P56914 (NUOG2_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit G 2
EC=1.6.99.5

Alternative name(s):
NADH dehydrogenase I subunit G 2
NDH-1 subunit G 2

Gene names

Name:	nuoG2
Ordered Locus Names:	RA0828
ORF Names:	SMa1523

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	853 AA.
Sequence status	Complete.
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 ubiquinone. 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. Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Domain	Repeat
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Plasmid
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 molybdenum ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on other nitrogenous compounds as donors 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 – 853	853	NADH-quinone oxidoreductase subunit G 2		PRO_0000118560
Regions
	Domain	1 – 78	78	2Fe-2S ferredoxin-type
	Domain	139 – 170	32	4Fe-4S ferredoxin-type 1
	Domain	179 – 209	31	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	34	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	62	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	94	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	98	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	101	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	107	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	148	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	151	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	154	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	198	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	224	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	227	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	231	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	259	1	Iron-sulfur 4 (4Fe-4S) Potential
Experimental info
	Sequence conflict	211	1	K → R in CAB51635. Ref.1
	Sequence conflict	285	1	T → A in CAB51635. Ref.1
	Sequence conflict	452	1	F → L in CAB51635. Ref.1
	Sequence conflict	459	1	T → I in CAB51635. Ref.1
	Sequence conflict	544	1	S → G in CAB51635. Ref.1
	Sequence conflict	554	1	R → K in CAB51635. Ref.1
	Sequence conflict	679	1	R → Q in CAB51635. Ref.1
	Sequence conflict	734	1	A → G in CAB51635. Ref.1
	Sequence conflict	756	1	H → R in CAB51635. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P56914 [UniParc]. Last modified November 2, 2001. Version 2. Checksum: CDF867CE3BD11A0B	FASTA	853	93,346
	10 20 30 40 50 60 MIKVTIDEQS LEVEAGSTVL AAAERLGIEI PTFCYWKRLP PLASCRMCLV EIEGLRRLQP 70 80 90 100 110 120 ACATVAADGM VVRTNTPLIE ETRSSMLDML LANHPLDCPI CDKGGECELQ DMVMAYGPGE 130 140 150 160 170 180 SRFRDPKRVF HSKDIRLSPV IIMNVNRCIQ CQRCVRMCEE VVGAVALGTV EKGMDTAVTG 190 200 210 220 230 240 FEGSLASCDQ CGNCVEVCPV GALMSFPYRY KARPWDLAET DTICPHCGTG CQLTVGARKG 250 260 270 280 290 300 EFMRVRSDWE HGVNRETLCV RGRFGLDFIE SRDRIKRPMI RRDGTLTPVS WEEAGDFLRQ 310 320 330 340 350 360 RLGVAEGKAA GGLISPRLPN EVLYQFQKLM RTVLRTNNVD CSSRWSAPLD ILVPIVASFY 370 380 390 400 410 420 SRDPLEQVIG KDCVLIIGGN VTEENPVTEY LLRDAARRRH TRLLMLSARP SRLDADARAV 430 440 450 460 470 480 LRAHPGGEGQ SLAAVVAALV AVTDEGLPDD IFAKTSGTTA SSGANDALDR LVSTLKEGRS 490 500 510 520 530 540 VTLLVSVDLL RSPLARKTLE QLGNLLQLLR LLGKEPSLQF LFDRANQMGA WDMGVLPGVL 550 560 570 580 590 600 PGLSPIADEA TRTRFERSWG AEIPREPGAD VDAMLELCEK GGMGVLYVVG SDPLISYPDR 610 620 630 640 650 660 EFVERALGAA NLLIVQDAFL TDTAGLADVV LPAAGYGEES GTFTNNEGRT QALRKFREPA 670 680 690 700 710 720 FDARSNLAIF GFIAALRERP LQPSTETVIF EEMTRLVPAY EGLTWEGLGA DGAFTTSAPK 730 740 750 760 770 780 PWTSGFFAPL SAPAVTDVLQ LITGNCLFHN GYVSEHSETL NSVADDPFIE MSAQDAAGLS 790 800 810 820 830 840 LSDGDQVLVR SARGELTAKL KVNRRFPHGL VFVPENYRAL RLNSLMRRGE YPCPVEIREC 850 AKRAASALDE ERV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rhizobium meliloti carries two sets of nuo genes." Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 41.
[2]	"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[3]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ245399 Genomic DNA. Translation: CAB51635.1. AE006469 Genomic DNA. Translation: AAK65486.1.
PIR	D95365.
RefSeq	NP_436074.1. NC_003037.1.
3D structure databases
ProteinModelPortal	P56914.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1235864.
GenomeReviews	Gene locus RA0828 in contig AE006469_GR.
KEGG	sme:SMa1523.
NMPDR	fig|266834.1.peg.828.
PATRIC	23628160. VBISinMel96828_0859.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG715033.
OMA	KDATIYD.
ProtClustDB	CLSK807690.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1523-MONOMER.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR009010. Asp_de-COase-like_fold. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. 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. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K00336.
Pfam	PF00111. Fer2. 1 hit. PF12838. Fer4_7. 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]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit. SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. 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

NUOG2_RHIME

Accession

Primary (citable) accession number: P56914

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 2, 2001
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program