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P09152

- NARG_ECOLI

UniProt

P09152 - NARG_ECOLI

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Protein

Respiratory nitrate reductase 1 alpha chain

Gene

narG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Iron-sulfur (4Fe-4S); via pros nitrogen
Metal bindingi54 – 541Iron-sulfur (4Fe-4S)
Metal bindingi58 – 581Iron-sulfur (4Fe-4S)
Metal bindingi93 – 931Iron-sulfur (4Fe-4S)
Metal bindingi223 – 2231Molybdenum

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  2. electron carrier activity Source: InterPro
  3. molybdenum ion binding Source: EcoCyc
  4. nitrate reductase activity Source: UniProtKB-EC
  5. oxidoreductase activity, acting on NAD(P)H Source: RefGenome

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. cytochrome complex assembly Source: EcoCyc
  3. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciEcoCyc:NARG-MONOMER.
ECOL316407:JW1215-MONOMER.
MetaCyc:NARG-MONOMER.

Protein family/group databases

TCDBi5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 1 alpha chain (EC:1.7.99.4)
Alternative name(s):
Nitrate reductase A subunit alpha
Quinol-nitrate oxidoreductase subunit alpha
Gene namesi
Name:narG
Synonyms:bisD, narC
Ordered Locus Names:b1224, JW1215
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10638. narG.

Subcellular locationi

GO - Cellular componenti

  1. intrinsic component of membrane Source: EcoCyc
  2. membrane Source: UniProtKB
  3. nitrate reductase complex Source: InterPro
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501H → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12471246Respiratory nitrate reductase 1 alpha chainPRO_0000063233Add
BLAST

Proteomic databases

PaxDbiP09152.
PRIDEiP09152.

Expressioni

Inductioni

By nitrate.

Gene expression databases

GenevestigatoriP09152.

Interactioni

Subunit structurei

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Interacts with the NarJ chaperone.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
narHP1134911EBI-547248,EBI-555067
narJP0AF2616EBI-547248,EBI-555043
narWP193177EBI-547248,EBI-555088
narYP193183EBI-547248,EBI-555059

Protein-protein interaction databases

DIPiDIP-10311N.
IntActiP09152. 22 interactions.
MINTiMINT-1233973.
STRINGi511145.b1224.

Structurei

Secondary structure

1
1247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi7 – 93Combined sources
Helixi11 – 133Combined sources
Beta strandi14 – 185Combined sources
Turni19 – 224Combined sources
Beta strandi23 – 264Combined sources
Helixi31 – 333Combined sources
Helixi34 – 407Combined sources
Beta strandi43 – 486Combined sources
Beta strandi52 – 554Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 747Combined sources
Helixi94 – 974Combined sources
Helixi98 – 1025Combined sources
Beta strandi113 – 1153Combined sources
Helixi116 – 12611Combined sources
Helixi132 – 1409Combined sources
Helixi143 – 1508Combined sources
Turni151 – 1544Combined sources
Beta strandi158 – 1603Combined sources
Helixi163 – 18018Combined sources
Helixi183 – 1853Combined sources
Beta strandi186 – 1894Combined sources
Helixi193 – 1953Combined sources
Helixi197 – 21014Combined sources
Beta strandi213 – 2153Combined sources
Turni218 – 2225Combined sources
Helixi227 – 2326Combined sources
Helixi241 – 2466Combined sources
Beta strandi248 – 2547Combined sources
Helixi257 – 2604Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 2717Combined sources
Helixi272 – 2743Combined sources
Beta strandi277 – 2815Combined sources
Helixi287 – 2915Combined sources
Beta strandi292 – 2965Combined sources
Turni300 – 3023Combined sources
Helixi303 – 31816Combined sources
Turni319 – 3213Combined sources
Helixi325 – 33410Combined sources
Beta strandi339 – 3457Combined sources
Beta strandi347 – 3559Combined sources
Helixi358 – 3603Combined sources
Beta strandi361 – 3633Combined sources
Helixi364 – 3663Combined sources
Helixi371 – 3733Combined sources
Beta strandi377 – 3793Combined sources
Helixi391 – 3933Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi405 – 4073Combined sources
Turni408 – 4103Combined sources
Turni421 – 4233Combined sources
Beta strandi425 – 4339Combined sources
Beta strandi450 – 46213Combined sources
Beta strandi468 – 4736Combined sources
Helixi474 – 4818Combined sources
Beta strandi493 – 4964Combined sources
Helixi505 – 5128Combined sources
Helixi516 – 53318Combined sources
Beta strandi537 – 5415Combined sources
Helixi543 – 5464Combined sources
Helixi551 – 56414Combined sources
Beta strandi574 – 5774Combined sources
Helixi587 – 5948Combined sources
Turni595 – 5995Combined sources
Beta strandi604 – 6063Combined sources
Helixi608 – 6158Combined sources
Helixi618 – 6214Combined sources
Helixi627 – 6293Combined sources
Helixi636 – 6383Combined sources
Helixi643 – 65210Combined sources
Beta strandi662 – 6643Combined sources
Turni666 – 6683Combined sources
Helixi669 – 6757Combined sources
Helixi680 – 69011Combined sources
Beta strandi691 – 6933Combined sources
Helixi696 – 6983Combined sources
Beta strandi702 – 7065Combined sources
Beta strandi709 – 7146Combined sources
Turni717 – 7215Combined sources
Beta strandi722 – 7243Combined sources
Helixi725 – 7317Combined sources
Turni744 – 7485Combined sources
Beta strandi753 – 7553Combined sources
Beta strandi767 – 7759Combined sources
Helixi778 – 7814Combined sources
Beta strandi784 – 7896Combined sources
Beta strandi797 – 7993Combined sources
Beta strandi805 – 8106Combined sources
Beta strandi813 – 8153Combined sources
Helixi823 – 83715Combined sources
Turni838 – 8414Combined sources
Beta strandi844 – 8518Combined sources
Helixi858 – 8603Combined sources
Beta strandi864 – 8663Combined sources
Helixi870 – 8723Combined sources
Turni879 – 8813Combined sources
Beta strandi885 – 8928Combined sources
Helixi893 – 8953Combined sources
Helixi896 – 9005Combined sources
Helixi906 – 9094Combined sources
Beta strandi912 – 9143Combined sources
Beta strandi917 – 9193Combined sources
Helixi922 – 93211Combined sources
Beta strandi936 – 9383Combined sources
Turni939 – 9424Combined sources
Beta strandi943 – 9453Combined sources
Helixi949 – 95911Combined sources
Turni961 – 9633Combined sources
Helixi965 – 97915Combined sources
Helixi984 – 9863Combined sources
Helixi988 – 9903Combined sources
Helixi997 – 10026Combined sources
Beta strandi1013 – 10153Combined sources
Beta strandi1019 – 10213Combined sources
Helixi1027 – 10326Combined sources
Beta strandi1041 – 10433Combined sources
Helixi1050 – 10545Combined sources
Turni1072 – 10787Combined sources
Beta strandi1085 – 10906Combined sources
Beta strandi1095 – 10984Combined sources
Turni1102 – 11043Combined sources
Helixi1106 – 11116Combined sources
Beta strandi1117 – 11215Combined sources
Helixi1122 – 11287Combined sources
Beta strandi1135 – 11406Combined sources
Beta strandi1143 – 115210Combined sources
Beta strandi1159 – 11613Combined sources
Beta strandi1168 – 11714Combined sources
Turni1176 – 11783Combined sources
Beta strandi1179 – 11813Combined sources
Helixi1185 – 11873Combined sources
Helixi1195 – 11973Combined sources
Beta strandi1205 – 12073Combined sources
Turni1209 – 12113Combined sources
Beta strandi1222 – 12276Combined sources
Beta strandi1229 – 12313Combined sources
Beta strandi1234 – 12385Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90A1-1247[»]
1R27X-ray2.00A/C2-1247[»]
1SIWX-ray2.20A2-1247[»]
1Y4ZX-ray2.00A2-1247[»]
1Y5IX-ray1.90A2-1247[»]
1Y5LX-ray2.50A2-1247[»]
1Y5NX-ray2.50A2-1247[»]
3EGWX-ray1.90A2-1245[»]
3IR5X-ray2.30A1-1247[»]
3IR6X-ray2.80A1-1247[»]
3IR7X-ray2.50A1-1247[»]
ProteinModelPortaliP09152.
SMRiP09152. Positions 2-1245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 107654Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Domaini

Apoenzyme contains at least 2 NarJ-binding sites, one interfering with membrane anchoring and another being involved in molybdenum insertion. The first binding-site is a short peptide sequence near the N-terminus that contains a twin-arginine homologous motif.2 Publications

Sequence similaritiesi

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5013.
HOGENOMiHOG000237341.
InParanoidiP09152.
KOiK00370.
OMAiQGTDSAM.
OrthoDBiEOG6RC3JS.
PhylomeDBiP09152.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006468. NarG.
IPR028189. Nitr_red_alph_N.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
PF14710. Nitr_red_alph_N. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01580. narG. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09152-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH
60 70 80 90 100
GVNCTGSCSW KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS
110 120 130 140 150
WYLYSANRLK YPMMRKRLMK MWREAKALHS DPVEAWASII EDADKAKSFK
160 170 180 190 200
QARGRGGFVR SSWQEVNELI AASNVYTIKN YGPDRVAGFS PIPAMSMVSY
210 220 230 240 250
ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE SADWYNSSYI
260 270 280 290 300
IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ
310 320 330 340 350
GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY
360 370 380 390 400
AAGRMLRAAD LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK
410 420 430 440 450
WNLEQRDGKT GEETELQLSL LGSQDEIAEV GFPYFGGDGT EHFNKVELEN
460 470 480 490 500
VLLHKLPVKR LQLADGSTAL VTTVYDLTLA NYGLERGLND VNCATSYDDV
510 520 530 540 550
KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII VGAGLNHWYH
560 570 580 590 600
LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ
610 620 630 640 650
RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA
660 670 680 690 700
ERMGWLPSAP QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP
710 720 730 740 750
ENGKNHPRNL FIWRSNLLGS SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV
760 770 780 790 800
KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC LYSDIILPTA TWYEKDDMNT
810 820 830 840 850
SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG HLGKETDIVT
860 870 880 890 900
LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF
910 920 930 940 950
TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI
960 970 980 990 1000
DAAEMILTLA PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI
1010 1020 1030 1040 1050
QAQPRKIISS PTWSGLEDEH VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ
1060 1070 1080 1090 1100
WMRDFGESLL VYRPPIDTRS VKEVIGQKSN GNQEKALNFL TPHQKWGIHS
1110 1120 1130 1140 1150
TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN SNGALTARAV
1160 1170 1180 1190 1200
VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG
1210 1220 1230 1240
GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK
Length:1,247
Mass (Da):140,489
Last modified:January 23, 2007 - v4
Checksum:i640ABAD5FF01DF25
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101Y → K AA sequence (PubMed:3053688)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16181 Genomic DNA. Translation: CAA34303.1.
X01164 Genomic DNA. Translation: CAA25611.1.
M11586 Genomic DNA. Translation: AAA24201.1.
U00096 Genomic DNA. Translation: AAC74308.1.
AP009048 Genomic DNA. Translation: BAA36094.1.
X15996 Genomic DNA. Translation: CAA34127.1.
L36649 Genomic DNA. Translation: AAA64296.1.
PIRiE64869. RDECNA.
RefSeqiNP_415742.1. NC_000913.3.
YP_489494.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74308; AAC74308; b1224.
BAA36094; BAA36094; BAA36094.
GeneIDi12934277.
945782.
KEGGiecj:Y75_p1199.
eco:b1224.
PATRICi32117708. VBIEscCol129921_1276.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16181 Genomic DNA. Translation: CAA34303.1 .
X01164 Genomic DNA. Translation: CAA25611.1 .
M11586 Genomic DNA. Translation: AAA24201.1 .
U00096 Genomic DNA. Translation: AAC74308.1 .
AP009048 Genomic DNA. Translation: BAA36094.1 .
X15996 Genomic DNA. Translation: CAA34127.1 .
L36649 Genomic DNA. Translation: AAA64296.1 .
PIRi E64869. RDECNA.
RefSeqi NP_415742.1. NC_000913.3.
YP_489494.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q16 X-ray 1.90 A 1-1247 [» ]
1R27 X-ray 2.00 A/C 2-1247 [» ]
1SIW X-ray 2.20 A 2-1247 [» ]
1Y4Z X-ray 2.00 A 2-1247 [» ]
1Y5I X-ray 1.90 A 2-1247 [» ]
1Y5L X-ray 2.50 A 2-1247 [» ]
1Y5N X-ray 2.50 A 2-1247 [» ]
3EGW X-ray 1.90 A 2-1245 [» ]
3IR5 X-ray 2.30 A 1-1247 [» ]
3IR6 X-ray 2.80 A 1-1247 [» ]
3IR7 X-ray 2.50 A 1-1247 [» ]
ProteinModelPortali P09152.
SMRi P09152. Positions 2-1245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10311N.
IntActi P09152. 22 interactions.
MINTi MINT-1233973.
STRINGi 511145.b1224.

Protein family/group databases

TCDBi 5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbi P09152.
PRIDEi P09152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74308 ; AAC74308 ; b1224 .
BAA36094 ; BAA36094 ; BAA36094 .
GeneIDi 12934277.
945782.
KEGGi ecj:Y75_p1199.
eco:b1224.
PATRICi 32117708. VBIEscCol129921_1276.

Organism-specific databases

EchoBASEi EB0632.
EcoGenei EG10638. narG.

Phylogenomic databases

eggNOGi COG5013.
HOGENOMi HOG000237341.
InParanoidi P09152.
KOi K00370.
OMAi QGTDSAM.
OrthoDBi EOG6RC3JS.
PhylomeDBi P09152.

Enzyme and pathway databases

BioCyci EcoCyc:NARG-MONOMER.
ECOL316407:JW1215-MONOMER.
MetaCyc:NARG-MONOMER.

Miscellaneous databases

EvolutionaryTracei P09152.
PROi P09152.

Gene expression databases

Genevestigatori P09152.

Family and domain databases

InterProi IPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006468. NarG.
IPR028189. Nitr_red_alph_N.
[Graphical view ]
Pfami PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
PF14710. Nitr_red_alph_N. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01580. narG. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.
    Mol. Gen. Genet. 218:249-256(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / TG1.
  2. "Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon."
    Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.
    Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / TG1.
  3. Blasco F.
    Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
    Strain: K12 / TG1.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene."
    McPherson M.J., Baron A.J., Pappin D.J.C., Wootton J.C.
    FEBS Lett. 177:260-264(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
    Strain: K12.
  8. "Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli."
    Li S.F., Rabi T., Demoss J.A.
    J. Bacteriol. 164:25-32(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
    Strain: PK27.
  9. "The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells."
    Noji S., Nohno T., Saito T., Taniguchi S.
    FEBS Lett. 252:139-143(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    Strain: K12.
  10. "Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals."
    Li S.F., Demoss J.A.
    J. Bacteriol. 169:4614-4620(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
  11. "Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli."
    Sodergren E.J., Hsu P.Y., Demoss J.A.
    J. Biol. Chem. 263:16156-16162(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
  12. "Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit."
    Magalon A., Asso M., Guigliarelli B., Rothery R.A., Bertrand P., Giordano G., Blasco F.
    Biochemistry 37:7363-7370(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-50, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
  13. "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli."
    Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B., Santini C.L., Giordano G.
    Mol. Microbiol. 28:435-447(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARJ.
  14. "Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli."
    Chan C.S., Howell J.M., Workentine M.L., Turner R.J.
    Biochem. Biophys. Res. Commun. 343:244-251(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARJ, DOMAIN.
  15. "NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly."
    Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.
    J. Biol. Chem. 281:2170-2176(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARJ, DOMAIN.
    Strain: K12 / MC4100 / JA176.
  16. "Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase."
    Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R., Claude J.B., Guerlesquin F., Magalon A.
    FEBS J. 277:1886-1895(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARJ.
  17. "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
    Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
    Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  18. "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
    Jormakka M., Richardson D., Byrne B., Iwata S.
    Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-1247.

Entry informationi

Entry nameiNARG_ECOLI
AccessioniPrimary (citable) accession number: P09152
Secondary accession number(s): P78294
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3