ID NAPA_VIBHB Reviewed; 829 AA.
AC A7N7J3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 29-MAY-2013, entry version 44.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; OrderedLocusNames=VIBHAR_05377;
OS Vibrio harveyi (strain ATCC BAA-1116 / BB120).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=338187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA Irgon J., Wilson R.K.;
RL Submitted (AUG-2007) 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 -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
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DR EMBL; CP000790; ABU73282.1; -; Genomic_DNA.
DR RefSeq; YP_001447509.1; NC_009784.1.
DR ProteinModelPortal; A7N7J3; -.
DR SMR; A7N7J3; 41-827.
DR STRING; 338187.VIBHAR_05377; -.
DR EnsemblBacteria; ABU73282; ABU73282; VIBHAR_05377.
DR GeneID; 5557405; -.
DR KEGG; vha:VIBHAR_05377; -.
DR PATRIC; 20135202; VBIVibHar24526_4089.
DR eggNOG; COG0243; -.
DR HOGENOM; HOG000031441; -.
DR KO; K02567; -.
DR OMA; IISAPYE; -.
DR ProtClustDB; PRK13532; -.
DR BioCyc; VHAR338187:GJCH-4363-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 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 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 29 Tat-type signal (Potential).
FT CHAIN 30 829 Periplasmic nitrate reductase.
FT /FTId=PRO_1000069726.
FT DOMAIN 41 97 4Fe-4S Mo/W bis-MGD-type.
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 829 AA; 93061 MW; EEA20FAF8A4AF69E CRC64;
MKMTRRAFVK ANAAASAAAV AGITLPASAT NLIASSDQTK ITWDKAPCRF CGTGCSVLVG
TQNGKVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLT KPLLRMKDGK YSKDGDFAPV
SWDTAFDIMA EKWKASLEKK GPTSIGMFGS GQWTVMEGYA AAKMMKAGFR SNNIDPNARH
CMASAVVGFM RAFGIDEPMG CYDDFENADA FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK
VNVLSTYYHR SFELADHGYI FNPQSDLAIA NFIANYIIEN DAVNWDFVNK HTNFTQADTD
IGYGLRDDDP LQKAAKNPNS GKLTSISFEE YKKSVAPYTV EKASEISGVE KEKLIELAKQ
YADPNTKVMS LWTMGMNQHT RGVWMNNLIY NIHLLTGKIA TPGNSPFSLT GQPSACGTAR
EVGTFAHRLP ADMVVANPKH RKIAEDIWKL PEGTIPPKPG FHAVLQDRML HDGVLNCYWV
QCNNNMQAGP NINTERLPGY RNPENFIVVS DPYPTATAQA ADLVLPTAMW IEKEGAYGNA
ERRTQAWYQQ VETIGDAKSD LWQVMEFAKR FKMEEVWPEE LLAKAPEYRG KTMYDMLFKN
GQVDKFPIEE AREMNDDAHH FGYYVQKGLF EEYATFGRGH GHDLAPYDVY HTVRGLRWPV
VDGKETQWRF KEGSDPYAKA GSGWDFYGNA DGKAKIISAP YEAPPEVPNE EFDLWLCTGR
VLEHWHTGTM TRRVPELYKA VPDAVVYMHP ADAKKRNVRR GEEVLIANKR GEVRVRVETR
GRNRPPEGLV FVPFFDARIL INKLILDATD PLSKQTDFKK CPVKITKIA
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