SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19319

- NARZ_ECOLI

UniProt

P19319 - NARZ_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Respiratory nitrate reductase 2 alpha chain
Gene
narZ, b1468, JW1463
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and 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

Binds 1 4Fe-4S cluster per subunit By similarity.
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit By similarity.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. 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:NARZ-MONOMER.
ECOL316407:JW1463-MONOMER.
MetaCyc:NARZ-MONOMER.

Protein family/group databases

TCDBi5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 2 alpha chain (EC:1.7.99.4)
Gene namesi
Name:narZ
Ordered Locus Names:b1468, JW1463
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10648. narZ.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nitrate reductase complex Source: InterPro
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 12461245Respiratory nitrate reductase 2 alpha chain
PRO_0000063234Add
BLAST

Proteomic databases

PaxDbiP19319.
PRIDEiP19319.

Expressioni

Gene expression databases

GenevestigatoriP19319.

Interactioni

Subunit structurei

Tetramer composed of an alpha, a beta and 2 gamma chains. Alpha and beta are catalytic chains; gamma chain is involved in binding the enzyme complex to the cytoplasmic membrane.

Binary interactionsi

WithEntry#Exp.IntActNotes
narHP113494EBI-547262,EBI-555067
narJP0AF263EBI-547262,EBI-555043
narWP193173EBI-547262,EBI-555088

Protein-protein interaction databases

DIPiDIP-10324N.
IntActiP19319. 29 interactions.
MINTiMINT-1261362.
STRINGi511145.b1468.

Structurei

3D structure databases

ProteinModelPortaliP19319.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5013.
HOGENOMiHOG000237341.
KOiK00370.
OMAiVKQEPVL.
OrthoDBiEOG6RC3JS.
PhylomeDBiP19319.

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.

P19319-1 [UniParc]FASTAAdd to Basket

« Hide

MSKLLDRFRY FKQKGETFAD GHGQVMHSNR DWEDSYRQRW QFDKIVRSTH     50
GVNCTGSCSW KIYVKNGLVT WEIQQTDYPR TRPDLPNHEP RGCPRGASYS 100
WYLYSANRLK YPLIRKRLIE LWREALKQHS DPVLAWASIM NDPQKCLSYK 150
QVRGRGGFIR SNWQELNQLI AAANVWTIKT YGPDRVAGFS PIPAMSMVSY 200
AAGTRYLSLL GGTCLSFYDW YCDLPPASPM TWGEQTDVPE SADWYNSSYI 250
IAWGSNVPQT RTPDAHFFTE VRYKGTKTIA ITPDYSEVAK LCDQWLAPKQ 300
GTDSALAMAM GHVILKEFHL DNPSDYFINY CRRYSDMPML VMLEPRDDGS 350
YVPGRMIRAS DLVDGLGESN NPQWKTVAVN TAGELVVPNG SIGFRWGEKG 400
KWNLESIAAG TETELSLTLL GQHDAVAGVA FPYFGGIENP HFRSVKHNPV 450
LVRQLPVKNL TLVDGNTCPV VSVYDLVLAN YGLDRGLEDE NSAKDYAEIK 500
PYTPAWGEQI TGVPRQYIET IAREFADTAH KTHGRSMIIL GAGVNHWYHM 550
DMNYRGMINM LIFCGCVGQS GGGWAHYVGQ EKLRPQTGWL PLAFALDWNR 600
PPRQMNSTSF FYNHSSQWRY EKVSAQELLS PLADASKYSG HLIDFNVRAE 650
RMGWLPSAPQ LGRNPLGIKA EADKAGLSPT EFTAQALKSG DLRMACEQPD 700
SSSNHPRNLF VWRSNLLGSS GKGHEYMQKY LLGTESGIQG EELGASDGIK 750
PEEVEWQTAA IEGKLDLLVT LDFRMSSTCL FSDIVLPTAT WYEKDDMNTS 800
DMHPFIHPLS AAVDPAWESR SDWEIYKGIA KAFSQVCVGH LGKETDVVLQ 850
PLLHDSPAEL SQPCEVLDWR KGECDLIPGK TAPNIVAVER DYPATYERFT 900
SLGPLMDKLG NGGKGISWNT QDEIDFLGKL NYTKRDGPAQ GRPLIDTAID 950
ASEVILALAP ETNGHVAVKA WQALGEITGR EHTHLALHKE DEKIRFRDIQ 1000
AQPRKIISSP TWSGLESDHV SYNAGYTNVH ELIPWRTLSG RQQLYQDHPW 1050
MRAFGESLVA YRPPIDTRSV SEMRQIPPNG FPEKALNFLT PHQKWGIHST 1100
YSENLLMLTL SRGGPIVWIS ETDARELTIV DNDWVEVFNA NGALTARAVV 1150
SQRVPPGMTM MYHAQERIMN IPGSEVTGMR GGIHNSVTRV CPKPTHMIGG 1200
YAQLAWGFNY YGTVGSNRDE FIMIRKMKNV NWLDDEGRDQ VQEAKK 1246
Length:1,246
Mass (Da):140,227
Last modified:January 23, 2007 - v5
Checksum:iDB37433A9AB0E16E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1103 – 11031E → D in CAA34964. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17110 Genomic DNA. Translation: CAA34964.1.
U00096 Genomic DNA. Translation: AAC74550.1.
AP009048 Genomic DNA. Translation: BAA15105.1.
X94992 Genomic DNA. Translation: CAA64449.1.
PIRiG64899.
RefSeqiNP_415985.1. NC_000913.3.
YP_489733.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74550; AAC74550; b1468.
BAA15105; BAA15105; BAA15105.
GeneIDi12933903.
945999.
KEGGiecj:Y75_p1444.
eco:b1468.
PATRICi32118228. VBIEscCol129921_1534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17110 Genomic DNA. Translation: CAA34964.1 .
U00096 Genomic DNA. Translation: AAC74550.1 .
AP009048 Genomic DNA. Translation: BAA15105.1 .
X94992 Genomic DNA. Translation: CAA64449.1 .
PIRi G64899.
RefSeqi NP_415985.1. NC_000913.3.
YP_489733.1. NC_007779.1.

3D structure databases

ProteinModelPortali P19319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10324N.
IntActi P19319. 29 interactions.
MINTi MINT-1261362.
STRINGi 511145.b1468.

Protein family/group databases

TCDBi 5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbi P19319.
PRIDEi P19319.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74550 ; AAC74550 ; b1468 .
BAA15105 ; BAA15105 ; BAA15105 .
GeneIDi 12933903.
945999.
KEGGi ecj:Y75_p1444.
eco:b1468.
PATRICi 32118228. VBIEscCol129921_1534.

Organism-specific databases

EchoBASEi EB0642.
EcoGenei EG10648. narZ.

Phylogenomic databases

eggNOGi COG5013.
HOGENOMi HOG000237341.
KOi K00370.
OMAi VKQEPVL.
OrthoDBi EOG6RC3JS.
PhylomeDBi P19319.

Enzyme and pathway databases

BioCyci EcoCyc:NARZ-MONOMER.
ECOL316407:JW1463-MONOMER.
MetaCyc:NARZ-MONOMER.

Miscellaneous databases

PROi P19319.

Gene expression databases

Genevestigatori P19319.

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 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], PARTIAL PROTEIN SEQUENCE.
  2. Blasco F.
    Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. Bonnefoy V., Ratouchniak J., Blasco F., Chippaux M.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    Strain: K12.

Entry informationi

Entry nameiNARZ_ECOLI
AccessioniPrimary (citable) accession number: P19319
Secondary accession number(s): P78063
, P78154, P78155, P78156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 136 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi