ID   NAPA_HAHCH              Reviewed;         830 AA.
AC   Q2SGV7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=HCH_03364;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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.
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DR   EMBL; CP000155; ABC30117.1; -; Genomic_DNA.
DR   RefSeq; YP_434542.1; -.
DR   SMR; Q2SGV7; 40-829.
DR   GeneID; 3838263; -.
DR   GenomeReviews; CP000155_GR; HCH_03364.
DR   KEGG; hch:HCH_03364; -.
DR   NMPDR; fig|349521.5.peg.2967; -.
DR   HOGENOM; Q2SGV7; -.
DR   OMA; Q2SGV7; NAYWVQV.
DR   BioCyc; HCHE349521:HCH_03364-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     30       Tat-type signal (Potential).
FT   CHAIN        31    830       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000256073.
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   830 AA;  93708 MW;  C120B7A0EC56DAB8 CRC64;
     MTTRREFIKR SAAVTAACTA GISLSGEASN VITDSEYTRL KWSKAPCRFC GTGCSVNVAV
     KDNQVVATHG DIQSEVNRGL NCVKGYFLSK IMYGKDRLTQ PLLRKKNGEY HKDGDFTPVT
     WDEAFDVMAK QFKKTLKEKG PTAVGMFGSG QWTVWEGYAA VKLYKAGFRS NNIDPNARHC
     MASAVAGFMR TFGIDEPMGC YDDIEHADAF VLWGSNMAEM HPILWTRVTD RRLSHPHVKV
     AVLSTFQHRC FDLADLPIIF TPQADLAILN YIARYIIEKD MVNWDFVNKH VRFKVGAADI
     GYGLRPEHQL ELAAANASNP GGAKDSSFEE YKNFLQQYDA QFVSKLSGAS KEKLDQLAEL
     YANPKTRVTS FWTMGFNQHT RGVWCNNLVY NLHLLTGKIS SPGNSPFSLT GQPSACGTAR
     EVGTFAHRLP ADMVVTNPKH PEFAEKTWKI PPGVIPDKPG YHAVLQNRKL RDGELNAYWV
     QVNNNVQAAP NMLEETLPGY RNPNNFIVVS EAYPTVTSQA ADLILPAAMW VEKEGAYGNA
     ERRTQFWRQL VSAPGEAKSD LWQIMEFSKR FTTDEVWPEE ILSKSPEFKG KSLFDVLFAN
     NSVNKYSIEE IDPNYKNHES EHFGFYVQKG LFEEYAIFGR GHGHDLAEFD RYHEARGLRW
     PVVDGKETLW RFREGSDPYV KKGAGYQFYG HSDGKAIIFA LPYEPPAESP DQDYPYWLVT
     GRVLEHWHSG SMTQRVPELY LAVPDALVYM HPDDARKLGV RRGDEIKVVS RRGEMRSRVE
     TRGRNKPPVG LVFVPWFDAS QLINKCTLDA TDPISKQTDF KKCAVKLIKV
//