Entry
Name
nicotinate dehydrogenase;
nicotinic acid hydroxylase;
nicotinate hydroxylase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
nicotinate:NADP+ 6-oxidoreductase (hydroxylating)
Reaction(IUBMB)
nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH + H+ [RN:
R01720 ]
Reaction(KEGG)
Substrate
Product
Comment
A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
History
EC 1.17.1.5 created 1972 as EC 1.5.1.13, transferred 2004 to EC 1.17.1.5
Pathway
ec00760 Nicotinate and nicotinamide metabolism
ec01120 Microbial metabolism in diverse environments
Orthology
K20445 nicotinate dehydrogenase FAD-subunit
K20446 nicotinate dehydrogenase small FeS subunit
K20447 nicotinate dehydrogenase large molybdopterin subunit
K20448 nicotinate dehydrogenase medium molybdopterin subunit
Genes
SOF : NCTC11214_04501(ndhM)
MALU : KU6B_09420 KU6B_24970
DTI : Desti_0416 Desti_0691
CPAT : CLPA_c02860(ndhF1) CLPA_c02870(ndhS1) CLPA_c02880(ndhL)
CPAE : CPAST_c02860(ndhF1) CPAST_c02870(ndhS1) CPAST_c02880(ndhL)
CALD : PWK10_12180 PWK10_12185
ACOL : K5I23_11315 K5I23_11320 K5I23_11325
DOR : Desor_0445 Desor_0446 Desor_1381 Desor_1382
DAI : Desaci_2061 Desaci_2062 Desaci_2063
DMI : Desmer_1309 Desmer_1310
FWA : DCMF_22605 DCMF_25575
AACX : DEACI_1213 DEACI_1473 DEACI_1474 DEACI_1596 DEACI_3801 DEACI_3802
ACAE : HYG86_14455 HYG86_14460
PROM : QO263_02190 QO263_18065 QO263_18070 QO263_18075 QO263_18080
BCOC : BLCOC_22520(ndhS_3)
MTHO : MOTHE_c12030(ndhM) MOTHE_c12040(ndhL)
MTHZ : MOTHA_c12900(ndhM) MOTHA_c12910(ndhL)
TEP : TepRe1_0411 TepRe1_0412 TepRe1_0413
TAE : TepiRe1_0458 TepiRe1_0459 TepiRe1_0460(ndhM)
NTH : Nther_2150 Nther_2151 Nther_2152 Nther_2153
TIS : P3962_00500 P3962_08805 P3962_08810 P3962_08820
TIZ : RBU61_01420 RBU61_01430 RBU61_01435
SOVA : SOV_13250(ndhL) SOV_13260(ndhM)
SSID : SPSIL_018490(ndhL) SPSIL_018500(ndhM)
FBS : N510_000961(ndhF) N510_000962(ndhS)
PFLA : Pflav_009980 Pflav_036150 Pflav_072710 Pflav_072730
IPO : Ilyop_0111 Ilyop_0112 Ilyop_0113 Ilyop_0114
» show all
Taxonomy
Reference
Authors
Holcenberg JS, Stadtman ER.
Title
Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.
Journal
J Biol Chem 244:1194-203 (1969)
Reference
Authors
Gladyshev VN, Khangulov SV, Stadtman TC
Title
Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri.
Journal
Sequence
Reference
Authors
Gladyshev VN, Khangulov SV, Stadtman TC.
Title
Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme.
Journal
Reference
Authors
Dilworth GL.
Title
Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri.
Journal
Reference
Authors
Dilworth GL.
Title
Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri.
Journal
Reference
6
Authors
Nagel M, Andreesen JR.
Title
Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini.
Journal
Arch Microbiol 154:605-613 (1990)
Other DBs
ExplorEnz - The Enzyme Database: 1.17.1.5
ExPASy - ENZYME nomenclature database: 1.17.1.5