P19050 (NDHK1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
NAD(P)H dehydrogenase I subunit K 1
NDH-1 subunit K 1
Short name=NDH-K 1

Gene names

Name:	ndhK1
Synonyms:	psbG
Ordered Locus Names:	slr1280

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration By similarity. HAMAP MF_01356
Catalytic activity	NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01356
Subunit structure	NDH-1 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions.
Subcellular location	Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Probable Ref.6.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Thylakoid
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD NADP Plastoquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro metal ion binding 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
	Propeptide	1 – 2	2	HAMAP MF_01356		PRO_0000358500
	Chain	3 – 248	246	NAD(P)H-quinone oxidoreductase subunit K 1 HAMAP MF_01356		PRO_0000118760
Sites
	Metal binding	62	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	63	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	127	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	158	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	P19050 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: FF68BEA64B92F6E7	FASTA	248	27,346
	10 20 30 40 50 60 MSPNPANPTD LERVATAKIL NPASRSQVTQ DLSENVILTT VDDLYNWAKL SSLWPLLYGT 70 80 90 100 110 120 ACCFIEFAAL IGSRFDFDRF GLVPRSSPRQ ADLIITAGTI TMKMAPALVR LYEEMPEPKY 130 140 150 160 170 180 VIAMGACTIT GGMFSSDSTT AVRGVDKLIP VDVYIPGCPP RPEAIFDAII KLRKKVANES 190 200 210 220 230 240 IQERAITQQT HRYYSTSHQM KVVAPILDGK YLQQGTRSAP PRELQEAMGM PVPPALTTSQ QKEQLNRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid DNA and of the cyanobacterium Synechocystis sp. PCC6803." Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L. Mol. Gen. Genet. 216:60-69(1989) [PubMed: 2499764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
[3]	"Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803: identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex." Prommeenate P., Lennon A.M., Markert C., Hippler M., Nixon P.J. J. Biol. Chem. 279:28165-28173(2004) [PubMed: 15102833] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION AS A MEMBER OF THE NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, SUBCOMPLEXES OF NDH-1.
[4]	"Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803." Berger S., Ellersiek U., Kinzelt D., Steinmueller K. FEBS Lett. 326:246-250(1993) [PubMed: 8325373] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, CHARACTERIZATION AS A MEMBER OF THE NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX.
[5]	"Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803." Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M. J. Biol. Chem. 280:2587-2595(2005) [PubMed: 15548534] [Abstract] Cited for: PROTEIN SEQUENCE OF 90-119, CHARACTERIZATION AS A MEMBER OF THE NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, SUBCOMPLEXES OF NDH-1.
[6]	"Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC 6803." Srivastava R., Pisareva T., Norling B. Proteomics 5:4905-4916(2005) [PubMed: 16287171] [Abstract] Cited for: SUBCELLULAR LOCATION IN THYLAKOID.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17439 Genomic DNA. Translation: CAA35485.1. BA000022 Genomic DNA. Translation: BAA18284.1.
PIR	S04437.
RefSeq	NP_441604.1. NC_000911.1.
3D structure databases
ProteinModelPortal	P19050.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19050. 7 interactions.
STRING	P19050.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	953061.
GenomeReviews	Gene locus slr1280 in contig BA000022_GR.
KEGG	syn:slr1280.
NMPDR	fig|1148.1.peg.1705.
PATRIC	23840647. VBISynSp132158_1878.
Phylogenomic databases
eggNOG	COG0377.
HOGENOM	HBG553221.
OMA	ITMKMAP.
PhylomeDB	P19050.
ProtClustDB	PRK06411.
Enzyme and pathway databases
BioCyc	SSP1148:SLR1280-MONOMER.
Family and domain databases
HAMAP	MF_01356. NDH1_NuoB. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
Gene3D	G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit.
KO	K05582.
PANTHER	PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
TIGRFAMs	TIGR01957. NuoB_fam. 1 hit.
PROSITE	PS01150. COMPLEX1_20K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDHK1_SYNY3

Accession

Primary (citable) accession number: P19050

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program