[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; DOI=10.1093/glycob/9.6.595; PubMed=10336992 [NCBI, ExPASy, EBI, Israel, Japan] Lind T., Falk E., Hjertson E., Kusche-Gullberg M., Lidholt K.; "cDNA cloning and expression of UDP-glucose dehydrogenase from bovine kidney."; Glycobiology 9:595-600(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Ascending colon; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 1-469. TISSUE=Liver; PubMed=7920253 [NCBI, ExPASy, EBI, Israel, Japan] Hempel J., Perozich J., Romovacek H., Hinich A., Kuo I., Feingold D.S.; "UDP-glucose dehydrogenase from bovine liver: primary structure and relationship to other dehydrogenases."; Protein Sci. 3:1074-1080(1994).
[4]	PROTEIN SEQUENCE OF 268-281. TISSUE=Liver; PubMed=6896145 [NCBI, ExPASy, EBI, Israel, Japan] Franzen B., Carrubba C., Feingold D.S., Ashcom J., Franzen J.S.; "Amino acid sequence of the tryptic peptide containing the catalytic-site thiol group of bovine liver uridine diphosphate glucose dehydrogenase."; Biochem. J. 199:599-602(1981).

Comments

FUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.
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 .
SUBUNIT: Homohexamer.
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

AF095792; AAC64183.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC150068; AAI50069.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A17150; A17150.

NP_776636.1; -.

3D structure databases

ModBase

P12378.

Ontologies

GO:0001702;	Biological process: gastrulation with mouth forming second (inferred from sequence or structural similarity from AgBase).
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.

BLOCKS

P12378.

Genome annotation databases

Ensembl

ENSBTAG00000014521; Bos taurus. [Contig view]

GeneID

281564; -.

KEGG

bta:281564; -.

Phylogenomic databases

HOVERGEN

P12378; -.

Other

ProtoNet

P12378.

UniRef

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

Keywords

Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 494`	`494`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074059`
`NP_BIND`	`6 23`	`18`	`NAD (By similarity).`
`REGION`	`162 165`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`276 276`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`41 41`		`NAD (By similarity).`
`BINDING`	`93 93`		`NAD (By similarity).`
`BINDING`	`131 131`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`165 165`		`NAD (By similarity).`
`BINDING`	`220 220`		`Substrate (By similarity).`
`BINDING`	`273 273`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`279 279`		`NAD (By similarity).`
`BINDING`	`339 339`		`Substrate (By similarity).`
`BINDING`	`346 346`		`NAD (By similarity).`
`MOD_RES`	`473 473`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`157 157`		`Missing (in Ref. 3; AA sequence).`
`CONFLICT`	`278 281`		`QKDV -> ZZGK (in Ref. 4; AA sequence).`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 55136 Da [This is the MW of the unprocessed precursor]

CRC64: 8560E27089C4D03E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDINES RINAWNSPTL PIYEPGLKEV 

        70         80         90        100        110        120 
VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS 

       130        140        150        160        170        180 
HGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI 

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPREKILT TNTWSSELSK LTANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW 

       310        320        330        340        350        360 
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE 

       370        380        390        400        410        420 
GAHLHIYDPK VPREQIVVDL SHPGVSKDDQ VARLVTISKD PYEACDGAHA VVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK KMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP 

       490 
KFSLQDMPNK KPRV

P12378 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