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Database: UniProt
Entry: B0BR28
LinkDB: B0BR28
Original site: B0BR28 
ID   NAPA_ACTPJ              Reviewed;         827 AA.
AC   B0BR28;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   14-MAY-2014, entry version 52.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=APJL_1461;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K.,
RA   Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y.,
RA   Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L.,
RA   Zhu G.-F., Wang S., Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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-bis(molybdopterin guanine
CC       dinucleotide) (Mo-bis-MGD) cofactor 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.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
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DR   EMBL; CP000687; ABY70013.1; -; Genomic_DNA.
DR   RefSeq; YP_001652457.1; NC_010278.1.
DR   ProteinModelPortal; B0BR28; -.
DR   SMR; B0BR28; 35-826.
DR   STRING; 434271.APJL_1461; -.
DR   EnsemblBacteria; ABY70013; ABY70013; APJL_1461.
DR   GeneID; 5850761; -.
DR   KEGG; apj:APJL_1461; -.
DR   PATRIC; 20752207; VBIActPle136345_1454.
DR   eggNOG; COG0243; -.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; AGKMHDS; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; APLE434271:GIX7-1480-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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     32       Tat-type signal (Potential).
FT   CHAIN        33    827       Periplasmic nitrate reductase.
FT                                /FTId=PRO_1000186349.
FT   DOMAIN       37     93       4Fe-4S Mo/W bis-MGD-type.
FT   METAL        44     44       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   827 AA;  93572 MW;  BE020AD5642AF456 CRC64;
     MELNRRDFMK ANAAMAAAAA AGMTIPVKNV YAADDGIRWD KAPCRFCGTG CSVLVGTKDG
     RVVATQGDPD AEVNRGLNCI KGYFLSKIMY GADRVQTPLL RMKDGKFHKE GDFTPVSWDQ
     AFTIMAEKVK DILKKKEPNS VGMFSSGQTT IFEGYAKVKL WKGGLRSNTI DPNARHCMAS
     AAVAFMRTFG MDEPMGCYND IEKTDAFVLW GSNMAEMHPI LWSRISDRRL SDDKVKVVVM
     STFEHRSFEL ADTPIIFKPH SDLAILNYIA NYIIQNDKVN WDFVNKHTKF KRGETDIGYG
     LRPDHPRQKA AKNAKTAGKM YDSDFEEFKK IVEPYTLEKA HEISGVPKDQ LETLAKMYAD
     PKQTLVSFWT MGFNQHVRGV WVNHMVYNVH LLTGKISTPG CGPFSLTGQP SACGTAREVG
     TFVHRLPADM VVTNPKHVEI VEKAWKLPKG TIPTVPGYPA VMQSRMLKDG KLNFLWQLCT
     NNMQGGPNIN EEIFPGWRNP ENFIVVSDPY PSVSAVAADL ILPTCMWVEK EGAYGNAERR
     TQFWRQQVKG PGESKSDLWQ IVEFSKYFKT DEVWDEALLA QMPEYRGKTL YEVLYKNGQV
     DKFDTPTNIP GYINDEAEHF GYYLQKGLFE EYAAFGRGHG HDLADFDTYH QVRGLRWPVV
     DGKETLWRYR EGFDPYVKAG EGVSFYGYPD KKAIILGVPY EEPAESPDEE YDLWLCTGRV
     LEHWHTGTMT RRVPELHRSF PNNLCWMHPD DAKARGLRHG DKVKLITRRG EIITHLDTRG
     RNKCPKGLIY TTFFDAGQLA NKLTLDATDP ISGETDYKKC AVKVVKA
//
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