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Protein

UDP-glucose 6-dehydrogenase TuaD

Gene

tuaD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.

Miscellaneous

The nature of the anionic polymer present in the cell wall of B.subtilis depends on phosphate availability. Under phosphate-replete growth conditions teichoic acids are present, whereas under phosphate-depleted conditions, at least part of the wall teichoic acid is replaced with teichuronic acid, a non-phosphate containing anionic polymer. The synthesis of teichuronic acid is accompanied by degradation of teichoic acid and reutilization of liberated phosphate for other cellular processes such as nucleic acid synthesis.

Catalytic activityi

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

Enzyme regulationi

Activated by phosphorylation; inhibited by dephosphorylation.1 Publication

Pathwayi: UDP-alpha-D-glucuronate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose.
Proteins known to be involved in this subpathway in this organism are:
  1. UDP-glucose 6-dehydrogenase YwqF (ywqF), Putative UDP-glucose 6-dehydrogenase YtcA (ytcA), UDP-glucose 6-dehydrogenase TuaD (tuaD)
This subpathway is part of the pathway UDP-alpha-D-glucuronate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose, the pathway UDP-alpha-D-glucuronate biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei261By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi3 – 20NADSequence analysisAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processCell wall biogenesis/degradation, Stress response
LigandNAD

Enzyme and pathway databases

BioCyciBSUB:BSU35580-MONOMER
MetaCyc:BSU35580-MONOMER
UniPathwayiUPA00038; UER00491

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose 6-dehydrogenase TuaD (EC:1.1.1.22)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
Alternative name(s):
Teichuronic acid biosynthesis protein TuaD
Gene namesi
Name:tuaD
Synonyms:yvhD
Ordered Locus Names:BSU35580
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000740751 – 461UDP-glucose 6-dehydrogenase TuaDAdd BLAST461

Post-translational modificationi

Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO32271
PRIDEiO32271

Expressioni

Inductioni

By phosphate starvation, via the PhoP/PhoR two-component regulatory system.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019241

Structurei

3D structure databases

ProteinModelPortaliO32271
SMRiO32271
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6Y Bacteria
COG1004 LUCA
HOGENOMiHOG000153773
InParanoidiO32271
KOiK00012
OMAiYDPIAIP
PhylomeDBiO32271

Family and domain databases

InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR036291 NAD(P)-bd_dom_sf
IPR017476 UDP-Glc/GDP-Man
IPR014027 UDP-Glc/GDP-Man_DH_C
IPR036220 UDP-Glc/GDP-Man_DH_C_sf
IPR014026 UDP-Glc/GDP-Man_DH_dimer
IPR001732 UDP-Glc/GDP-Man_DH_N
IPR028357 UDPglc_DH_bac
PfamiView protein in Pfam
PF00984 UDPG_MGDP_dh, 1 hit
PF03720 UDPG_MGDP_dh_C, 1 hit
PF03721 UDPG_MGDP_dh_N, 1 hit
PIRSFiPIRSF500134 UDPglc_DH_bac, 1 hit
PIRSF000124 UDPglc_GDPman_dh, 1 hit
SMARTiView protein in SMART
SM00984 UDPG_MGDP_dh_C, 1 hit
SUPFAMiSSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit
SSF52413 SSF52413, 1 hit
TIGRFAMsiTIGR03026 NDP-sugDHase, 1 hit

Sequencei

Sequence statusi: Complete.

O32271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIAVIGTG YVGLVSGTCF AEIGNKVVCC DIDESKIRSL KNGVIPIYEP
60 70 80 90 100
GLADLVEKNV LDQRLTFTND IPSAIRASDI IYIAVGTPMS KTGEADLTYV
110 120 130 140 150
KAAAKTIGEH LNGYKVIVNK STVPVGTGKL VQSIVQKASK GRYSFDVVSN
160 170 180 190 200
PEFLREGSAI HDTMNMERAV IGSTSHKAAA IIEELHQPFH APVIKTNLES
210 220 230 240 250
AEMIKYAANA FLATKISFIN DIANICERVG ADVSKVADGV GLDSRIGRKF
260 270 280 290 300
LKAGIGFGGS CFPKDTTALL QIAKSAGYPF KLIEAVIETN EKQRVHIVDK
310 320 330 340 350
LLTVMGSVKG RTISVLGLAF KPNTNDVRSA PALDIIPMLQ QLGAHVKAYD
360 370 380 390 400
PIAIPEASAI LGEQVEYYTD VYAAMEDTDA CLILTDWPEV KEMELVKVKT
410 420 430 440 450
LLKQPVIIDG RNLFSLEEMQ AAGYIYHSIG RPAVRGTEPS DKYFPGLPLE
460
ELAKDLGSVN L
Length:461
Mass (Da):49,816
Last modified:January 1, 1998 - v1
Checksum:iF3B4D189FEC90095
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015609 Genomic DNA Translation: AAB94865.1
AL009126 Genomic DNA Translation: CAB15575.1
PIRiF69727
RefSeqiNP_391438.1, NC_000964.3
WP_003242596.1, NZ_JNCM01000033.1

Genome annotation databases

EnsemblBacteriaiCAB15575; CAB15575; BSU35580
GeneIDi936766
KEGGibsu:BSU35580
PATRICifig|224308.179.peg.3849

Similar proteinsi

Entry informationi

Entry nameiTUAD_BACSU
AccessioniPrimary (citable) accession number: O32271
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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