NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=41;
PubMed=9765575 [NCBI, ExPASy, EBI, Israel, Japan]
Kereszt A., Kiss E., Reuhs B.L., Carlson R.W., Kondorosi A., Putnoky P.;
"Novel rkp gene clusters of Sinorhizobium meliloti involved in capsular polysaccharide production and invasion of the symbiotic nodule: the rkpK gene encodes a UDP-glucose dehydrogenase.";
J. Bacteriol. 180:5426-5431(1998).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan]
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.";
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).

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: Capsule biogenesis; capsule polysaccharide biosynthesis .
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

AJ222661; CAA10918.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC45661.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T46573; T46573.

RefSeq

NP_385188.1; -.

3D structure databases

HSSP

P11759; 1MV8. [HSSP ENTRY / PDB]

ModBase

O54068.

Enzyme and pathway databases

BioCyc

SMEL266834:SMC02641-MON; -.

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.
IPR001100; Pyr_nuc-diS_OxRdtase.
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.

PRINTS

PR00411; PNDRDTASEI.

Genome annotation databases

1232726; -.

AL591688_GR; R01082.

sme:SMc02641; -.

fig|266834.1.peg.2376; -.

Phylogenomic databases

HOGENOM

O54068; -.

Genome annotation databases

CMR

O54068; R01082.

Other

ProtoNet

O54068.

UniRef

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

Keywords

Capsule biogenesis/degradation; Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 437`	`437`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074050`
`ACT_SITE`	`265 265`		`By similarity.`
`CONFLICT`	`109 109`		`A -> S (in Ref. 1; CAA10918).`
`CONFLICT`	`142 142`		`A -> V (in Ref. 1; CAA10918).`
`CONFLICT`	`318 318`		`I -> Y (in Ref. 1; CAA10918).`
`CONFLICT`	`335 335`		`S -> T (in Ref. 1; CAA10918).`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 47122 Da [This is the MW of the unprocessed precursor]

CRC64: 2D458D39A1D8EEC1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKITMIGAGY VGLVSGVCFA DFGHDVVCVD KDEGKISALK KGQIPIFEPG LDHLVASNVA 

        70         80         90        100        110        120 
SGRLNFTDDL KTAVAASDVV FIAVGTPSRR GDGHADLSYV YAAAREIAAN LQGFTVVVTK 

       130        140        150        160        170        180 
STVPVGTGDE VERIIRETNP AADVTVVSNP EFLREGAAIE DFKRPDRIVI GVDGSDGRAR 

       190        200        210        220        230        240 
EVMTEVYRPL YLNQSPLVFT TRRTSELIKY AGNAFLAMKI TFINEIADLC EKVGANVQDV 

       250        260        270        280        290        300 
ARGIGLDGRI GSKFLHAGPG YGGSCFPKDT LALVKTAQDH DTPVRLVETT VAVNDNRKRA 

       310        320        330        340        350        360 
MGRKVIAAAG GDIRGSKIAV LGLTFKPNTD DMRDSPAIAV VQALQDAGAR VTGYDPEGME 

       370        380        390        400        410        420 
NARKLIEGLD CARDPYEAAA EADALVIITE WNEFRALDFD RLKSTMKTPL LVDLRNIYRK 

       430 
DEVAKHGFRY ASIGRPD

O54068 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