UniProt Accession

 NARH_ECOLI; P11349 

Genbank Protein ID

 M20147; U00096; AP009048; X16181 

Genbank Nucleotide ID

 AAA24195.1; AAC74309.1; BAA36095.1; CAA34304.1 

Protein Name

 Respiratory nitrate reductase 1 beta chain 

Protein Synonyms/Alias

 Nitrate reductase A subunit beta; Quinol-nitrate oxidoreductase subunit beta 

Gene Name

 narH 

Gene Synonyms/Alias

 b1225; JW1216 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
61	TDWENQEKYKGGWIR	acetylation	[1]
154	DLGGEFDKLAKDKNF	acetylation	[1]
290	AASTENEKDLYQRQL	acetylation	[1]
307	FLDPNDPKVIEQAIK	acetylation	[1]
314	KVIEQAIKDGIPLSV	acetylation	[1]
338	YKMAMEWKLALPLHP	acetylation	[1]
400	LLTAGDTKPVLRALK	acetylation	[1, 2]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. 

Sequence Annotation

 DOMAIN 7 35 4Fe-4S ferredoxin-type 1.
 DOMAIN 175 206 4Fe-4S ferredoxin-type 2.
 DOMAIN 208 237 4Fe-4S ferredoxin-type 3.
 METAL 16 16 Iron-sulfur 1 (4Fe-4S).
 METAL 19 19 Iron-sulfur 1 (4Fe-4S).
 METAL 22 22 Iron-sulfur 1 (4Fe-4S).
 METAL 26 26 Iron-sulfur 2 (4Fe-4S).
 METAL 184 184 Iron-sulfur 3 (4Fe-4S).
 METAL 187 187 Iron-sulfur 3 (4Fe-4S).
 METAL 192 192 Iron-sulfur 3 (4Fe-4S).
 METAL 196 196 Iron-sulfur 4 (3Fe-4S).
 METAL 217 217 Iron-sulfur 4 (3Fe-4S).
 METAL 223 223 Iron-sulfur 4 (3Fe-4S).
 METAL 227 227 Iron-sulfur 3 (4Fe-4S).
 METAL 244 244 Iron-sulfur 2 (4Fe-4S).
 METAL 247 247 Iron-sulfur 2 (4Fe-4S).
 METAL 259 259 Iron-sulfur 2 (4Fe-4S).
 METAL 263 263 Iron-sulfur 1 (4Fe-4S).  

Keyword

 3D-structure; 3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase; Reference proteome; Repeat; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 512 AA 

Protein Sequence

Gene Ontology

 GO:0031224; C:intrinsic to membrane; IDA:EcoCyc.
 GO:0009325; C:nitrate reductase complex; IEA:InterPro.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IPI:EcoCyc.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0009055; F:electron carrier activity; IPI:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008940; F:nitrate reductase activity; IEA:EC.
 GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
 GO:0017004; P:cytochrome complex assembly; IDA:EcoCyc.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. 

Interpro

 IPR017896; 4Fe4S_Fe-S-bd.
 IPR006547; NO3_Rdtase_bsu. 

Pfam

 PF13247; Fer4_11 

SMART

  

PROSITE

 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2 

PRINTS