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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   28-MAR-2018, entry version 99.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {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       complex NapAB. Receives electrons from NapB and catalyzes the
CC       reduction of nitrate to nitrite. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: 2 ferrocytochrome + nitrate + 2 H(+) = 2
CC       ferricytochrome + nitrite. {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: Component of the periplasmic nitrate reductase NapAB
CC       complex composed of NapA and NapB. {ECO:0000255|HAMAP-
CC       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       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
DR   EMBL; BX640431; CAE37995.1; -; Genomic_DNA.
DR   RefSeq; WP_010928685.1; NC_002928.3.
DR   ProteinModelPortal; Q7W733; -.
DR   SMR; Q7W733; -.
DR   EnsemblBacteria; CAE37995; CAE37995; BPP2702.
DR   KEGG; bpa:BPP2702; -.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; TQHWRQQ; -.
DR   Proteomes; UP000001421; Chromosome.
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:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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   PANTHER; PTHR11615:SF123; PTHR11615:SF123; 1.
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                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT                                /FTId=PRO_0000045978.
FT   DOMAIN       41     97       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      214    221       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      245    249       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      264    266       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      511    512       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      721    730       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
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}.
FT   BINDING      85     85       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     152    152       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     177    177       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     181    181       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     375    375       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     379    379       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     485    485       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     534    534       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     561    561       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     797    797       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     805    805       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     822    822       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {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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