[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=406 / Type 3; PubMed=7929009 [NCBI, ExPASy, EBI, Israel, Japan] Arrecubieta C., Lopez R., Garcia E.; "Molecular characterization of cap3A, a gene from the operon required for the synthesis of the capsule of Streptococcus pneumoniae type 3: sequencing of mutations responsible for the unencapsulated phenotype and localization of the capsular cluster on the pneumococcal chromosome."; J. Bacteriol. 176:6375-6383(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=406 / Type 3; DOI=10.1016/0378-1119(95)00657-5; PubMed=8566758 [NCBI, ExPASy, EBI, Israel, Japan] Arrecubieta C., Garcia E., Lopez R.; "Sequence and transcriptional analysis of a DNA region involved in the production of capsular polysaccharide in Streptococcus pneumoniae type 3."; Gene 167:1-7(1995).
[3]	SEQUENCE REVISION TO 129 AND 228. Garcia E., Arrecubieta C., Munoz R., Mollerach M., Lopez R.; Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=WU2 / Serotype 3; DOI=10.1084/jem.181.3.973; PubMed=7869055 [NCBI, ExPASy, EBI, Israel, Japan] Dillard J.P., Vandersea M.W., Yother J.; "Characterization of the cassette containing genes for type 3 capsular polysaccharide biosynthesis in Streptococcus pneumoniae."; J. Exp. Med. 181:973-983(1995).

Comments

FUNCTION: Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis. Directly responsible for the transformation of some unencapsulated serotype-3 SP mutants to the encapsulated phenotype.
CATALYTIC ACTIVITY: UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH.
PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1 .
SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

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

Z47210; CAA87403.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z12159; CAA78147.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U15171; AAC43311.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q07172; 1DLJ. [HSSP ENTRY / PDB]

ModBase

Q57346.

Ontologies

GO:0003979;	Molecular function: UDP-glucose 6-dehydrogenase activity (inferred from electronic annotation from EC).
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.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Capsule biogenesis/degradation; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 394`	`394`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074053`
`NP_BIND`	`2 19`	`18`	`NAD (Potential).`
`ACT_SITE`	`259 259`		`By similarity.`
`CONFLICT`	`215 215`		`R -> A (in Ref. 4; AAC43311).`
`CONFLICT`	`247 247`		`Y -> D (in Ref. 4; AAC43311).`

Sequence information

Length: 394 AA [This is the length of the unprocessed precursor]

Molecular weight: 44697 Da [This is the MW of the unprocessed precursor]

CRC64: C68671ED88140FC3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIAIAGSGY VGLSLAVLLA QHHEVKVIDV IKDKVESINN RKSPIKDEAI EKYLVEKELN 

        70         80         90        100        110        120 
LEASLDPAHV YKDVEYAIIA TPTNYDVDLN QFDTSSVEAA IKTCMEYNDT CTIVIKSTIP 

       130        140        150        160        170        180 
EGYTKEVREK FNTDRIIFSP EFLRESKALY DNLYPSRIVV GTDLDDSELT KRAWQFADLL 

       190        200        210        220        230        240 
KGGAIKEEVP ILVVAFNEAE VAKLFSNTYL ATRVRYFNEI DTYSEVKGLN PKTIIDIVCY 

       250        260        270        280        290        300 
DPRIGSYYNN PSFGYGGYCL PKDTKQLKAS FRDVPENLIT AVVQSNKTRK DYIAGAILAK 

       310        320        330        340        350        360 
QPSVVGIYRL IMKSDSDNFR SSAVKGVMER LDNYGKEIVI YEPTIECDTF MGYRVIKSLD 

       370        380        390 
EFKNISDIVV ANRMNDDLRD IQEKLYTRDL FGRE

Q57346 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools