ID   NAPA_MANSM              Reviewed;         830 AA.
AC   Q65Q72;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=MS2281;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K.,
RA   Kim C.H., Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(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.
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DR   EMBL; AE016827; AAU38888.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_089473.1; -.
DR   SMR; Q65Q72; 38-829.
DR   GeneID; 3075593; -.
DR   GenomeReviews; AE016827_GR; MS2281.
DR   KEGG; msu:MS2281; -.
DR   NMPDR; fig|221988.1.peg.2146; -.
DR   HOGENOM; Q65Q72; -.
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:UniProtKB-KW.
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   InterPro; IPR019546; TAT_signal.
DR   InterPro; IPR017909; Twin_arg_translocation_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   Pfam; PF10518; TAT_signal; 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    830       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045991.
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).
SQ   SEQUENCE   830 AA;  93765 MW;  AF0EDF9F2472B59E CRC64;
     MELNRRDFMK ANAAVAAAAA AGITIPVKNV HAADDDMGIR WDKAPCRYCG TGCSVLVGTK
     DGRVVATQGD PDAEVNRGLN CIKGYFLSKI MYGADRVQTP LLRMKDGKFH KEGDFTPVSW
     DQAFTVMADK IKAILKEKKD PNAIGMFSSG QTTIFEGYAK VKLWKAGLRS NTIDPNARHC
     MASAAVAFLR TFGMDEPMGC YNDIEKTDAF VLWGSNMAEM HPILWSRISD RRLSSDKVKV
     VVMSTFEHRS FELADTPIIF KPHSDLAILN YIANYIIQND KVNWDFVNKH TKFKRGETDI
     GYGLRPEHPL EVAAKNRKTA GKMYDSDFEE FKKIVAPYTL EEAHRISGVP KDQLETLAKM
     YADPQQNLVS FWTMGFNQHT RGVWVNHMVY NVHLLTGKIS KPGCGPFSLT GQPSACGTAR
     EVGTFVHRLP ADMVVTNPKH VEIAENIWKL PKGTISNKPG FPAVQQSRAL KDGKLNFLWQ
     LCTNNMQGGP NINEEIFPGW RNPDNLIVVS DPYPSASAVA ADLILPTCMW VEKEGAYGNA
     ERRTQFWRQQ VKGPGQSRSD LWQIVEFSKY FKTEEVWSEE LLAQMPEYRG KTLYEVLYLN
     GEVNKFQTPT NVPGYINDEA EDFGFYLQKG LFEEYASFGR GHGHDLADFD TYHQVRGLRW
     PVVDGKETLW RYREGYDPYV KAGEEVSFYG YPDKKAIILG VPYEAPAESP DEEYDLWLCT
     GRVLEHWHTG TMTRRVPELH KAFPNNLCWM HPTDAKKRGL RHGDKVKLIT RRGEMISHLD
     TRGRNKCPEG LIYTTFFDAG QLANKLTLDA TDPISGETDY KKCAVKVVKA
//