ID NAPA_WOLSU Reviewed; 928 AA. AC Q7M962; Q8GBG1; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 25-NOV-2008, entry version 38. DE RecName: Full=Periplasmic nitrate reductase; DE EC=1.7.99.4; DE Flags: Precursor; GN Name=napA; OrderedLocusNames=WS1178; OS Wolinella succinogenes. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=844; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22708814; PubMed=12823811; RX DOI=10.1046/j.1365-2958.2003.03544.x; RA Simon J., Saenger M., Schuster S.C., Gross R.; RT "Electron transport to periplasmic nitrate reductase (NapA) of RT Wolinella succinogenes is independent of a NapC protein."; RL Mol. Microbiol. 49:69-79(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSMZ 1740; RX MEDLINE=22882897; PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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 (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; AJ512686; CAD55547.1; -; Genomic_DNA. DR EMBL; BX571660; CAE10263.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_907363.1; -. DR HSSP; Q53176; 1OGY. DR GeneID; 2554883; -. DR GenomeReviews; BX571656_GR; WS1178. DR KEGG; wsu:WS1178; -. DR NMPDR; fig|273121.1.peg.1090; -. DR HOGENOM; Q7M962; -. DR BioCyc; WSUC273121:WS1178-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 33 Tat-type signal (Potential). FT CHAIN 34 928 Periplasmic nitrate reductase. FT /FTId=PRO_0000046014. FT METAL 47 47 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 50 50 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 54 54 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 82 82 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 928 AA; 104968 MW; 9D5A8D055AA6D451 CRC64; MAFSRREFLK SAAAASAASA VGMSVPSQLL AQAQEGEKGW RWDKSVCRFC GTGCGIMVAT KNDQIVAVKG DPAAPVNRGL NCIKGYFNAK IMYGADRLTD PLLRVNEKGE FDKQGKFKPV SWKKAFDVME AQFKRAYNEL GPTGIGVFGS GQYTIQEGYM AAKLIKGGFR SNNLDPNARH CMASAVAAFM ETFGIDEPAG CYDDIELTDT IITWGANMAE MHPILWARVT DKKLSNPDKV KVINLSTYTN RTSDLADIEI IFTPQTDLAI WNYIAREIVY NHPESIDMEF VKNHCIFTTG FTDIGYGMRT DIKHAKYDPK ELDIAAKERS KVLSEAEGVT LRYLGMKAGD VMEMKHNATA GNHWEITFED FKKALEPYTL DFVAKLAKGN SEESLESFKE KLQKLANLYI EKERKVVSFW TMGMNQHTRG TWVNEQSYMV HFLLGKQAKP GSGAFSLTGQ PSACGTAREV GTFSHRLPAD MVVANPKHRA VSEKIWKLPE GTLNPKMGAH YMNIMRDLED GKIKFAWIQV NNPWQNTANA NHWIKAAREM DNFIVCSDAY PGISAKVADL ILPTAMIYEK WGAYGNAERR TQHWRQQVVP VGNAMPDVWQ MAEFSKRFKL KEVWGAKKID DKLTLPDVLE KAKAMGYSPE DTLFEVLFAN SEAKSFKAKD PIGEGFENTE VFGDRRNVAG SDGEVFKGYG FFIHKYLWEE YRRFGNGHGH DLADFDTYHK VRGLKWPVVD GKETQWRFNA KYDPYARKAG SGEFAFYGDA MKELPRGDLL SPKTEEKFKL TNKAKIFFRP YMDPPEMPSS EYPLWLCTGR VLEHWHSGTM TMRVPELYRA VPEALCYMHP EDAKKLGVKQ NEAVWVESRR GKVKARVDTR GRNRTPLGLV YVPWFDEKVY INKVCLDATC PISKQTDFKK CAVKVYKA //