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Database: UniProt/SWISS-PROT
Entry: NAPA_BORPA
LinkDB: NAPA_BORPA
Original site: NAPA_BORPA 
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   26-NOV-2014, entry version 80.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.7.99.4 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
CC       (Mo-bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01630};
CC   -!- SUBUNIT: Interacts with NapB. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
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DR   EMBL; BX640431; CAE37995.1; -; Genomic_DNA.
DR   RefSeq; NP_884918.1; NC_002928.3.
DR   RefSeq; WP_010928685.1; 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; HPKTRVA; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; BPAR257311:BPP2702-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-HAMAP.
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_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF50692; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        39    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045978.
FT   DOMAIN       41     97       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   METAL        48     48       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        51     51       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        55     55       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
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
//
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