ID NAPA_YERPE Reviewed; 830 AA. AC Q8ZCF3; Q0WCN0; Q74SF1; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 25-NOV-2008, entry version 46. DE RecName: Full=Periplasmic nitrate reductase; DE EC=1.7.99.4; DE Flags: Precursor; GN Name=napA; OrderedLocusNames=YPO3038, YP_2661; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX MEDLINE=21470413; PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., RA Yang H., Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL590842; CAL21640.1; -; Genomic_DNA. DR EMBL; AE017042; AAS62853.1; -; Genomic_DNA. DR PIR; AE0369; AE0369. DR RefSeq; NP_993976.1; -. DR HSSP; Q53176; 1OGY. DR SMR; Q8ZCF3; 38-827. DR GeneID; 2766408; -. DR GenomeReviews; AE017042_GR; YP_2661. DR GenomeReviews; AL590842_GR; YPO3038. DR KEGG; ype:YPO3038; -. DR KEGG; ypm:YP_2661; -. DR HOGENOM; Q8ZCF3; -. DR BioCyc; YPES214092:YPO3038-MON; -. DR BioCyc; YPES229193:YP2661-MON; -. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. 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 GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01630; -; 1. DR InterPro; IPR009010; Asp_de-COase-like_fold. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR006657; MPT_dinuc_bd. DR InterPro; IPR010051; NO3_reductase_lsu_periplasm. DR InterPro; IPR006311; Tat. DR Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 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 31 Tat-type signal (Potential). FT CHAIN 32 830 Periplasmic nitrate reductase. FT /FTId=PRO_0000046015. FT METAL 46 46 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 49 49 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 53 53 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 81 81 Iron-sulfur (4Fe-4S) (By similarity). FT CONFLICT 341 341 A -> T (in Ref. 2; AAS62853). SQ SEQUENCE 830 AA; 93226 MW; C83E1665F370EF6D CRC64; MKLSRRDFMK ANAAVAAAAA AGMTIPTVAK AVGETTNAIK WDKAPCRFCG TGCGVLVGTQ NGRIVASQGD PDSPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKDGQYD KEGDFTPISW EKAFDIMELK FKNALKEKGP TAVGMFGSGQ WTVWEGYAAL KLLKGGFRSN NLDPNARHCM ASSVVGFMRT FGMDEPMGCY DDIEEADAFV LWGSNMAEMH PVLWSRMTSR RLTNAHVRIA VLSTYEHRSF ELADNPIVFT PQTDLVIMNY IANYIIQNNA VDKDFLAQHV NFRRGATDIG YGLRPTHPLE KAAKNPGSDA SEPMSFEDFK TFVAEYTLEK AAKMSGVPED QLESLAQLYA DPKVKLVSYW TMGFNQHTRG VWANNMCYNL HLLTGKISTP GSGPFSLTGQ PSACGTAREV GTFSHRLPAD MVVTNEKHRQ IAETTWQLPA GTIPEKVGLH AVAQDRALKD GTLNAYWVMC NNNMQAGPNI NEERMPGWRD PRNFIVVSDP YPTISALSAD LILPTSMWVE KEGAYGNAER RTQFWRQQVP SPGEAKSDLW QIVEFAKRFN VEEVWPAELV NQKPEYRGKN LYEVLFANDV VSKYPLSEIP DDQLNDEARD FGFYIQKGLF EEYASFGRGH AHDLAPFDVY HQVRGLRWPV VDGKETLWRY REGFDPFVPK GEEVRFYGKP DGKAVIFALP YEPAAESPDQ EYDLWLSTGR VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARGLHR GDKVKVISRR GEVISLVETR GRNRPPRGLV YMPFFDAAQL VNNLTLDATD PLSKETDFKK CAVKLERVVA //