Reviewed, UniProtKB/Swiss-Prot Q9XAR0 (NUOG_STRCO)

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:	SCO4568
ORF Names:	SCD16A.15c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	843 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. 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 – 843	843	NADH-quinone oxidoreductase subunit G		PRO_0000118563
Regions
	Domain	20 – 98	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	54	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	65	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	68	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	82	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	116	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	120	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	123	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	129	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	169	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	172	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	175	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	219	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	245	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	248	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	252	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	280	1	Iron-sulfur 4 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9XAR0-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 318D67C27AAA5193	FASTA	843	88,862
	10 20 30 40 50 60 MTVTTSTPSG GGAAAVPPED LVTLTIDGAE ISVPKGTLVI RAAEQLGIEI PRFCDHPLLD 70 80 90 100 110 120 PAGACRQCIV EVEGQRKPMA SCTITCTDGM VVKTQLTSPV AEKAQHGVME LLLINHPLDC 130 140 150 160 170 180 PVCDKGGECP LQNQAMSHGQ SDSRFEGKKR TYEKPVPIST QVLLDRERCV LCARCTRFSN 190 200 210 220 230 240 QVAGDPMIEL IERGALQQVG TGEGDPFESY FSGNTIQICP VGALTSAAYR FRSRPFDLIS 250 260 270 280 290 300 SPSVCEHCSG GCATRTDHRR GKVMRRLAAN EPEVNEEWIC DKGRFGFRYA QQRDRLTTPL 310 320 330 340 350 360 VRNAEGELEP ASWPEALQIA AQGLLASRGR TGVLTGGRLT VEDAYAYSKF ARVALDTNDI 370 380 390 400 410 420 DFRARVHSAE EADFLAAHVA GRGRDLGGSS RTESGGGAGV TYTSLEKAPA VLLVGFEAEE 430 440 450 460 470 480 EAPGVFLRLR KAWRKHGQKV FSLATHATRG LEKAGGTLLP AAPGTETEWL DALASGVGLE 490 500 510 520 530 540 EGGTQAAEAL RAEGAVIVVG ERLASVAGGL TSAVRTSAAT GARLVWIPRR AGERGAIEAG 550 560 570 580 590 600 ALPSLLPGGR PATDPRAREE VAALWGLADL PHRYGRDTGE IVEAAARGEL QALLVAGVEV 610 620 630 640 650 660 ADLPDPTRAR AALDEAGFVV SLELRPSEVS ERADVVLPVA AVAEKPGTFL NWEGRVRFFE 670 680 690 700 710 720 AALKPDQMTR RLAPTDARVL QMLADAMDVH LGLPDLRTTR AEIDRLGAWD GPRAGEPLQT 730 740 750 760 770 780 ASALPRPAAG EAVLAGHRLL LDQGLLQQGD EALAGTRHAA RARLSAATAA EAGVKDGDVL 790 800 810 820 830 840 AVTGPAGAVE LPLQVTEMPD RVVWLPLNSA GSGVASDAGV LPGTLVRIGP ATPAGAAPKE VEA

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939120 Genomic DNA. Translation: CAB44525.1.
PIR	T34618.
RefSeq	NP_628730.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1100008.
GenomeReviews	Gene locus SCO4568 in contig AL645882_GR.
KEGG	sco:SCO4568.
NMPDR	fig|100226.1.peg.4523.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9XAR0.
OMA	Q9XAR0. IGVQIPR.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO4568-MON.
BRENDA	1.6.99.5. 1084.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. 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]
Pfam	PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 2 hits. 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_STRCO

Accession

Primary (citable) accession number: Q9XAR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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