NDHA_MYCTU
ID NDHA_MYCTU Reviewed; 470 AA.
AC P95200; F2GN78; I6WYA2; Q7D9W6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Type II NADH:quinone oxidoreductase NdhA {ECO:0000305};
DE EC=1.6.5.9 {ECO:0000269|PubMed:15767566};
DE AltName: Full=Type II NADH dehydrogenase NdhA {ECO:0000303|PubMed:25128581};
GN Name=ndhA {ECO:0000303|PubMed:15767566};
GN OrderedLocusNames=Rv0392c {ECO:0000312|EMBL:CCP43122.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=H37Rv;
RX PubMed=15767566; DOI=10.1073/pnas.0500469102;
RA Weinstein E.A., Yano T., Li L.S., Avarbock D., Avarbock A., Helm D.,
RA McColm A.A., Duncan K., Lonsdale J.T., Rubin H.;
RT "Inhibitors of type II NADH:menaquinone oxidoreductase represent a class of
RT antitubercular drugs.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4548-4553(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=25128581; DOI=10.1016/j.gene.2014.08.024;
RA Awasthy D., Ambady A., Narayana A., Morayya S., Sharma U.;
RT "Roles of the two type II NADH dehydrogenases in the survival of
RT Mycobacterium tuberculosis in vitro.";
RL Gene 550:110-116(2014).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29382761; DOI=10.1073/pnas.1721545115;
RA Vilcheze C., Weinrick B., Leung L.W., Jacobs W.R. Jr.;
RT "Plasticity of Mycobacterium tuberculosis NADH dehydrogenases and their
RT role in virulence.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1599-1604(2018).
CC -!- FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase
CC that delivers electrons to the respiratory chain by oxidation of NADH
CC and reduction of quinones. {ECO:0000269|PubMed:15767566,
CC ECO:0000269|PubMed:29382761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000269|PubMed:15767566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + H(+) + NADH = a menaquinol + NAD(+);
CC Xref=Rhea:RHEA:29235, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:15767566};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q2FZV7};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q2FZV7};
CC -!- ACTIVITY REGULATION: Inhibited by phenothiazine analogs.
CC {ECO:0000269|PubMed:15767566}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15767566}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect virulence in
CC mice (PubMed:29382761). Deletion of the gene does not induce any major
CC redox perturbation in M.tuberculosis (PubMed:29382761). Non-essential,
CC can be deleted without causing any adverse effects in vitro
CC (PubMed:25128581). The ndh-ndhA double knockout could not be obtained,
CC suggesting that at least one type II NADH dehydrogenase is required for
CC M.tuberculosis growth (PubMed:29382761). {ECO:0000269|PubMed:25128581,
CC ECO:0000269|PubMed:29382761}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43122.1; -; Genomic_DNA.
DR RefSeq; NP_214906.1; NC_000962.3.
DR RefSeq; WP_003898428.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P95200; -.
DR SMR; P95200; -.
DR STRING; 83332.Rv0392c; -.
DR PaxDb; P95200; -.
DR PRIDE; P95200; -.
DR DNASU; 886430; -.
DR GeneID; 45424357; -.
DR GeneID; 886430; -.
DR KEGG; mtu:Rv0392c; -.
DR PATRIC; fig|83332.111.peg.431; -.
DR TubercuList; Rv0392c; -.
DR eggNOG; COG1252; Bacteria.
DR OMA; DHCIFLD; -.
DR PhylomeDB; P95200; -.
DR PHI-base; PHI:3629; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:MTBBASE.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Type II NADH:quinone oxidoreductase NdhA"
FT /id="PRO_0000452728"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 184
FT /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT BINDING 21..25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT BINDING 334..335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q2FZV7"
SQ SEQUENCE 470 AA; 50385 MW; 584208FA80048828 CRC64;
MTLSSGEPSA VGGRHRVVII GSGFGGLNAA KALKRADVDI TLISKTTTHL FQPLLYQVAT
GILSEGDIAP TTRLILRRQK NVRVLLGEVN AIDLKAQTVT SKLMDMTTVT PYDSLIVAAG
AQQSYFGNDE FATFAPGMKT IDDALELRGR ILGAFEAAEV STDHAERERR LTFVVVGAGP
TGVEVAGQIV ELAERTLAGA FRTITPSECR VILLDAAPAV LPPMGPKLGL KAQRRLEKMD
VEVQLNAMVT AVDYKGITIK EKDGGERRIE CACKVWAAGV AASPLGKMIA EGSDGTEIDR
AGRVIVEPDL TVKGHPNVFV VGDLMFVPGV PGVAQGAIQG ARYATTVIKH MVKGNDDPAN
RKPFHYFNKG SMATISRHSA VAQVGKLEFA GYFAWLAWLV LHLVYLVGYR NRIAALFAWG
ISFMGRARGQ MAITSQMIYA RLVMTLMEQQ AQGALAAAEQ AEHAEQEAAG
