Q3M9K9 (NU1C_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD(P)H-quinone oxidoreductase subunit 1
EC=1.6.5.-

Alternative name(s):
NAD(P)H dehydrogenase I subunit 1
NDH-1 subunit 1
NDH-A

Gene names

Name:	ndhA
Ordered Locus Names:	Ava_2714

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient By similarity. HAMAP MF_01350
Catalytic activity	NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01350
Subunit structure	NDH-1 is composed of at least 11 different subunits By similarity.
Subcellular location	Cellular thylakoid membrane; Multi-pass membrane protein By similarity HAMAP MF_01350.
Sequence similarities	Belongs to the complex I subunit 1 family.

Ontologies

Keywords
Cellular component	Membrane Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	NAD NADP Plastoquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW 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 – 372	372	NAD(P)H-quinone oxidoreductase subunit 1 HAMAP MF_01350		PRO_0000240035
Regions
	Transmembrane	27 – 47	21	Helical; Potential
	Transmembrane	65 – 85	21	Helical; Potential
	Transmembrane	97 – 117	21	Helical; Potential
	Transmembrane	128 – 148	21	Helical; Potential
	Transmembrane	166 – 186	21	Helical; Potential
	Transmembrane	204 – 224	21	Helical; Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Transmembrane	308 – 328	21	Helical; Potential
	Transmembrane	347 – 367	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3M9K9 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: C66CF9A01C7D60C5	FASTA	372	40,262
	10 20 30 40 50 60 MNSGIDLQGT FIKSLMDLGI PPGTAKAIWM PLPMILMLIG ATVGVLVCVW LERKISAAAQ 70 80 90 100 110 120 QRIGPEYIGP LGLLAPVADG LKLVFKEDIV PAQADPWLFT LGPILVVLPV FLSYLIVPFG 130 140 150 160 170 180 QNIVITNIGT GIFLWIALSS IQPIGLLMAG YSSNNKYSLL GGLRAAAQSI SYEIPLALSV 190 200 210 220 230 240 LAIVMMSNSL STVDIVNQQS GYGILGWNIW RQPLGFLIFW IAALAECERL PFDLPEAEEE 250 260 270 280 290 300 LVAGYQTEYS GMKFALFYLS SYVNLVLSAL LVAVLYLGGW DFPIPINVLA NLVGVSEANP 310 320 330 340 350 360 VLQVVSAALG ITMTLVKAYF LVFIAILLRW TVPRVRIDQL LDLGWKFLLP VGLVNLLLTA 370 ALKLAFPVAF GG

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000117 Genomic DNA. Translation: ABA22327.1.
RefSeq	YP_323222.1. NC_007413.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3M9K9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3682212.
GenomeReviews	Gene locus Ava_2714 in contig CP000117_GR.
KEGG	ava:Ava_2714.
NMPDR	fig|240292.3.peg.1051.
PATRIC	35426323. VBIAnaVar43351_3707.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1005.
HOGENOM	HBG727670.
OMA	WNIFLQP.
PhylomeDB	Q3M9K9.
ProtClustDB	PRK06076.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_2714-MONOMER.
Family and domain databases
HAMAP	MF_01350. NDH1_NuoH. [Tree]
InterPro	IPR001694. NADH_UbQ_OxRdtase_su1/FPO. IPR018086. NADH_UbQ_OxRdtase_su1_CS. [Graphical view]
KO	K05572.
PANTHER	PTHR11432. Resp_NADH_DH_1. 1 hit.
Pfam	PF00146. NADHdh. 1 hit. [Graphical view]
PROSITE	PS00667. COMPLEX1_ND1_1. 1 hit. PS00668. COMPLEX1_ND1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NU1C_ANAVT

Accession

Primary (citable) accession number: Q3M9K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	October 25, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program