Cytochrome c-552 precursor - Sulfurospirillum deleyianum

Names and origin

Protein names

Recommended name:
    Cytochrome c-552
    EC=1.7.2.2
Alternative name(s):
    Ammonia-forming cytochrome c nitrite reductase
      Short name=Cytochrome c nitrite reductase

Gene names

Name:

nrfA

Organism

Sulfurospirillum deleyianum

Taxonomic identifier

65553 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Sulfurospirillum

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Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Plays a role in nitrite reduction. HAMAP MF_01182
Catalytic activity	NH₃ + 2 H₂O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H⁺. Ref.2
Cofactor	Binds 1 calcium ion per monomer. HAMAP MF_01182 Binds 5 heme groups covalently per monomer. Ref.2
Pathway	Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182
Subunit structure	Homodimer. May also exist as a membrane-associated heterooligomeric complex. Ref.2
Subcellular location	Periplasm. HAMAP MF_01182
Miscellaneous	X-ray crystallographic analysis includes a sulfate ion that is thought to be at the substrate binding site. HAMAP MF_01182
Sequence similarities	Belongs to the cytochrome c-552 family.

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Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrogen compound metabolic process Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrite reductase (cytochrome, ammonia-forming) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

HAMAP MF_01182

Chain

22 – 514

493

Cytochrome c-552 HAMAP MF_01182

PRO_0000006583

Sites

Metal binding

101

1

Iron (heme 3 axial ligand) HAMAP MF_01182

Metal binding

133

1

Iron (heme 1 axial ligand) HAMAP MF_01182

Metal binding

171

1

Iron (heme 2 axial ligand) HAMAP MF_01182

Metal binding

214

1

Iron (heme 3 axial ligand) HAMAP MF_01182

Metal binding

216

1

Calcium HAMAP MF_01182

Metal binding

217

1

Calcium; via carbonyl oxygen HAMAP MF_01182

Metal binding

280

1

Calcium; via carbonyl oxygen HAMAP MF_01182

Metal binding

281

1

Calcium HAMAP MF_01182

Metal binding

293

1

Iron (heme 5 axial ligand) HAMAP MF_01182

Metal binding

304

1

Iron (heme 4 axial ligand) HAMAP MF_01182

Metal binding

318

1

Iron (heme 2 axial ligand) HAMAP MF_01182

Metal binding

336

1

Iron (heme 5 axial ligand) HAMAP MF_01182

Metal binding

411

1

Iron (heme 4 axial ligand) HAMAP MF_01182

Binding site

129

1

Heme 1 (covalent) HAMAP MF_01182

Binding site

132

1

Heme 1 (covalent) HAMAP MF_01182

Binding site

167

1

Heme 2 (covalent) HAMAP MF_01182

Binding site

170

1

Heme 2 (covalent) HAMAP MF_01182

Binding site

210

1

Heme 3 (covalent) HAMAP MF_01182

Binding site

213

1

Heme 3 (covalent) HAMAP MF_01182

Binding site

217

1

Substrate HAMAP MF_01182

Binding site

282

1

Substrate HAMAP MF_01182

Binding site

300

1

Heme 4 (covalent) HAMAP MF_01182

Binding site

303

1

Heme 4 (covalent) HAMAP MF_01182

Binding site

332

1

Heme 5 (covalent) HAMAP MF_01182

Binding site

335

1

Heme 5 (covalent) HAMAP MF_01182

Secondary structure

1

.

514

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z4P4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E63C119D4FA98562
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FASTA

514

57,611

        10         20         30         40         50         60 
MKFKLLLAGS LVAVGAMALL ASNINEKEKQ RVELAKAPSE AGIAGKEKSE EWAKYYPRQF 

        70         80         90        100        110        120 
DSWKKTKEYD SFTDMLAKDP ALVIAWSGYA FSKDYNSPRG HYYALQDNVN SLRTGAPVDA 

       130        140        150        160        170        180 
KTGPLPTACW TCKSPDVPRL IEEDGELEYF TGKWAKYGSQ IVNVIGCANC HDDKTAELKV 

       190        200        210        220        230        240 
RVPHLNRGLQ AAGLKTFEES THQDKRTLVC AQCHVEYYFK KTEWKDAKGA DKTAMVVTLP 

       250        260        270        280        290        300 
WANGVGKDGN AGVEGMIKYY DEINFSDWTH NISKTPMLKA QHPGFEFWKS GIHGQKGVSC 

       310        320        330        340        350        360 
ADCHMPYTQE GSVKYSDHQV KENPLDSMDQ SCMNCHRESE SKLRGIVHQK YERKEFLNKV 

       370        380        390        400        410        420 
AFDNIGKAHL ETGKAIEAGA SDEELKEVRK LIRHGQFKAD MAIAAHGNYF HAPEETLRLL 

       430        440        450        460        470        480 
AAGSDDAQKA RLLLVKILAK HGVMDYIAPD FDTKDKAQKL AKVDIAALAA EKMKFKQTLE 

       490        500        510 
QEWKKEAKAK GRANPELYKD VDTINDGKSS WNKK

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References

[1]	"Structure of cytochrome c nitrite reductase." Einsle O., Messerschmidt A., Stach P., Bourenkov G.P., Bartunik H.D., Huber R., Kroneck P.M.H. Nature 400:476-480(1999) [PubMed: 10440380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[2]	"Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties." Schumacher W., Hole U., Kroneck P.M.H. Biochem. Biophys. Res. Commun. 205:911-916(1994) [PubMed: 7999130] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, HEME-BINDING.

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Cross-references

Sequence databases

AJ133037 mRNA. Translation: CAB37320.2. Different initiation.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QDB	X-ray	1.90	A/B/C	42-514	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.7.2.2. 191626.

Family and domain databases

HAMAP

MF_01182.
[Tree]

InterPro

IPR003321. Cyt_c552.
IPR011031. Multihaem_cyt.
[Graphical view]

Pfam

PF02335. Cytochrom_C552. 1 hit.
[Graphical view]

PIRSF

PIRSF000243. Cyt_c552. 1 hit.

PROSITE

PS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

NRFA_SULDE

Accession

Primary (citable) accession number: Q9Z4P4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 70 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families