GenomeNet

Database: UniProt
Entry: A7N7J3
LinkDB: A7N7J3
Original site: A7N7J3 
ID   NAPA_VIBCB              Reviewed;         829 AA.
AC   A7N7J3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   28-MAR-2018, entry version 74.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630};
GN   OrderedLocusNames=VIBHAR_05377;
OS   Vibrio campbellii (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       complex NapAB. Receives electrons from NapB and catalyzes the
CC       reduction of nitrate to nitrite. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: 2 ferrocytochrome + nitrate + 2 H(+) = 2
CC       ferricytochrome + nitrite. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
CC       (Mo-bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01630};
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB
CC       complex composed of NapA and NapB. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
DR   EMBL; CP000790; ABU73282.1; -; Genomic_DNA.
DR   RefSeq; WP_012129052.1; NC_022270.1.
DR   ProteinModelPortal; A7N7J3; -.
DR   SMR; A7N7J3; -.
DR   STRING; 338187.VIBHAR_05377; -.
DR   EnsemblBacteria; ABU73282; ABU73282; VIBHAR_05377.
DR   GeneID; 5557405; -.
DR   KEGG; vca:M892_24490; -.
DR   KEGG; vha:VIBHAR_05377; -.
DR   PATRIC; fig|338187.25.peg.4859; -.
DR   eggNOG; ENOG4107QIW; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; ANSMGTR; -.
DR   BioCyc; VCAM338187:G1HKJ-4909-MONOMER; -.
DR   Proteomes; UP000008152; Chromosome II.
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:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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   PANTHER; PTHR11615:SF123; PTHR11615:SF123; 1.
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; SSF50692; 1.
DR   TIGRFAMs; TIGR01706; NAPA; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
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; Reference proteome; Signal; Transport.
FT   SIGNAL        1     29       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        30    829       Periplasmic nitrate reductase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT                                /FTId=PRO_1000069726.
FT   DOMAIN       41     97       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      214    221       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      245    249       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      264    266       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      510    511       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      718    727       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   METAL        48     48       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        51     51       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        55     55       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING      85     85       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     152    152       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     177    177       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     181    181       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     374    374       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     378    378       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     484    484       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     533    533       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     560    560       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     794    794       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     802    802       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     819    819       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
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
//
DBGET integrated database retrieval system