UniProtKB - P09152 (NARG_ECOLI)
Protein
Respiratory nitrate reductase 1 alpha chain
Gene
narG
Organism
Escherichia coli (strain K12)
Status
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
- EC:1.7.5.1
Cofactori
Protein has several cofactor binding sites:- [4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster per subunit.
- Mo-bis(molybdopterin guanine dinucleotide)Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 50 | Iron-sulfur (4Fe-4S); via pros nitrogen | 1 | |
Metal bindingi | 54 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 58 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 93 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 223 | Molybdenum | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: EcoCyc
- electron transfer activity Source: EcoCyc
- metal ion binding Source: UniProtKB-KW
- 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
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Electron transport, Nitrate assimilation, Transport |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum |
Enzyme and pathway databases
BioCyci | EcoCyc:NARG-MONOMER MetaCyc:NARG-MONOMER |
BRENDAi | 1.7.5.1, 2026 1.7.99.4, 2026 |
Protein family/group databases
TCDBi | 5.A.3.1.1, the prokaryotic molybdopterin-containing oxidoreductase (pmo) family |
Names & Taxonomyi
Protein namesi | Recommended name: Respiratory nitrate reductase 1 alpha chain (EC:1.7.5.1)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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
Plasma Membrane
- intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
- NarGHI complex Source: EcoCyc
Other locations
- intrinsic component of membrane Source: EcoCyc
- membrane Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 50 | H → S: Loss of activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB07349, (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE DB04464, N-Formylmethionine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000063233 | 2 – 1247 | Respiratory nitrate reductase 1 alpha chainAdd BLAST | 1246 |
Proteomic databases
jPOSTi | P09152 |
PaxDbi | P09152 |
PRIDEi | P09152 |
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 PublicationsBinary interactionsi
Hide detailsP09152
With | #Exp. | IntAct |
---|---|---|
narH [P11349] | 13 | EBI-547248,EBI-555067 |
narJ [P0AF26] | 18 | EBI-547248,EBI-555043 |
narW [P19317] | 9 | EBI-547248,EBI-555088 |
narY [P19318] | 5 | EBI-547248,EBI-555059 |
Protein-protein interaction databases
BioGRIDi | 4263271, 68 interactors 850149, 5 interactors |
ComplexPortali | CPX-1974, Nitrate reductase A complex |
DIPi | DIP-10311N |
IntActi | P09152, 23 interactors |
MINTi | P09152 |
STRINGi | 511145.b1224 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P09152 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09152 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 43 – 107 | 4Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST | 65 |
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
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.Curated
Phylogenomic databases
eggNOGi | COG5013, Bacteria |
HOGENOMi | CLU_000422_14_1_6 |
InParanoidi | P09152 |
PhylomeDBi | P09152 |
Family and domain databases
CDDi | cd02776, MopB_CT_Nitrate-R-NarG-like, 1 hit |
InterProi | View protein in InterPro IPR009010, Asp_de-COase-like_dom_sf IPR037943, MopB_CT_Nitrate-R-NarG-like 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 |
Pfami | View protein in Pfam PF00384, Molybdopterin, 1 hit PF01568, Molydop_binding, 1 hit PF14710, Nitr_red_alph_N, 1 hit |
SMARTi | View protein in SMART SM00926, Molybdop_Fe4S4, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit |
TIGRFAMsi | TIGR01580, narG, 1 hit |
PROSITEi | View protein in PROSITE 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P09152-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 10 | Y → K AA sequence (PubMed:3053688).Curated | 1 |
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 WP_000032939.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC74308; AAC74308; b1224 BAA36094; BAA36094; BAA36094 |
GeneIDi | 57731990 945782 |
KEGGi | ecj:JW1215 eco:b1224 |
PATRICi | fig|1411691.4.peg.1057 |
Similar proteinsi
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 WP_000032939.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P09152 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263271, 68 interactors 850149, 5 interactors |
ComplexPortali | CPX-1974, Nitrate reductase A complex |
DIPi | DIP-10311N |
IntActi | P09152, 23 interactors |
MINTi | P09152 |
STRINGi | 511145.b1224 |
Chemistry databases
DrugBanki | DB07349, (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE DB04464, N-Formylmethionine |
Protein family/group databases
TCDBi | 5.A.3.1.1, the prokaryotic molybdopterin-containing oxidoreductase (pmo) family |
Proteomic databases
jPOSTi | P09152 |
PaxDbi | P09152 |
PRIDEi | P09152 |
Genome annotation databases
EnsemblBacteriai | AAC74308; AAC74308; b1224 BAA36094; BAA36094; BAA36094 |
GeneIDi | 57731990 945782 |
KEGGi | ecj:JW1215 eco:b1224 |
PATRICi | fig|1411691.4.peg.1057 |
Organism-specific databases
EchoBASEi | EB0632 |
Phylogenomic databases
eggNOGi | COG5013, Bacteria |
HOGENOMi | CLU_000422_14_1_6 |
InParanoidi | P09152 |
PhylomeDBi | P09152 |
Enzyme and pathway databases
BioCyci | EcoCyc:NARG-MONOMER MetaCyc:NARG-MONOMER |
BRENDAi | 1.7.5.1, 2026 1.7.99.4, 2026 |
Miscellaneous databases
EvolutionaryTracei | P09152 |
PROi | PR:P09152 |
Family and domain databases
CDDi | cd02776, MopB_CT_Nitrate-R-NarG-like, 1 hit |
InterProi | View protein in InterPro IPR009010, Asp_de-COase-like_dom_sf IPR037943, MopB_CT_Nitrate-R-NarG-like 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 |
Pfami | View protein in Pfam PF00384, Molybdopterin, 1 hit PF01568, Molydop_binding, 1 hit PF14710, Nitr_red_alph_N, 1 hit |
SMARTi | View protein in SMART SM00926, Molybdop_Fe4S4, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit |
TIGRFAMsi | TIGR01580, narG, 1 hit |
PROSITEi | View protein in PROSITE 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NARG_ECOLI | |
Accessioni | P09152Primary (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: | April 7, 2021 | |
This is version 207 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families