaliP0C0F4.
SMRiP0C0F4. Positions 1-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0F4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1454Substrate binding
Regioni249 – 2535Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1004.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
IPR028357. UDPglc_DH_bac.
[Graphical view]
PANTHERiPTHR11374. PTHR11374. 1 hit.
PfamiPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C0F4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI
60 70 80 90 100
EYYLKSKQLS IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV
110 120 130 140 150
IKEVLSVNSH ATLIIKSTIP IGFITEMRQK FQTDRIIFSP EFLRESKALY
160 170 180 190 200
DNLYPSRIIV SCEENDSPKV KADAEKFALL LKSAAKKNNV PVLIMGASEA
210 220 230 240 250
EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMIIQGIS YDDRIGMHYN
260 270 280 290 300
NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN
310 320 330 340 350
VLKEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP
360 370 380 390 400
MLNKLESEDQ SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG

RD
Length:402
Mass (Da):45,483
Last modified:September 13, 2005 - v1
Checksum:iDD1869D659F4CA58
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08444 Genomic DNA. Translation: AAA26899.1.
RefSeqiWP_011018341.1. NZ_JHTN01000039.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08444 Genomic DNA. Translation: AAA26899.1 .
RefSeqi WP_011018341.1. NZ_JHTN01000039.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0C0F4.
SMRi P0C0F4. Positions 1-402.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1004.

Enzyme and pathway databases

UniPathwayi UPA00038 ; UER00491 .
SABIO-RK P0C0F4.

Miscellaneous databases

EvolutionaryTracei P0C0F4.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
IPR028357. UDPglc_DH_bac.
[Graphical view ]
PANTHERi PTHR11374. PTHR11374. 1 hit.
Pfami PF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTi SM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsi TIGR03026. NDP-sugDHase. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, MUTAGENESIS OF CYS-260.

Entry informationi

Entry nameiUDG_STRPY
AccessioniPrimary (citable) accession number: P0C0F4
Secondary accession number(s): Q07172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: October 29, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3