NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
Peng H.L., Chang J.T., Lee J.H., Chang H.Y.;
"Organization of UDP glucose dehydrogenase and UDP glucose pyrophosphorylase gene cluster in Pseudomonas aeruginosa PAO1.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).

Comments

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 .
PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis .
SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
SEQUENCE CAUTION:
- Sequence=CAA09327.1; Type=Frameshift; Positions=336, 372, 429;

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

AJ010734; CAA09327.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG05410.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H83393; H83393.

RefSeq

NP_250712.1; -.

3D structure databases

HSSP

P11759; 1MV8. [HSSP ENTRY / PDB]

ModBase

O86422.

Enzyme and pathway databases

BioCyc

PAER208964:PA2022-MON; -.

Organism-specific databases

PseudoCAP

PA2022; -.

Ontologies

GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
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

IPR013328; DHase_multihelical.
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:1.10.1040.10; Opine_DH; 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.

ProtoNet

O86422.

Genome annotation databases

879866; -.

AE004091_GR; PA2022.

pae:PA2022; -.

fig|208964.1.peg.2022; -.

Phylogenomic databases

HOGENOM

O86422; -.

Genome annotation databases

CMR

O86422; PA2022.

Other

UniRef

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

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 453`	`453`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074049`
`NP_BIND`	`2 19`	`18`	`NAD (Potential).`
`ACT_SITE`	`266 266`		`By similarity.`
`CONFLICT`	`81 81`		`F -> L (in Ref. 1; CAA09327).`
`CONFLICT`	`453 453`		`A -> R (in Ref. 1; CAA09327).`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 49690 Da [This is the MW of the unprocessed precursor]

CRC64: A8E7954D0D11557D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRLCVIGAGY VGLVTAACFA EMGNQVRCVE RDRERVARLR RGEMPIYEPG LESILRDQLD 

        70         80         90        100        110        120 
AARLTFTASL AEGLADAEVV FIAVGTPCGE DGSADLSHVL AVAEQLGAQL RQACIVVNKS 

       130        140        150        160        170        180 
TVPVGTAERV EEIIRLGLAR RRKRFRVAVA SNPEFLKEGS AVDDFRRPDR VIIGSAETQA 

       190        200        210        220        230        240 
GETLRQLYAP FLRNHERVLL MGRREAEFSK YAANAFLATK ISFMNEMAGL CALTGVDIED 

       250        260        270        280        290        300 
VRRGMGSDKR IGTHFIYAGC GYGGSCFPKD VRALIRSAEQ QGYDSQILRA VEARNARQKE 

       310        320        330        340        350        360 
LLFETLGELF QGRWQGRTVA LWGLAFKPGT DDLREAPSLV LLEALLRHGV RVRAHDPVAN 

       370        380        390        400        410        420 
AGVAARYPEA VACARLTLHD SPYAAVEGAD ALVLVTEWKQ FRQPDFQKIR GSMRTPLLVD 

       430        440        450 
GRNLYAPARM AELGFIYQGI GRPRAGHCKA SAA

O86422 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