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UniProtKB/Swiss-Prot entry Q0HMH8

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

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Entry information
Entry name NRFA_SHESM
Primary accession number Q0HMH8
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on December 12, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 19)
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: Shewmr4_0659
From
Shewanella sp. (strain MR-4) [TaxID: 60480] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
"Complete sequence of Shewanella sp. MR-4.";
Submitted (AUG-2006) 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
CP000446; ABI37739.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_732796.1; -.
3D structure databases
ModBase Q0HMH8.
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 Q0HMH8.
Genome annotation databases
GeneID 4251590; -.
GenomeReviews CP000446_GR; Shewmr4_0659.
KEGG she:Shewmr4_0659; -.
Phylogenomic databases
HOGENOM Q0HMH8; -.
Genome annotation databases
CMR Q0HMH8; Shewmr4_0659.
Other
ProtoNet Q0HMH8.
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    27  27     Potential. 
CHAIN   28   467  440     Cytochrome c-552. PRO_0000268976
METAL   87    87        Iron (heme 3 axial ligand) (By similarity). 
METAL   119   119        Iron (heme 1 axial ligand) (By similarity). 
METAL   157   157        Iron (heme 2 axial ligand) (By similarity). 
METAL   199   199        Iron (heme 3 axial ligand) (By similarity). 
METAL   201   201        Calcium (By similarity). 
METAL   202   202        Calcium (via carbonyl oxygen) (By similarity). 
METAL   250   250        Calcium (via carbonyl oxygen) (By similarity). 
METAL   252   252        Calcium (By similarity). 
METAL   264   264        Iron (heme 5 axial ligand) (By similarity). 
METAL   275   275        Iron (heme 4 axial ligand) (By similarity). 
METAL   290   290        Iron (heme 2 axial ligand) (By similarity). 
METAL   307   307        Iron (heme 5 axial ligand) (By similarity). 
METAL   382   382        Iron (heme 4 axial ligand) (By similarity). 
BINDING   115   115        Heme 1 (covalent) (By similarity). 
BINDING   118   118        Heme 1 (covalent) (By similarity). 
BINDING   153   153        Heme 2 (covalent) (By similarity). 
BINDING   156   156        Heme 2 (covalent) (By similarity). 
BINDING   195   195        Heme 3 (covalent) (By similarity). 
BINDING   198   198        Heme 3 (covalent) (By similarity). 
BINDING   202   202        Substrate (By similarity). 
BINDING   253   253        Substrate (By similarity). 
BINDING   271   271        Heme 4 (covalent) (By similarity). 
BINDING   274   274        Heme 4 (covalent) (By similarity). 
BINDING   303   303        Heme 5 (covalent) (By similarity). 
BINDING   306   306        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 467 AA [This is the length of the unprocessed precursor] Molecular weight: 51955 Da [This is the MW of the unprocessed precursor] CRC64: 2CCCF72DE6260D00 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MMKKMTGKSF ALSALVAASF MAAGAMASDK TEPRNEVYKD KFANQYNSWH DTAKSEEITD 

        70         80         90        100        110        120 
ALAGDPSLVI LWAGYGFAKD YNAPRGHMYA VTDVRNTLRT GAPTNAEDGP MPMACWSCKS 

       130        140        150        160        170        180 
PDVPRLIEEQ GEDGYFKGKW AKGGPEVVNT IGCSDCHEKG TPKLRISRPF AERGMEALGT 

       190        200        210        220        230        240 
PFDKASKKDK QSMVCGQCHV EYYFEKKDDR KGFVKFPWDS GTTVEQMEAY YDAIEFSDWT 

       250        260        270        280        290        300 
HSLSKTPMLK AQHPGYETWK MGVHGKNDVS CVDCHMPKVT NDKGRKYTDH KVGNPFDRFD 

       310        320        330        340        350        360 
ETCATCHSQS KEFLEGITKE RYAKVKELKA RAEGQLVKAH FEAAKAWEVG ATEAEMKPIL 

       370        380        390        400        410        420 
TDIRHAQWRW DFAIASHGVA AHAPEEALRI LGTAVDKAAD ARVKLAQLLA KKGVTDAVAI 

       430        440        450        460 
PDISTKAKAQ AALGMDMDKM NAEKEAFKKD MLPKWDAEAK KREATYK
Q0HMH8 in FASTA format

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