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{{Infobox enzyme
| Name = UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
| EC_number = 1.1.1.305
| CAS_number = 
| IUBMB_EC_number = 1/1/1/305
| GO_code = 
| image = 
| width = 
| caption =
}}
'''UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid [[Decarboxylation|decarboxylating]])''' ({{EC number|1.1.1.305}}, ''UDP-GlcUA decarboxylase'', ''ArnADH'') is an [[enzyme]] with system name ''UDP-glucuronate:NAD<sup>+</sup> oxidoreductase (decarboxylating)''.<ref>{{cite journal | title = A formyltransferase required for polymyxin resistance in ''Escherichia coli'' and the modification of lipid A with 4-amino-4-deoxy-L-arabinose.  Identification and function of UDP-4-deoxy-4-formamido-L-arabinose |author = Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. |journal = J. Biol. Chem. |year = 2005 |volume = 280 |pages = 14154–14167 |pmid = 15695810 | doi = 10.1074/jbc.M414265200 | issue = 14}}</ref><ref>{{cite journal | title = Crystal structure of ''Escherichia coli'' ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and  polymyxin resistance |author = Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. |journal = Biochemistry |year = 2004 |volume = 43 |pages = 13370–13379 |pmid = 15491143 | doi = 10.1021/bi048551f | issue = 42 | pmc = 2680612}}</ref><ref>{{cite journal | title = Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in  4-amino-4-deoxy-L-arabinose biosynthesis |author = Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. |journal = J. Biol. Chem. |year = 2005 |volume = 280 |pages = 23000–23008 |pmid = 15809294 | doi = 10.1074/jbc.M501534200 | issue = 24 | pmc = 3326539}}</ref><ref>{{cite journal | title = Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance |author = Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. |journal = Structure |year = 2005 |volume = 13 |pages = 929–942 |pmid = 15939024 | doi = 10.1016/j.str.2005.03.018 | issue = 6 | pmc = 2997725}}</ref><ref>{{cite journal | title = An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in ''Escherichia coli'' |author = Yan, A., Guan, Z. and Raetz, C.R.H. |journal = J. Biol. Chem. |year = 2007 |volume = 282 |pages = 36077–36089 |pmid = 17928292 | doi = 10.1074/jbc.M706172200 | issue = 49 | pmc = 2613183}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: UDP-glucuronate + NAD<sup>+</sup> <math>\rightleftharpoons</math> UDP-beta-L-threo-pentapyranos-4-ulose + CO<sub>2</sub> + NADH + H<sup>+</sup>

The activity is part of a bifunctional enzyme also performing the reaction of [[EC 2.1.2.13]] (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).

== References ==
{{reflist}}

== External links ==
* {{MeshName|UDP-glucuronic+acid+dehydrogenase+(UDP-4-keto-hexauronic+acid+decarboxylating)}}

[[Category:EC 1.1.1]]