[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 35512 / DSM 2944 / LMD 82.5 / NCCB 82005; PubMed=7639719 [NCBI, ExPASy, EBI, Israel, Japan] Berks B.C., Richardson D.J., Reilly A., Willis A.C., Ferguson S.J.; "The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha."; Biochem. J. 309:983-992(1995).
[2]	CHARACTERIZATION. STRAIN=M-6; PubMed=8119278 [NCBI, ExPASy, EBI, Israel, Japan] Berks B.C., Richardson D.J., Robinson C., Reilly A., Aplin R.T., Ferguson S.J.; "Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha."; Eur. J. Biochem. 220:117-124(1994).
[3]	CHARACTERIZATION, AND PROTEIN SEQUENCE OF 642-655 AND 699-715. STRAIN=M-6; DOI=10.1016/0014-5793(94)00445-5; PubMed=8194605 [NCBI, ExPASy, EBI, Israel, Japan] Breton J., Berks B.C., Reilly A., Thomson A.J., Ferguson S.J., Richardson D.J.; "Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase."; FEBS Lett. 345:76-80(1994).

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.
CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced acceptor.
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
COFACTOR: Binds 1 molybdenum ion per subunit.
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
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 not been experimentally proven.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

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

Z36773; CAA85346.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S50163; S50163.

3D structure databases

HSSP

P81186; 2NAP. [HSSP ENTRY / PDB]

ModBase

Q56350.

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).

Other

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

Keywords

4Fe-4S; 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 31`	`31`	`Tat-type signal (Potential).`
`CHAIN`	`32 831`	`800`	`Periplasmic nitrate reductase.`	`PRO_0000019172`
`METAL`	`48 48`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`51 51`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`55 55`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`83 83`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CONFLICT`	`128 128`		`T -> D (in Ref. 1; AA sequence).`

Sequence information

Length: 831 AA [This is the length of the unprocessed precursor]

Molecular weight: 92618 Da [This is the MW of the unprocessed precursor]

CRC64: ED78963BD2DA2144 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTISRRDLLK AQAAGIAAMA ANIPLSSQAP AVPGGVESLQ ITWSKAPCRF CGTGCGVMVG 

        70         80         90        100        110        120 
VKEGRVVATH GDLLAEVNRG LNCVKGYFLS KIMYGADRLT QPLLRKKDGV YAKDGEFTPV 

       130        140        150        160        170        180 
SWEEAFDTMA AQAKRVLRDK GPTALGMFGS GQWTIFEGYA ATKLMRAGFR SNNLDPNARH 

       190        200        210        220        230        240 
CMASAAYAFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVA DRRLGHPHVK 

       250        260        270        280        290        300 
VAVLSTFTHR SSDLADIPIV FKPGTDLAIL NYIANHIIQT GRVNRDFVDR HTTFVAGATG 

       310        320        330        340        350        360 
IGYGLRDDDP REMAARTAED PAATTPSTFE EFAELVSEYT LDKVSELSGV EPAFLEQLAE 

       370        380        390        400        410        420 
LYADPDRKVM SLWTMGFNQH VRGVWANQMV YNLHLLTGKI SEPGNSPFSL TGQASACGTA 

       430        440        450        460        470        480 
RQVGTFRHRL PSDMTVTNPE RRQDAEEIWR IPHGVIPEQP GLHAVAQDRA LHDGTLNFYW 

       490        500        510        520        530        540 
IQVNNNLQAS PNNDGEAWPG YRNPDNFIVV SDAYPTVTAL AADLILPAAM WVEKEGAYGN 

       550        560        570        580        590        600 
AERRTHVWHQ LVEAPGEARS DLWQMMEFST RFTTDEVWPE EILAANPNYR GQSLFDVLFR 

       610        620        630        640        650        660 
NGSVDRFDLS ELNPVTPTAE SNAFGFYVQK GLFEEYAPFG RGHGHDLAPY DTYHEVRGLR 

       670        680        690        700        710        720 
WPVVDGKETL WRYREGLDPY VEPGAGVQFY GNPDGKARII AVPYEPPAEP PDEEYNIWLV 

       730        740        750        760        770        780 
TGRVLEHWHS GSMTMRVPEL YRAFPGARCF MNPEDARDMG FNQGAEVRIV SRRGEIRSRV 

       790        800        810        820        830 
ETRGRNRMPR GVVFVPWFDA SQLINKVTLD ATDPISKQTD FKKCAVKILP V

Q56350 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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