ID NAPA_BORPA Reviewed; 831 AA.
AC Q7W733;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 69.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; OrderedLocusNames=BPP2702;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC (NAP). Only expressed at high levels during aerobic growth. NapAB
CC complex receives electrons from the membrane-anchored tetraheme
CC protein NapC, thus allowing electron flow between membrane and
CC periplasm. Essential function for nitrate assimilation and may
CC have a role in anaerobic metabolism (By similarity).
CC -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC acceptor.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC -!- COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
CC -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC per subunit (By similarity).
CC -!- SUBUNIT: Interacts with NapB (By similarity).
CC -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC -!- PTM: Predicted to be exported by the Tat system. The position of
CC the signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
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DR EMBL; BX640431; CAE37995.1; -; Genomic_DNA.
DR RefSeq; NP_884918.1; NC_002928.3.
DR ProteinModelPortal; Q7W733; -.
DR SMR; Q7W733; 41-828.
DR STRING; 257311.BPP2702; -.
DR EnsemblBacteria; CAE37995; CAE37995; BPP2702.
DR GeneID; 1665471; -.
DR KEGG; bpa:BPP2702; -.
DR PATRIC; 21149320; VBIBorPar43418_2838.
DR eggNOG; COG0243; -.
DR HOGENOM; HOG000031441; -.
DR KO; K02567; -.
DR OMA; NAYWVQV; -.
DR ProtClustDB; PRK13532; -.
DR BioCyc; BPAR257311:BPP2702-MONOMER; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:HAMAP.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP.
DR GO; GO:0042128; P:nitrate assimilation; IEA:HAMAP.
DR Gene3D; 2.40.40.20; -; 1.
DR HAMAP; MF_01630; Nitrate_reduct; 1; -.
DR InterPro; IPR009010; Asp_de-COase-like_dom.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR TIGRFAMs; TIGR01706; NAPA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW Periplasm; Signal; Transport.
FT SIGNAL 1 38 Tat-type signal (Potential).
FT CHAIN 39 831 Periplasmic nitrate reductase.
FT /FTId=PRO_0000045978.
FT METAL 48 48 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 51 51 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 55 55 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 83 83 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 831 AA; 93168 MW; 7A9ED7B93B241585 CRC64;
MSMARRDFIK QTAAAAAATV AGVPLTGYTQ NIVTESEAAK LKWSKAPCRF CGTGCGVNVA
VKDNQVVATH GDFNAEVNKG LNCVKGYFLS KIMYGSDRLT QPLLRIKDGK YAKDGEFAPV
SWDQAFDVMA EQFKRVLKDK GPEAVGMFGS GQWTVWEGYA ALKLMKAGFR TNNLDPNARH
CMASAAVGFM RTFGADEPMG CYDDIENADA FVLWGSNMAE MHPILWTRVT DRRLSAPATK
VAVLSTFEHR SYELADLTLT FEPQSDLAIL NYIANHIIRT KRVNRDFVDK HTVFREGNAD
IGYGLRPEHP LQQAARNAGD AGGSKPITFD DFARFVSKYD LEYTAKLSGV PKNRLEELAE
LYADPKVRVT SFWTMGFNQH TRGVWCNNMV YNIHLLTGKI STPGNSPFSL TGQPSACGTA
REVGTFSHRL PADLVVTNPE HRRHAEEIWK LPDGTIPSKV GAHAVLQNRM LKDGKINAYW
VMVNNNMQAA ANLMNEGLPG YRNPENFIVV SDAYPTVTTL SADLILPAAM WVEKEGAYGN
AERRTQFWHQ LVDAPGQARS DLWQLVEFSK RFKVEEVWPA DLLAKKPEYR GKTLYDVLFA
NGKVNQFPNT ELDPEYANQE AQAFGFYLQK GLFEEYAEFG RGHGHDLAPF DVYHKARGLR
WPVVDGKETL WRYREGSDPY VKPGTGFQFY GNPDGKAVIF ALPYEPPPEA PDKEYPFWLS
TGRVLEHWHS GSMTRRVPEL YKAFPEAVCF MHPDDAQALG VRRGVEVEVV SRRGKMRTRV
ETRGRDKPPR GLVFVPWFDA GQLINKVTLD ATDPISFQTD FKKCAVKIVK V
//
