ID   NAPA_COLP3              Reviewed;         832 AA.
AC   Q487G4;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Periplasmic nitrate reductase;
DE            EC=1.7.99.4;
DE   Flags: Precursor;
GN   Name=napA; OrderedLocusNames=CPS_1057;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ26086.1; -; Genomic_DNA.
DR   RefSeq; YP_267801.1; -.
DR   SMR; Q487G4; 41-831.
DR   GeneID; 3520335; -.
DR   GenomeReviews; CP000083_GR; CPS_1057.
DR   KEGG; cps:CPS_1057; -.
DR   NMPDR; fig|167879.3.peg.1019; -.
DR   TIGR; CPS_1057; -.
DR   HOGENOM; Q487G4; -.
DR   OMA; Q487G4; EESYVIN.
DR   BioCyc; CPSY167879:CPS_1057-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    832       Periplasmic nitrate reductase.
FT                                /FTId=PRO_0000045982.
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   832 AA;  93469 MW;  67EC37296448C080 CRC64;
     MTINRREFIK ANAIAAAAAV AGVSVPAVAS NLITSSDITK LKWDKAACRF CGTGCSVNVG
     VMDGKVVATH GDIKSPVNKG LSCVKGYFLS KIMYGKDRLT TPLLRMTNGK YDKEGEFTPI
     SWDQAFNVMA EKANDALKKD GPEALGMFGS GQWTVQEGYA AVKLMKAGFR TNNIDPNARH
     CMASAVGGFM RTFGIDEPMG CYDDLEAADA FVLWGSNMAE MHPILWTRLT DRRLSAPHVK
     VAVLSTFEHR SFDLADNGMI FTPQTDLAIL NYIANYIIQT GRVNKDFVSK HTNFRLGETD
     IGYGLRPEHP LEQKAKNNGK TKGSSTPIDF DEYAKFVSTY TVESVSKLSG VPEHKLKELA
     EMYADPKIKV TSFWTMGFNQ HTRGVWANNL VYNIHLLTGK ISTPGNSPFS LTGQPSACGT
     AREVGTFSHR LPADMVVKNP KHRAIAEKIW DLPEGTIPAK PGYHAVLQNR MLKDGKLNFY
     WVQCNNNMQA AANINEEAYP GYRNPKNFIV VSDPYPTVTA QAADLILPTA MWVEKEGMYG
     NAERRTQSWY QMVEAPEGAK SDMWQLVEFS KRFKVEDVWP EELIAKKPEV RGKTLFDVLY
     KDASVGKFPL SEIPEDRLND ESRDFGFYIQ KGLFEEYASF GRGHAHDLAP YDRYHKERGL
     RWPVVNGKET KWRFKEGSDP YCKPGSDWDF YGKPDGRAVI FALPYEPAAE SPDEEYDLWL
     STGRVLEHWH SGSMTQRVPE LYKAMPDALV YMHPDDAKKR NMRRGDLVKL ISRRGEVQTR
     VETRGRNKPP VGLVYMPWFD ASRLVNKVTL DATDPLSKET DYKKCAIKIV KV
//