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UniProtKB/Swiss-Prot entry Q8D8E5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NRFA_VIBVU
Primary accession number Q8D8E5
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 40)
Name and origin of the protein
Protein name Cytochrome c-552 [Precursor]
Synonyms EC 1.7.2.2
Ammonia-forming cytochrome c nitrite reductase
Cytochrome c nitrite reductase
Gene name
Name: nrfA
OrderedLocusNames: VV1_3035
From
Vibrio vulnificus [TaxID: 672] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CMCP6;
Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
"Complete genome sequence of Vibrio vulnificus CMCP6.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE016795; AAO11359.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_761832.1; -.
3D structure databases
HSSP P32050; 1GU6. [HSSP ENTRY / PDB]
ModBase Q8D8E5.
Enzyme and pathway databases
BioCyc VVUL216895:VV1_3035-MON; -.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0042279; Molecular function: nitrite reductase (cytochrome, ammonia-forming) activity (inferred from electronic annotation from HAMAP).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01182; -; 1.
PBIL [Tree]
InterPro IPR003321; Cyt_c552.
IPR017570; Cytc_552_NO2Rdtase_formate-dep.
IPR011031; Multihaem_cyt.
Graphical view of domain structure.
Pfam PF02335; Cytochrom_C552; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000243; Cyt_c552; 1.
PROSITE PS51008; MULTIHEME_CYTC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q8D8E5.
Genome annotation databases
GeneID 1179862; -.
GenomeReviews AE016795_GR; VV1_3035.
KEGG vvu:VV1_3035; -.
Phylogenomic databases
HOGENOM Q8D8E5; -.
Genome annotation databases
CMR Q8D8E5; VV1_3035.
Other
ProtoNet Q8D8E5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    29  29     Potential. 
CHAIN   30   474  445     Cytochrome c-552. PRO_0000268983
METAL   91    91        Iron (heme 3 axial ligand) (By similarity). 
METAL   123   123        Iron (heme 1 axial ligand) (By similarity). 
METAL   161   161        Iron (heme 2 axial ligand) (By similarity). 
METAL   210   210        Iron (heme 3 axial ligand) (By similarity). 
METAL   212   212        Calcium (By similarity). 
METAL   213   213        Calcium (via carbonyl oxygen) (By similarity). 
METAL   258   258        Calcium (via carbonyl oxygen) (By similarity). 
METAL   260   260        Calcium (By similarity). 
METAL   272   272        Iron (heme 5 axial ligand) (By similarity). 
METAL   283   283        Iron (heme 4 axial ligand) (By similarity). 
METAL   298   298        Iron (heme 2 axial ligand) (By similarity). 
METAL   315   315        Iron (heme 5 axial ligand) (By similarity). 
METAL   390   390        Iron (heme 4 axial ligand) (By similarity). 
BINDING   119   119        Heme 1 (covalent) (By similarity). 
BINDING   122   122        Heme 1 (covalent) (By similarity). 
BINDING   157   157        Heme 2 (covalent) (By similarity). 
BINDING   160   160        Heme 2 (covalent) (By similarity). 
BINDING   206   206        Heme 3 (covalent) (By similarity). 
BINDING   209   209        Heme 3 (covalent) (By similarity). 
BINDING   213   213        Substrate (By similarity). 
BINDING   261   261        Substrate (By similarity). 
BINDING   279   279        Heme 4 (covalent) (By similarity). 
BINDING   282   282        Heme 4 (covalent) (By similarity). 
BINDING   311   311        Heme 5 (covalent) (By similarity). 
BINDING   314   314        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 474 AA [This is the length of the unprocessed precursor] Molecular weight: 53092 Da [This is the MW of the unprocessed precursor] CRC64: AE11CC4539C1B8A4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSIKHWMASS VSVTALVMTA LLNITAVSAE EKGLVDPRND AFEQNHPDQY QSWKKTSESV 

        70         80         90        100        110        120 
EIEDALAEDP NMVILWAGYG FAKDYNKARG HFYALDDVRQ TLRTGGPQDA KSGPMPMACW 

       130        140        150        160        170        180 
SCKSPDVARV IDERGEDGYF EGKWARLGAE IANPIGCADC HDTRSEKFKN GEPELALTRP 

       190        200        210        220        230        240 
YVERAFQAIN KPFEQQSRLD KQASVCAQCH VEYYFTGPTK AVKFPWDMGT GVQQMEEYYD 

       250        260        270        280        290        300 
ALGFADWTHA VSKAPMLKAQ HPGFETWREG IHGKNKVVCV DCHMPKVKKE DGTVYTDHKV 

       310        320        330        340        350        360 
GNPFDRFEDT CAQCHTQSKD QLREIVSTRK AQVLNMKLTA EKQIVAAHFE AGAAWKAGAT 

       370        380        390        400        410        420 
EEEMKPILQD IRHAQWRWDY AIASHGVHMH APEVALEVLG TAVDRAADAR TKLVRLLATK 

       430        440        450        460        470 
GITEPVQIPD ISTKAAAQKA LGMDMEKMNA EKQHFLKTVV PDWDKAAAER ESKY
Q8D8E5 in FASTA format

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