ID NAPA_SALCH Reviewed; 828 AA.
AC Q57M92;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 29-MAY-2013, entry version 59.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; OrderedLocusNames=SCH_2264;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y.,
RA Wang H.-S., Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a
RT highly invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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 -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
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; AE017220; AAX66170.1; -; Genomic_DNA.
DR RefSeq; YP_217251.1; NC_006905.1.
DR ProteinModelPortal; Q57M92; -.
DR SMR; Q57M92; 1-35, 37-827.
DR STRING; 321314.SC2264; -.
DR PRIDE; Q57M92; -.
DR EnsemblBacteria; AAX66170; AAX66170; SCH_2264.
DR GeneID; 3334753; -.
DR KEGG; sec:SC2264; -.
DR PATRIC; 32325491; VBISalEnt136302_2723.
DR eggNOG; COG0243; -.
DR KO; K02567; -.
DR OMA; HWIKAAR; -.
DR ProtClustDB; PRK13532; -.
DR BioCyc; SENT321314:GJCS-2366-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_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; Asp_decarb_fold; 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; 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 32 828 Periplasmic nitrate reductase.
FT /FTId=PRO_0000045999.
FT DOMAIN 39 95 4Fe-4S Mo/W bis-MGD-type.
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 828 AA; 92874 MW; 0CF99BC8B2509A85 CRC64;
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP MLRMKDGSYH KDGEFTPVSW
EQAFDVMEEK FKTSLKEKGP EAIGMFGSGQ WTIWEGYAAA KLFKAGFRSN NIDPNARHCM
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITNR RLSDPNVKVA
VLSTFQHRSF ELADNGIVFT PQSDLVILNY IANYIIQNNA VNQDFFTKHV NLRKGATDIG
YGLRPTHPLE KAAKNPGSDA SEPMSFDEYK AFVAEYTLDK TAEMTGVPKD QLEQLAQLYA
DPNKRVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
GTFSHRLPAD MVVTNEKHRD ICEKHWQIPA GTIPAKVGLH AVAQDRALKD GKLNVYWVMC
NNNMQAGPNI NEDRMPGWRD PRNFIIVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER
RTQFWRQQIK APGEAKSDLW QLVQFSRRFK TEEVWPEALL AQKPELRGKT LYDVLFATPA
VSKFPLSELK EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HNARGLRWPV
VEGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAESPDN EYDLWLSTGR
VLEHWHTGSM TRRVPELHRA FPEAVVFIHP LDAKARDLRR GDKVKVSSRR GEVISIVETR
GRNRPPQGLV YMPFFDAAQL VNNLTLDATD PLSKETDFKK CAVKLAKV
//
