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 01-MAY-2013, entry version 45.
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 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; 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; HWIKAAR; -.
DR ProtClustDB; PRK13532; -.
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-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 32 Tat-type signal (Potential).
FT CHAIN 33 827 Periplasmic nitrate reductase.
FT /FTId=PRO_1000186349.
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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