Reviewed, UniProtKB/Swiss-Prot P06255 (NU1C_MARPO)

Names and origin

Protein names

Recommended name:
    NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
    EC=1.6.5.-
Alternative name(s):
    NAD(P)H dehydrogenase subunit 1
      Short name=NDH subunit 1
    NADH-plastoquinone oxidoreductase subunit 1

Gene names

Name:	ndhA
Synonyms:	ndh1

Encoded on

Plastid; Chloroplast

Organism

Marchantia polymorpha (Liverwort)

Taxonomic identifier

3197 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Marchantiophyta › Superclass II › Marchantiopsida › Marchantiidae › Marchantiales › Marchantiaceae › Marchantia

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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.
Catalytic activity	NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01350
Subunit structure	NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the complex I subunit 1 family.

Ontologies

Keywords
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transmembrane
Ligand	NAD NADP Plastoquinone
Molecular function	Oxidoreductase
PTM	Quinone
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 – 368	368	NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350		PRO_0000117510
Regions
	Transmembrane	27 – 47	21	Potential
	Transmembrane	97 – 117	21	Potential
	Transmembrane	130 – 150	21	Potential
	Transmembrane	166 – 186	21	Potential
	Transmembrane	204 – 224	21	Potential
	Transmembrane	249 – 269	21	Potential
	Transmembrane	270 – 290	21	Potential
	Transmembrane	305 – 325	21	Potential
	Transmembrane	348 – 368	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	P06255-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: EB37938FB4B75C0B	FASTA	368	41,510
	10 20 30 40 50 60 MISNINLEDK FFSFFFTLGF SKEFFNFLWI IFSILILMLG VTIGVLVLVW LERKISAAIQ 70 80 90 100 110 120 QRIGPEYAGP LGIIQALADG IKLFLKEDIV PAQGDVWLFN IGPILVLIPV FLSYLVIPFE 130 140 150 160 170 180 YNVILANFSI GVFFWIAVSS VVPLGLLMAG YGSNNKYSFL GGLRAAAQSI SYEIPLALSV 190 200 210 220 230 240 LSIALLSNSL STVDIVEAQS KYGFLSWNLW RQPIGFIVFF IASLAECERL PFDLPEAEEE 250 260 270 280 290 300 LVAGYQTEYS GMKFAFFYLA SYLNLLVSSL FVTILYLGGW HFSIPFFSLF KNFEWNLMSN 310 320 330 340 350 360 GISEVISIII GIVITLVKSY LFLFISIMTR WTLPRIRIDQ LLNLGWKFLL PIALGNLLLT TSFQLFLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA." Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K., Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H. Nature 322:572-574(1986) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Structure and organization of Marchantia polymorpha chloroplast genome. IV. Inverted repeat and small single copy regions." Kohchi T., Shirai H., Fukuzawa H., Sano T., Komano T., Umesono K., Inokuchi H., Ozeki H., Ohyama K. J. Mol. Biol. 203:353-372(1988) [PubMed: 3199437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X04465 Genomic DNA. Translation: CAA28139.1.
PIR	DELVN1. A00413.
RefSeq	NP_039353.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2702580.
Family and domain databases
HAMAP	MF_01350. [Tree]
InterPro	IPR001694. NADH_UbQ_OxRdtase_su1. IPR018086. NADH_UbQ_OxRdtase_su1_CS. [Graphical view]
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_MARPO

Accession

Primary (citable) accession number: P06255

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 64 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)