[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / BHB2600; Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.; "Automated multiplex sequencing of the E.coli genome."; Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[2]	SEQUENCE REVISION. Robison K.; Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-757. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan] Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.; "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."; DNA Res. 3:379-392(1996).
[6]	PROTEIN SEQUENCE OF 37-43, AND SUBCELLULAR LOCATION. DOI=10.1111/j.1574-6968.1999.tb13564.x; PubMed=10234835 [NCBI, ExPASy, EBI, Israel, Japan] Thomas G., Potter L., Cole J.A.; "The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site."; FEMS Microbiol. Lett. 174:167-171(1999).

Comments

FUNCTION: Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism (By similarity).
CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit (By similarity).
SUBUNIT: Interacts with napB (By similarity).
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.
SEQUENCE CAUTION:
- Sequence=AAA16399.1; Type=Frameshift; Positions=19, 27;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00008; AAA16399.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75266.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15989.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64990; D64990.

RefSeq

AP_002802.1; -.
NP_416710.1; -.

3D structure databases

PDB

2NYA; X-ray; 2.50 A; A/F=37-828.	[ExPASy / RCSB / EBI]
2PQ4; NMR; -; B=1-35.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2NYA; -.
2PQ4; -.

ModBase

P33937.

Protein-protein interaction databases

DIP

DIP:10304N; -.

IntAct

P33937; -.

Enzyme and pathway databases

BioCyc

EcoCyc:NAPA-MON; -.
MetaCyc:NAPA-MON; -.

Organism-specific databases

EchoBASE

EB1994; -.

EcoGene

EG12067; napA.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0008940;	Molecular function: nitrate reductase activity (inferred from electronic annotation from HAMAP).
GO:0006777;	Biological process: Mo-molybdopterin cofactor biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01630; -; 1.
PBIL [Tree]

InterPro

IPR009010; Asp_de-COase-like_fold.
IPR006656; Mopterin_OxRdtase.
IPR006963; Mopterin_OxRdtase_Fe4S4.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR010051; NO3_reductase_lsu_periplasm.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.

Pfam

PF04879; Molybdop_Fe4S4; 1.
PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01706; NAPA; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; 1.
PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P33937.

Genome annotation databases

GeneID

947093; -.

GenomeReviews

U00096_GR; b2206.
AP009048_GR; JW2194.

KEGG

ecj:JW2194; -.
eco:b2206; -.

Phylogenomic databases

HOGENOM

P33937; -.

Genome annotation databases

CMR

P33937; b2206.

Other

ProtoNet

P33937.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 36`	`36`	`Tat-type signal.`
`CHAIN`	`37 828`	`792`	`Periplasmic nitrate reductase.`	`PRO_0000019170`
`METAL`	`46 46`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`49 49`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`53 53`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`81 81`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CONFLICT`	`98 98`		`T -> R (in Ref. 1; AAA16399).`
`HELIX`	`6 21`	`16`
`STRAND`	`26 29`	`4`
`STRAND`	`40 45`	`6`
`STRAND`	`47 49`	`3`
`STRAND`	`54 60`	`7`
`STRAND`	`63 69`	`7`
`TURN`	`74 78`	`5`
`HELIX`	`82 85`	`4`
`HELIX`	`86 89`	`4`
`STRAND`	`101 109`	`9`
`STRAND`	`114 117`	`4`
`HELIX`	`120 137`	`18`
`HELIX`	`140 142`	`3`
`STRAND`	`143 147`	`5`
`HELIX`	`153 164`	`12`
`TURN`	`165 167`	`3`
`STRAND`	`172 174`	`3`
`HELIX`	`175 177`	`3`
`TURN`	`178 180`	`3`
`HELIX`	`181 190`	`10`
`HELIX`	`200 205`	`6`
`STRAND`	`207 213`	`7`
`HELIX`	`216 219`	`4`
`HELIX`	`221 232`	`12`
`STRAND`	`238 246`	`9`
`HELIX`	`248 252`	`5`
`STRAND`	`254 258`	`5`
`TURN`	`261 263`	`3`
`HELIX`	`264 277`	`14`
`HELIX`	`283 289`	`7`
`STRAND`	`290 295`	`6`
`HELIX`	`308 311`	`4`
`STRAND`	`321 323`	`3`
`HELIX`	`326 334`	`9`
`HELIX`	`338 345`	`8`
`HELIX`	`349 360`	`12`
`STRAND`	`366 371`	`6`
`HELIX`	`372 375`	`4`
`HELIX`	`380 394`	`15`
`STRAND`	`402 406`	`5`
`TURN`	`411 416`	`6`
`HELIX`	`417 420`	`4`
`HELIX`	`436 446`	`11`
`HELIX`	`461 469`	`9`
`STRAND`	`475 480`	`6`
`HELIX`	`483 486`	`4`
`TURN`	`490 493`	`4`
`HELIX`	`494 499`	`6`
`STRAND`	`504 511`	`8`
`HELIX`	`514 517`	`4`
`STRAND`	`519 525`	`7`
`HELIX`	`528 530`	`3`
`STRAND`	`533 536`	`4`
`STRAND`	`540 545`	`6`
`HELIX`	`558 565`	`8`
`HELIX`	`566 568`	`3`
`HELIX`	`571 574`	`4`
`HELIX`	`577 580`	`4`
`HELIX`	`584 586`	`3`
`HELIX`	`591 595`	`5`
`TURN`	`599 602`	`4`
`HELIX`	`606 608`	`3`
`HELIX`	`616 621`	`6`
`HELIX`	`625 637`	`13`
`TURN`	`638 641`	`4`
`HELIX`	`647 650`	`4`
`STRAND`	`656 658`	`3`
`STRAND`	`667 671`	`5`
`TURN`	`672 674`	`3`
`STRAND`	`694 698`	`5`
`STRAND`	`710 712`	`3`
`STRAND`	`714 719`	`6`
`HELIX`	`731 733`	`3`
`HELIX`	`735 738`	`4`
`STRAND`	`745 747`	`3`
`HELIX`	`750 754`	`5`
`TURN`	`755 757`	`3`
`STRAND`	`763 768`	`6`
`STRAND`	`771 782`	`12`
`STRAND`	`789 793`	`5`
`HELIX`	`801 803`	`3`
`TURN`	`811 813`	`3`
`STRAND`	`821 826`	`6`

Sequence information

Length: 828 AA [This is the length of the unprocessed precursor]

Molecular weight: 93042 Da [This is the MW of the unprocessed precursor]

CRC64: CE2D7AB000FEAFCA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ 

        70         80         90        100        110        120 
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW 

       130        140        150        160        170        180 
DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM 

       190        200        210        220        230        240 
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA 

       250        260        270        280        290        300 
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG 

       310        320        330        340        350        360 
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA 

       370        380        390        400        410        420 
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV 

       430        440        450        460        470        480 
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC 

       490        500        510        520        530        540 
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER 

       550        560        570        580        590        600 
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE 

       610        620        630        640        650        660 
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV 

       670        680        690        700        710        720 
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR 

       730        740        750        760        770        780 
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR 

       790        800        810        820 
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV

P33937 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools