Reviewed, UniProtKB/Swiss-Prot P98008 (NORB_PSEST)

Names and origin

Protein names

Recommended name:
    Nitric oxide reductase subunit B
    EC=1.7.99.7
Alternative name(s):
    Nitric oxide reductase cytochrome b subunit
    NOR large subunit

Gene names

Name:

norB

Organism

Pseudomonas stutzeri (Pseudomonas perfectomarina)

Taxonomic identifier

316 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	474 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	Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). NorB is the catalytic subunit of the enzyme complex. Shows proton pump activity across the membrane in denitrifying bacterial cells. The mononitrogen reduction is probably coupled to electron transport phosphorylation.
Catalytic activity	Nitrous oxide + acceptor + H(2)O = 2 nitric oxide + reduced acceptor.
Pathway	Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 3/4.
Subunit structure	Heterodimer of cytochromes b (large subunit) and c (small subunit).
Subcellular location	Cell membrane; Multi-pass membrane proteinPotential.
Induction	By nitric oxide Probable.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: InterPro mitochondrial respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric oxide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 474	473	Nitric oxide reductase subunit B		PRO_0000183473
Regions
	Transmembrane	19 – 39	21	Potential
	Transmembrane	61 – 81	21	Potential
	Transmembrane	95 – 115	21	Potential
	Transmembrane	145 – 165	21	Potential
	Transmembrane	169 – 189	21	Potential
	Transmembrane	207 – 227	21	Potential
	Transmembrane	243 – 263	21	Potential
	Transmembrane	270 – 290	21	Potential
	Transmembrane	308 – 328	21	Potential
	Transmembrane	348 – 368	21	Potential
	Transmembrane	390 – 410	21	Potential
	Transmembrane	433 – 453	21	Potential
Sites
	Metal binding	60	1	Iron (low-spin heme axial ligand) Probable
	Metal binding	207	1	Iron B Probable
	Metal binding	258	1	Iron B Probable
	Metal binding	259	1	Iron B Probable
	Metal binding	347	1	Iron (high-spin heme axial ligand) Probable
	Metal binding	349	1	Iron (low-spin heme axial ligand) Probable

Sequences

	Sequence		Length	Mass (Da)
	P98008-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6455FC53DCB27896	FASTA	474	53,137
	10 20 30 40 50 60 MSSFNPHLKF QSQAVAKPYF VFALILFVGQ VLFGLIMGLQ YVVGDFLFPL LPFNVARMVH 70 80 90 100 110 120 TNLLIVWLLF GFMGAAYYLI PEESDCELHS PKLAIILFWV FAAAGVLTIL GYLFVPYAAL 130 140 150 160 170 180 AEMTRNDLLP TMGREFLEQP TITKIGIVVV ALGFLYNIGM TMLKGRKTVV STVMMTGLIG 190 200 210 220 230 240 LAVFFLFAFY NPENLSRDKF YWWFVVHLWV EGVWELIMGA MLAFVLIKVT GVDREVIEKW 250 260 270 280 290 300 LYVIIAMALI TGIIGTGHHF FWIGAPTVWL WVGSIFSALE PLPFFAMVLF ALNMVNRRRR 310 320 330 340 350 360 EHPNKAASLW AIGTTVTAFL GAGVWGFMHT LAPVNYYTHG SQLTAAHGHL AFYGAYAMIV 370 380 390 400 410 420 MTMISYAMPR LRGLGEAPDA RAQRIEVWGF WLMTISMIAI TLFLTAAGVV QIWLQRIPAD 430 440 450 460 470 GAAMSFMNTA DQLAIFFWLR FIAGVFFLIG LVCYLYSFRQ RGRVPVVVAA PAAA

References

[1]	"Nitric oxide reductase from Pseudomonas stutzeri. Primary structure and gene organization of a novel bacterial cytochrome bc complex." Zumft W.G., Braun C., Cuypers H. Eur. J. Biochem. 219:481-490(1994) [PubMed: 7508388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16. Strain: ATCC 14405 / 218 / ZoBell.
[2]	"Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri." Heiss B., Frunzke K., Zumft W.G. J. Bacteriol. 171:3288-3297(1989) [PubMed: 2542222] [Abstract] Cited for: EPR SPECTROSCOPY. Strain: ATCC 14405 / 218 / ZoBell.
[3]	"The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases." Cheesman M.R., Zumft W.G., Thomson A.J. Biochemistry 37:3994-4000(1998) [PubMed: 9521721] [Abstract] Cited for: EPR SPECTROSCOPY. Strain: ATCC 14405 / 218 / ZoBell.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X53676 Genomic DNA. Translation: CAA82229.1.
PIR	S41117.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-241.
Family and domain databases
InterPro	IPR000883. COX1. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NORB_PSEST

Accession

Primary (citable) accession number: P98008

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)