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Protein

Respiratory nitrate reductase 1 alpha chain

Gene

narG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi50Iron-sulfur (4Fe-4S); via pros nitrogen1
Metal bindingi54Iron-sulfur (4Fe-4S)1
Metal bindingi58Iron-sulfur (4Fe-4S)1
Metal bindingi93Iron-sulfur (4Fe-4S)1
Metal bindingi223Molybdenum1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: EcoCyc
  • molybdenum ion binding Source: InterPro
  • molybdopterin cofactor binding Source: EcoCyc
  • nitrate reductase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
  • nitrate metabolic process Source: EcoCyc
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.
BRENDAi1.7.5.1. 2026.
1.7.99.4. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10638. narG.

Subcellular locationi

GO - Cellular componenti

  • intrinsic component of membrane Source: EcoCyc
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • NarGHI complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi50H → S: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000632332 – 1247Respiratory nitrate reductase 1 alpha chainAdd BLAST1246

Proteomic databases

PaxDbiP09152.
PRIDEiP09152.

Expressioni

Inductioni

By nitrate.

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

BioGridi4263271. 19 interactors.
DIPiDIP-10311N.
IntActiP09152. 22 interactors.
MINTiMINT-1233973.
STRINGi511145.b1224.

Structurei

Secondary structure

11247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi7 – 9Combined sources3
Helixi11 – 13Combined sources3
Beta strandi14 – 18Combined sources5
Turni19 – 22Combined sources4
Beta strandi23 – 26Combined sources4
Helixi31 – 33Combined sources3
Helixi34 – 40Combined sources7
Beta strandi43 – 48Combined sources6
Beta strandi52 – 55Combined sources4
Beta strandi60 – 65Combined sources6
Beta strandi68 – 74Combined sources7
Helixi94 – 97Combined sources4
Helixi98 – 102Combined sources5
Beta strandi113 – 115Combined sources3
Helixi116 – 126Combined sources11
Helixi132 – 140Combined sources9
Helixi143 – 150Combined sources8
Turni151 – 154Combined sources4
Beta strandi158 – 160Combined sources3
Helixi163 – 180Combined sources18
Helixi183 – 185Combined sources3
Beta strandi186 – 189Combined sources4
Helixi193 – 195Combined sources3
Helixi197 – 210Combined sources14
Beta strandi213 – 215Combined sources3
Turni218 – 222Combined sources5
Helixi227 – 232Combined sources6
Helixi241 – 246Combined sources6
Beta strandi248 – 254Combined sources7
Helixi257 – 260Combined sources4
Helixi262 – 264Combined sources3
Helixi265 – 271Combined sources7
Helixi272 – 274Combined sources3
Beta strandi277 – 281Combined sources5
Helixi287 – 291Combined sources5
Beta strandi292 – 296Combined sources5
Turni300 – 302Combined sources3
Helixi303 – 318Combined sources16
Turni319 – 321Combined sources3
Helixi325 – 334Combined sources10
Beta strandi339 – 345Combined sources7
Beta strandi347 – 355Combined sources9
Helixi358 – 360Combined sources3
Beta strandi361 – 363Combined sources3
Helixi364 – 366Combined sources3
Helixi371 – 373Combined sources3
Beta strandi377 – 379Combined sources3
Helixi391 – 393Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi405 – 407Combined sources3
Turni408 – 410Combined sources3
Turni421 – 423Combined sources3
Beta strandi425 – 433Combined sources9
Beta strandi450 – 462Combined sources13
Beta strandi468 – 473Combined sources6
Helixi474 – 481Combined sources8
Beta strandi493 – 496Combined sources4
Helixi505 – 512Combined sources8
Helixi516 – 533Combined sources18
Beta strandi537 – 541Combined sources5
Helixi543 – 546Combined sources4
Helixi551 – 564Combined sources14
Beta strandi574 – 577Combined sources4
Helixi587 – 594Combined sources8
Turni595 – 599Combined sources5
Beta strandi604 – 606Combined sources3
Helixi608 – 615Combined sources8
Helixi618 – 621Combined sources4
Helixi627 – 629Combined sources3
Helixi636 – 638Combined sources3
Helixi643 – 652Combined sources10
Beta strandi662 – 664Combined sources3
Turni666 – 668Combined sources3
Helixi669 – 675Combined sources7
Helixi680 – 690Combined sources11
Beta strandi691 – 693Combined sources3
Helixi696 – 698Combined sources3
Beta strandi702 – 706Combined sources5
Beta strandi709 – 714Combined sources6
Turni717 – 721Combined sources5
Beta strandi722 – 724Combined sources3
Helixi725 – 731Combined sources7
Turni744 – 748Combined sources5
Beta strandi753 – 755Combined sources3
Beta strandi767 – 775Combined sources9
Helixi778 – 781Combined sources4
Beta strandi784 – 789Combined sources6
Beta strandi797 – 799Combined sources3
Beta strandi805 – 810Combined sources6
Beta strandi813 – 815Combined sources3
Helixi823 – 837Combined sources15
Turni838 – 841Combined sources4
Beta strandi844 – 851Combined sources8
Helixi858 – 860Combined sources3
Beta strandi864 – 866Combined sources3
Helixi870 – 872Combined sources3
Turni879 – 881Combined sources3
Beta strandi885 – 892Combined sources8
Helixi893 – 895Combined sources3
Helixi896 – 900Combined sources5
Helixi906 – 909Combined sources4
Beta strandi912 – 914Combined sources3
Beta strandi917 – 919Combined sources3
Helixi922 – 932Combined sources11
Beta strandi936 – 938Combined sources3
Turni939 – 942Combined sources4
Beta strandi943 – 945Combined sources3
Helixi949 – 959Combined sources11
Turni961 – 963Combined sources3
Helixi965 – 979Combined sources15
Helixi984 – 986Combined sources3
Helixi988 – 990Combined sources3
Helixi997 – 1002Combined sources6
Beta strandi1013 – 1015Combined sources3
Beta strandi1019 – 1021Combined sources3
Helixi1027 – 1032Combined sources6
Beta strandi1041 – 1043Combined sources3
Helixi1050 – 1054Combined sources5
Turni1072 – 1078Combined sources7
Beta strandi1085 – 1090Combined sources6
Beta strandi1095 – 1098Combined sources4
Turni1102 – 1104Combined sources3
Helixi1106 – 1111Combined sources6
Beta strandi1117 – 1121Combined sources5
Helixi1122 – 1128Combined sources7
Beta strandi1135 – 1140Combined sources6
Beta strandi1143 – 1152Combined sources10
Beta strandi1159 – 1161Combined sources3
Beta strandi1168 – 1171Combined sources4
Turni1176 – 1178Combined sources3
Beta strandi1179 – 1181Combined sources3
Helixi1185 – 1187Combined sources3
Helixi1195 – 1197Combined sources3
Beta strandi1205 – 1207Combined sources3
Turni1209 – 1211Combined sources3
Beta strandi1222 – 1227Combined sources6
Beta strandi1229 – 1231Combined sources3
Beta strandi1234 – 1238Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 1074Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST65

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

eggNOGiENOG4105CRU. Bacteria.
COG5013. LUCA.
HOGENOMiHOG000237341.
InParanoidiP09152.
KOiK00370.
OMAiWQRPPRH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti10Y → K AA sequence (PubMed:3053688).Curated1

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.
WP_000032939.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74308; AAC74308; b1224.
BAA36094; BAA36094; BAA36094.
GeneIDi945782.
KEGGiecj:JW1215.
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.
PIRiE64869. RDECNA.
RefSeqiNP_415742.1. NC_000913.3.
WP_000032939.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263271. 19 interactors.
DIPiDIP-10311N.
IntActiP09152. 22 interactors.
MINTiMINT-1233973.
STRINGi511145.b1224.

Protein family/group databases

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

Proteomic databases

PaxDbiP09152.
PRIDEiP09152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74308; AAC74308; b1224.
BAA36094; BAA36094; BAA36094.
GeneIDi945782.
KEGGiecj:JW1215.
eco:b1224.
PATRICi32117708. VBIEscCol129921_1276.

Organism-specific databases

EchoBASEiEB0632.
EcoGeneiEG10638. narG.

Phylogenomic databases

eggNOGiENOG4105CRU. Bacteria.
COG5013. LUCA.
HOGENOMiHOG000237341.
InParanoidiP09152.
KOiK00370.
OMAiWQRPPRH.
PhylomeDBiP09152.

Enzyme and pathway databases

BioCyciEcoCyc:NARG-MONOMER.
ECOL316407:JW1215-MONOMER.
MetaCyc:NARG-MONOMER.
BRENDAi1.7.5.1. 2026.
1.7.99.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP09152.
PROiP09152.

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]
ProtoNetiSearch...

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 2, 2016
This is version 178 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.