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| Accession Number: | P11349 |
| Protein Name: | NarH aka B1225 |
| Length: | 512 |
| Molecular Weight: | 58066.00 |
| Species: | Escherichia coli [83333] |
| Location1 / Topology2 / Orientation3: | Cell membrane1 / Peripheral membrane protein2 |
| Substrate | electron |
Cross database links:
| DIP: | DIP-10312N |
|---|---|
| RefSeq: | AP_001853.1 NP_415743.1 |
| Entrez Gene ID: | 945780 |
| BioCyc: | EcoCyc:NARH-MONOMER ECOL168927:B1225-MONOMER MetaCyc:NARH-MONOMER |
| KEGG: | ecj:JW1216 eco:b1225 |
Gene Ontology
GO:0031224
C:intrinsic to membrane
GO:0009325
C:nitrate reductase complex
GO:0005886
C:plasma membrane
GO:0051538
F:3 iron, 4 sulfur cluster binding
GO:0051539
F:4 iron, 4 sulfur cluster binding
GO:0009055
F:electron carrier activity
GO:0046872
F:metal ion binding
GO:0008940
F:nitrate reductase activity
GO:0005515
F:protein binding
GO:0009061
P:anaerobic respiration
GO:0017004
P:cytochrome complex assembly
GO:0022900
P:electron transport chain
GO:0042128
P:nitrate assimilation
GO:0006810
P:transport
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References (13)[1] “Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer.” Blasco F.et.al. 2674654 [2] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.” Oshima T.et.al. 8905232 [3] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [5] “narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes.” Sodergren E.J.et.al. 2832376 [6] “Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli.” Sodergren E.J.et.al. 3053688 [7] “EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism.” Guigliarelli B.et.al. 1321049 [8] “Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes.” Augier V.et.al. 8383531 [9] “Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes.” Augier V.et.al. 8388253 [10] “Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters.” Guigliarelli B.et.al. 8664273 [11] “The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters.” Rothery R.A.et.al. 9516445 | |
| Structure: | |
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| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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1: MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE 61: KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS 121: QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL 181: PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK 241: SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 301: LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS 361: PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET 421: VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF 481: GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP