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 (By similarity).
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

AE004091; AAG04563.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F83499; F83499.

RefSeq

NP_249865.1; -.

3D structure databases

HSSP

Q53176; 1OGY. [HSSP ENTRY / PDB]

SMR

Q9I4G3; 35-824.

ModBase

Q9I4G3.

Enzyme and pathway databases

BioCyc

PAER208964:PA1174-MON; -.

Organism-specific databases

PseudoCAP

PA1174; -.

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.
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.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; 1.
PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.

BLOCKS

Q9I4G3.

Genome annotation databases

878409; -.

AE004091_GR; PA1174.

pae:PA1174; -.

fig|208964.1.peg.1175; -.

Phylogenomic databases

HOGENOM

Q9I4G3; -.

Genome annotation databases

CMR

Q9I4G3; PA1174.

Other

ProtoNet

Q9I4G3.

UniRef

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

Keywords

4Fe-4S; Complete proteome; 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 24`	`24`	`Potential.`
`CHAIN`	`25 829`	`805`	`Periplasmic nitrate reductase.`	`PRO_0000045995`
`METAL`	`43 43`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`46 46`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`50 50`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`78 78`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 829 AA [This is the length of the unprocessed precursor]

Molecular weight: 92975 Da [This is the MW of the unprocessed precursor]

CRC64: 4B543C34FEDB0398 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSPRPTPPP FAAAAAGLPI LVRASNLVTE ADVTSLVWNK APCRFCGTGC SVMVATRDGQ 

        70         80         90        100        110        120 
VVATHGDIKA EVNRGINCVK GYFLSKIMYG SDRLTRPLLR MKDGKFDKQG EFQPISWEQA 

       130        140        150        160        170        180 
FDIMAEKFKA ALKAKGPESV GMFGSGQWTV WEGYAANKLF KAGLRSNNID PNARHCMASA 

       190        200        210        220        230        240 
VMGFMRSFGM DEPMGCYDDI EATDSFVLWG SNMAEMHPVL WSRVTDRRLS APQVKVAVLS 

       250        260        270        280        290        300 
TFEHRSFELA DLPMVFKPQT DLIILNYIAN HIIESGAVNR DFVERHVRFA HGAEDIGYGL 

       310        320        330        340        350        360 
RPDDPLEKKA KNADKANTWS DIDFKAFAEF VKPYTLERTA RESGVPAERL KALAELYADP 

       370        380        390        400        410        420 
KRKVVSFWTM GFNQHTRGVW ANNLIYNIHL LTGKISEPGN SPFSLTGQPS ACGTAREVGT 

       430        440        450        460        470        480 
FSHRLPADLV VTNPKHRETA EKIWKVPAGT IQEKVGFHAV QQSRMLKDGV LNVYWTQVSN 

       490        500        510        520        530        540 
NMQAGPNVMQ EVLPGWRNPD NFVIVSDVYP TVSAQAADLI LPSAMWVEKE GAFGNAERRT 

       550        560        570        580        590        600 
QFWHQLVKAP GEAKSDLWQL VEFSKRFTTD EVWPAELLAK APELKGKTLY DVLFRNGQVD 

       610        620        630        640        650        660 
RFPASDLAKG YANDEVDAFG FYIQKGLFEE YAAFGRGHGH DLAPFDAYHE ARGLRWPVVD 

       670        680        690        700        710        720 
GKETRWRYRE GYDPYVSKGS GVQFYGYPDK KAIVFALPYE PPAEAPDQDY PFWLATGRVL 

       730        740        750        760        770        780 
EHWHTGSMTA RVPELYKAVP DALVYMHPED ARQLKLRRGS EVKVVSRRGE IRARVETRGR 

       790        800        810        820 
NKPPQGLVFV PFFDANKLIN KVTLDATDPI SKQTDYKKCA VRIELLNLA

Q9I4G3 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