ID   NAPA_SACD2              Reviewed;         831 AA.
AC   Q21PN1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=Sde_0084;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P., Weiner R.;
RT   "Complete sequence of Saccharophagus degradans 2-40.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000282; ABD79348.1; -; Genomic_DNA.
DR   RefSeq; YP_525560.1; -.
DR   SMR; Q21PN1; 43-830.
DR   GeneID; 3967323; -.
DR   GenomeReviews; CP000282_GR; Sde_0084.
DR   KEGG; sde:Sde_0084; -.
DR   NMPDR; fig|203122.1.peg.2635; -.
DR   HOGENOM; Q21PN1; -.
DR   OMA; Q21PN1; NAYWVQV.
DR   BioCyc; SDEG203122:SDE_0084-MON; -.
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; 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   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     29       Tat-type signal (Potential).
FT   CHAIN        30    831       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000256076.
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        51     51       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        55     55       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        83     83       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   831 AA;  93164 MW;  8B6EA1C70B7AF770 CRC64;
     MTVTRRDFVR HQALATAAAA AGVAVPAAAT NIVTTAADNK LVWSKAPCRF CGTGCSVNVA
     TKEGRVVATH GDIKSPVNRG LNCVKGYFLS KVMYGEDRLT QPLLRKKNGV YAKDGEFEPV
     TWEEAFTIMA EKFKKTLKEK GPEGIGMFGS GQWTVWEGYA ASKLMKAGFR SNNIDPNARH
     CMASAVGGFM RTFGIDEPMG CYDDFEHADA FVLWGSNMAE MHPILWTRIA DRRLSYPHVQ
     VAVMSTYEHR SFDLADLGVV FTPQSDLAIA NFIANYIIQN KKVNWDFVKK HTNFRVGTTD
     IGYGLRPEHP LQKAAKNADS AGASEPIDFE TYAKFVADYT VEKASEISGV SEDKLIKLAK
     LYADPNIKVM SLWTMGVNQH TRGVWMNNLI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADMVVTNPK HRAYAEKIWK LPEGSIPEKV GAHAVLQSRK LKDGEINAYW
     VQVNNNVQAG PNINEEVLPG YRNPQNFIVV SDAYPTVTAQ AADLILPSAM WVEKEGAYGN
     AERRTQFWHQ LVNAPGDARS DLWQLVEFSK YFKVEEVWPA DLIAKMPEAK GKTLFDILYK
     NGKVNKFPLA QVSKDYENKE ADAFGFYIQK GLFEEYAEFG RGHGHDLADF DRYHEERGLR
     WPVVNGEETL WRYREGSDPY VEKGKGVQFY GKPDGKAIIF ALPYEPPAES PNKEYPFWLC
     TGRVIEHWHS GSMTQRVPEL YKAFPDAVCF MHPEDARSAG LRRGDKVKLQ SIRGHIITRI
     ETRGRNKPPK GLVFVPWFDA RQLINKVTLD ATDPISKQTD FKKCAVKVER V
//