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UniProtKB/Swiss-Prot entry A6L890


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

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Entry information
Entry name NRFA_PARD8
Primary accession number A6L890
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on July 24, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 13)
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: BDI_0109
From
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [TaxID: 435591] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidetes (class); Bacteroidales; Porphyromonadaceae; Parabacteroides.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0050156; PubMed=17579514 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.;
"Evolution of symbiotic bacteria in the distal human intestine.";
PLoS Biol. 5:1574-1586(2007).
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
CP000140; ABR41904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001301526.1; -.
3D structure databases
ModBase A6L890.
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).
QuickGo view.
Family and domain databases
HAMAP MF_01182; -; 1.
PBIL [Tree]
InterPro IPR003321; Cyt_c552.
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 A6L890.
Genome annotation databases
GeneID 5305200; -.
GenomeReviews CP000140_GR; BDI_0109.
KEGG pdi:BDI_0109; -.
CMR A6L890; BDI_0109.
Other
ProtoNet A6L890.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Repeat; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   494  463     Cytochrome c-552. PRO_1000065804
METAL   116   116        Iron (heme 3 axial ligand) (By similarity). 
METAL   148   148        Iron (heme 1 axial ligand) (By similarity). 
METAL   186   186        Iron (heme 2 axial ligand) (By similarity). 
METAL   228   228        Iron (heme 3 axial ligand) (By similarity). 
METAL   230   230        Calcium (By similarity). 
METAL   231   231        Calcium; via carbonyl oxygen (By similarity). 
METAL   276   276        Calcium; via carbonyl oxygen (By similarity). 
METAL   278   278        Calcium (By similarity). 
METAL   290   290        Iron (heme 5 axial ligand) (By similarity). 
METAL   301   301        Iron (heme 4 axial ligand) (By similarity). 
METAL   315   315        Iron (heme 2 axial ligand) (By similarity). 
METAL   332   332        Iron (heme 5 axial ligand) (By similarity). 
METAL   407   407        Iron (heme 4 axial ligand) (By similarity). 
BINDING   144   144        Heme 1 (covalent) (By similarity). 
BINDING   147   147        Heme 1 (covalent) (By similarity). 
BINDING   182   182        Heme 2 (covalent) (By similarity). 
BINDING   185   185        Heme 2 (covalent) (By similarity). 
BINDING   224   224        Heme 3 (covalent) (By similarity). 
BINDING   227   227        Heme 3 (covalent) (By similarity). 
BINDING   231   231        Substrate (By similarity). 
BINDING   279   279        Substrate (By similarity). 
BINDING   297   297        Heme 4 (covalent) (By similarity). 
BINDING   300   300        Heme 4 (covalent) (By similarity). 
BINDING   328   328        Heme 5 (covalent) (By similarity). 
BINDING   331   331        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 494 AA [This is the length of the unprocessed precursor] Molecular weight: 56145 Da [This is the MW of the unprocessed precursor] CRC64: 58ECCCF0E077EF53 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEKKLKSWQG WLLFGGTMVV VFVLGMIAAS VNERHAEVTS VMNNKKTEIT GIEARNDKFE 

        70         80         90        100        110        120 
SNYPREYQTW EATADTSFKS LYNGNQAVDV LEARPEMVIL WAGYAFSKDY STPRGHMHAI 

       130        140        150        160        170        180 
EDMRNTLRVG APMTENEGPQ PATCWTCKSP DVPRMMQAMG VDNFYKGKWA SLGKEIVNPI 

       190        200        210        220        230        240 
GCADCHEPEN MNLHISRPAL IEAFQRQGKD ITKATQQEMR SLVCAQCHVE YYFKGDGKYL 

       250        260        270        280        290        300 
TFPWDKGSTV EDMEAYYDEA GFADYTHKLS RAPILKAQHP DYEISQMGIH AQRGVSCADC 

       310        320        330        340        350        360 
HMPYKSEGGV KYSDHHIQSP LAMIDRTCQV CHRESEETLR NNVYERQNKA NEMRNRLETE 

       370        380        390        400        410        420 
LAKAHVEAKF AWDKGATEDQ MKDVLKLIRQ AQWRWDFGVA SHGGAFHAPQ EIQRILGNGL 

       430        440        450        460        470        480 
DKAMQARLAT AKVLAKLGYT DDVPMPDFST KEKAQQYIGL DMAAERTAKE KFLNTIVPQW 

       490 
MKEAQENNRL AKNI 

A6L890 in FASTA format

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