B0BZW2 (NU1C_ACAM1) 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:	AM1_2158

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Acaryochloris

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_1000086932
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	176 – 196	21	Helical; Potential
	Transmembrane	204 – 224	21	Helical; Potential
	Transmembrane	249 – 269	21	Helical; Potential
	Transmembrane	308 – 328	21	Helical; Potential
	Transmembrane	351 – 371	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	B0BZW2 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 49FB2D64BA663085	FASTA	372	40,677
	10 20 30 40 50 60 MNPGIDLEQR FVETLMELGL TPGVAKTIWL PIPMLLMIIG ATVGVLVSVW LERKISAAAQ 70 80 90 100 110 120 QRIGPEYIGP LGILAPVADG IKLVFKEDIV PANTDPWLFT LGPILVVIPV FFSYLIVPFG 130 140 150 160 170 180 QNILITDLGI GIFFWIALSS IAPIGLLMAG YSSNNKYSLL GGLRAAAQSI SYEIPLALAV 190 200 210 220 230 240 LAVVMMSNSL STIDIVNQQS GYGILGWNVI RQPIGFMLFW IAALAECERL PFDLPEAEEE 250 260 270 280 290 300 LVAGYQTEYA GMKFALFYLG SYVNLVLSSI LVAVLYFGGW DLPIPATMIA DWINVDPNNA 310 320 330 340 350 360 IFELVTAGLG LVMTLLKAYF FLFLAILLRW TVPRVRIDQL LDFGWKFLLP VGLVNLLLTA 370 GLKLAFPFAF GG

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MBIC 11017.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW27172.1.
RefSeq	YP_001516486.1. NC_009925.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B0BZW2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5680972.
GenomeReviews	Gene locus AM1_2158 in contig CP000828_GR.
KEGG	amr:AM1_2158.
PATRIC	20618654. VBIAcaMar40141_1962.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG727670.
OMA	WNIFLQP.
PhylomeDB	B0BZW2.
ProtClustDB	PRK06076.
Enzyme and pathway databases
BioCyc	AMAR329726:AM1_2158-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_ACAM1

Accession

Primary (citable) accession number: B0BZW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program