Reviewed, UniProtKB/Swiss-Prot P95175 (NUOG_MYCTU)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit G
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit G
    NDH-1 subunit G

Gene names

Name:	nuoG
Ordered Locus Names:	Rv3151, MT3239
ORF Names:	MTCY03A2.07c

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	806 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity.
Catalytic activity	NADH + quinone = NAD+ + quinol.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 3 4Fe-4S clusters per subunit By similarity.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular component	membrane Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 806	806	NADH-quinone oxidoreductase subunit G		PRO_0000118559
Regions
	Domain	15 – 93	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	49	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	60	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	63	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	77	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	111	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	115	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	118	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	124	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	164	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	167	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	170	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	214	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	240	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	243	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	247	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	275	1	Iron-sulfur 4 (4Fe-4S) Potential
Experimental info
	Sequence conflict	474	1	I → M in AAK47578. Ref.2
	Sequence conflict	604	1	T → A in AAK47578. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P95175-1 [UniParc]. Last modified July 1, 1997. Version 2. Checksum: 519A1EA833181064	FASTA	806	85,424
	10 20 30 40 50 60 MTQAADTDIR VGQPEMVTLT IDGVEISVPK GTLVIRAAEL MGIQIPRFCD HPLLEPVGAC 70 80 90 100 110 120 RQCLVEVEGQ RKPLASCTTV ATDDMVVRTQ LTSEIADKAQ HGVMELLLIN HPLDCPMCDK 130 140 150 160 170 180 GGECPLQNQA MSNGRTDSRF TEAKRTFAKP INISAQVLLD RERCILCARC TRFSDQIAGD 190 200 210 220 230 240 PFIDMQERGA LQQVGIYADE PFESYFSGNT VQICPVGALT GTAYRFRARP FDLVSSPSVC 250 260 270 280 290 300 EHCASGCAQR TDHRRGKVLR RLAGDDPEVN EEWNCDKGRW AFTYATQPDV ITTPLIRDGG 310 320 330 340 350 360 DPKGALVPTS WSHAMAVAAQ GLAAARGRTG VLVGGRVTWE DAYAYAKFAR ITLGTNDIDF 370 380 390 400 410 420 RARPHSAEEA DFLAARIAGR HMAVSYADLE SAPVVLLVGF EPEDESPIVF LRLRKAARRH 430 440 450 460 470 480 RVPVYTIAPF ATGGLHKMSG RLIKTVPGGE PAALDDLATG AVGDLLATPG AVIIVGERLA 490 500 510 520 530 540 TVPGGLSAAA RLADTTGARL AWVPRRAGER GALEAGALPT LLPGGRPLAD EVARAQVCAA 550 560 570 580 590 600 WHIAELPAAA GRDADGILAA AADETLAALL VGGIEPADFA DPDAVLAALD ATGFVVSLEL 610 620 630 640 650 660 RHSTVTERAD VVFPVAPTTQ KAGAFVNWEG RYRTFEPALR GSTLQAGQSD HRVLDALADD 670 680 690 700 710 720 MGVHLGVPTV EAAREELAAL GIWDGKHAAG PHIAATGPTQ PEAGEAILTG WRMLLDEGRL 730 740 750 760 770 780 QDGEPYLAGT ARTPVVRLSP DTAAEIGAAD GEAVTVSTSR GSITLPCSVT DMPDRVVWLP 790 800 LNSAGSTVHR QLRVTIGSIV KIGAGS

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842582 Genomic DNA. Translation: CAB06288.1. AE000516 Genomic DNA. Translation: AAK47578.1. Different initiation.
PIR	H70647.
RefSeq	NP_217667.1. NP_337764.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	887540. 923368.
GenomeReviews	Gene locus MT3239 in contig AE000516_GR. Gene locus Rv3151 in contig AL123456_GR.
KEGG	mtc:MT3239. mtu:Rv3151.
TIGR	MT3239.
Organism-specific databases
TubercuList	Rv3151.
Phylogenomic databases
HOGENOM	P95175.
OMA	P95175. LKQGGQW.
Enzyme and pathway databases
BRENDA	1.6.99.5. 809.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR009010. Asp_de-COase-like_fold. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006657. MPT_dinuc_bd. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOG_MYCTU

Accession

Primary (citable) accession number: P95175

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)