ndh

ndh
168

NADH dehydrogenase (Menaquinone 7 & no proton)

Locus
BSU_12290
Molecular weight
41.79 kDa
Isoelectric point
6.29
Protein length
392 aaSequenceBlast
Gene length
1179 bpSequenceBlast
Function
respiration
Product
NADH dehydrogenase (Menaquinone 7 & no proton)
Essential
no
Synonyms
ndh, yjlD
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1252 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,299,074 1,300,252
Phenotypes of a mutant
inactivation of ndh facilitates growth without a cell wall (due to reduction of oxidative stress) PubMed
poor growth PubMed
non-transformable PubMed
The protein
Protein family
NADH dehydrogenase family (with YutJ and YumB, according to UniProt)
Cofactors
FAD PubMed
Structure
4NWZ (PDB) (from C. thermarum, 42% identity) PubMed
P80861 (AlphaFold)
Paralogous protein(s)
YumB
Localization
membrane associated PubMed
Additional information
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Genes
yjlC-ndh
Description
PubMed
Regulation
induced at high NADH+ levels (Rex) PubMed
repressed under anaerobic conditions (ResD) PubMed
Regulatory mechanism
Rex: repression, PubMed, in rex regulon
stringent response: negative regulation, in stringent response
ResD: repression, PubMed, in resD regulon
Open in new tab

yjlC→ndh

2025-03-28 06:46:30

Jstuelk

160

8fc075b2517874a07db87d69d9d785f0de7f3d21

1C60502BB7D833D4CC4509CD6E259B0F8D511F21

Genes
yjlB-yjlC-ndh
Description
PubMed
Open in new tab

yjlB→ndh

2025-03-31 23:41:58

Jstuelk

140

d86a69dcbb03e87c0c11960d4290b254a76a2100

D56200C8EE048511C4EFA1B76D998771F9C5F8C9

Biological materials
Mutant
MGNA-A358 (yjlD::erm), available at the NBRP B. subtilis, Japan
BKE12290 (ndh::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATCGTATATCCTCCGTCCT, downstream forward: _UP4_TAATCCTTTTAATGAATCTG
BKK12290 (ndh::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATCGTATATCCTCCGTCCT, downstream forward: _UP4_TAATCCTTTTAATGAATCTG
References
O'Reilly FJ, Graziadei A, Forbrig C, Bremenkamp R, Charles K, Lenz S, Elfmann C, Fischer L, Stülke J, Rappsilber JProtein complexes in cells by AI-assisted structural proteomics.Molecular systems biology. 2023 Feb 23; :e11544. PMID: 36815589
Vamshi Krishna K, Venkata Mohan S Purification and Characterization of NDH-2 Protein and Elucidating Its Role in Extracellular Electron Transport and Bioelectrogenic Activity. Frontiers in microbiology. 2019; 10:880. doi:10.3389/fmicb.2019.00880. PMID:31133996
Chumsakul O, Anantsri DP, Quirke T, Oshima T, Nakamura K, Ishikawa S, Nakano MM Genome-wide Identification of ResD, NsrR, and Fur Binding in Bacillus subtilis during Anaerobic Fermentative Growth by in vivo Footprinting. Journal of bacteriology. 2017 Apr 24; . pii:JB.00086-17. doi:10.1128/JB.00086-17. PMID:28439033
Koo BM, Kritikos G, Farelli JD, Todor H, Tong K, Kimsey H, Wapinski I, Galardini M, Cabal A, Peters JM, Hachmann AB, Rudner DZ, Allen KN, Typas A, Gross CA Construction and Analysis of Two Genome-Scale Deletion Libraries for Bacillus subtilis. Cell systems. 2017 Mar 22; 4(3):291-305.e7. pii:S2405-4712(16)30447-1. doi:10.1016/j.cels.2016.12.013. PMID:28189581
Kawai Y, Mercier R, Wu LJ, Domínguez-Cuevas P, Oshima T, Errington J Cell growth of wall-free L-form bacteria is limited by oxidative damage. Current biology : CB. 2015 Jun 15; 25(12):1613-8. doi:10.1016/j.cub.2015.04.031. pii:S0960-9822(15)00482-0. PMID:26051891
Heikal A, Nakatani Y, Dunn E, Weimar MR, Day CL, Baker EN, Lott JS, Sazanov LA, Cook GM Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. Molecular microbiology. 2014 Mar; 91(5):950-64. doi:10.1111/mmi.12507. PMID:24444429
Meyer FM, Gerwig J, Hammer E, Herzberg C, Commichau FM, Völker U, Stülke J Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon. Metabolic engineering. 2011 Jan; 13(1):18-27. doi:10.1016/j.ymben.2010.10.001. PMID:20933603
Hahne H, Wolff S, Hecker M, Becher D From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics. 2008 Oct; 8(19):4123-36. doi:10.1002/pmic.200800258. PMID:18763711
Gyan S, Shiohira Y, Sato I, Takeuchi M, Sato T Regulatory loop between redox sensing of the NADH/NAD(+) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis. Journal of bacteriology. 2006 Oct; 188(20):7062-71. . PMID:17015645
Eymann C, Dreisbach A, Albrecht D, Bernhardt J, Becher D, Gentner S, Tam le T, Büttner K, Buurman G, Scharf C, Venz S, Völker U, Hecker M A comprehensive proteome map of growing Bacillus subtilis cells. Proteomics. 2004 Oct; 4(10):2849-76. . PMID:15378759
Eymann C, Homuth G, Scharf C, Hecker M Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis. Journal of bacteriology. 2002 May; 184(9):2500-20. . PMID:11948165
Ye RW, Tao W, Bedzyk L, Young T, Chen M, Li L Global gene expression profiles of Bacillus subtilis grown under anaerobic conditions. Journal of bacteriology. 2000 Aug; 182(16):4458-65. . PMID:10913079

56F407D408272F3674612C9CDFE4A922680EC694

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Time of last update: 2025-04-06 02:53:24

Author of last update: Jstuelk