(data stored in ACNUC7421 zone)

SWISSPROT: NAPA_PARXL

ID   NAPA_PARXL              Reviewed;         827 AA.
AC   Q13I15;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 93.
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=Bxeno_C0346; ORFNames=Bxe_C0367;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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:
CC       Reaction=2 [Fe(II)cytochrome] + 2 H(+) + nitrate = 2
CC         [Fe(III)cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909,
CC         Rhea:RHEA-COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC         Evidence={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; CP000272; ABE36274.1; -; Genomic_DNA.
DR   RefSeq; WP_011493534.1; NZ_CP008761.1.
DR   SMR; Q13I15; -.
DR   STRING; 266265.Bxe_C0367; -.
DR   PRIDE; Q13I15; -.
DR   EnsemblBacteria; ABE36274; ABE36274; Bxe_C0367.
DR   GeneID; 4009881; -.
DR   KEGG; bxb:DR64_8074; -.
DR   KEGG; bxe:Bxe_C0367; -.
DR   PATRIC; fig|266265.5.peg.8136; -.
DR   eggNOG; ENOG4107QIW; Bacteria.
DR   eggNOG; COG0243; LUCA.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; VCVKGAT; -.
DR   OrthoDB; 323168at2; -.
DR   BioCyc; BXEN266265:BXE_RS38420-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
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 transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
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   InterPro; IPR019546; TAT_signal_bac_arc.
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   TIGRFAMs; TIGR01409; TAT_signal_seq; 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;
DR   PRODOM; Q13I15.
DR   SWISS-2DPAGE; Q13I15.
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     32       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        33    827       Periplasmic nitrate reductase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT                                /FTId=PRO_0000256070.
FT   DOMAIN       37     93       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      241    245       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      260    262       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      507    508       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   REGION      717    726       Mo-bis(molybdopterin guanine
FT                                dinucleotide) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   METAL        44     44       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        47     47       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        79     79       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING      81     81       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     148    148       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     173    173       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     371    371       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     375    375       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     481    481       Mo-bis(molybdopterin guanine
FT                                dinucleotide); via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     530    530       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     557    557       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     793    793       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   BINDING     801    801       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   BINDING     818    818       Mo-bis(molybdopterin guanine
FT                                dinucleotide). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
SQ   SEQUENCE   827 AA;  92597 MW;  3B9D6FE05EE4C769 CRC64;
     MTLSRRAFIK QTAAATAASA AGVVLPGVDA LAASDSLTWS KAPCRFCGTG CGVSVGVKNG
     KVVATQGDPQ AEVNRGLNCV KGYFLSKIMY GQDRLTTPLL RMKDGKYAKD GEFAPVSWDQ
     AFDVMADHFK RTLKEKGPTA VGMFGSGQWT VWEGYAAVKL MKAGFRSNNL DPNARHCMAS
     AVTGFMRTFG MDEPMGCYDD IEQADTFVLW GSNMSEMHPI LWTRITDRRL STPTTRVVVL
     STFEHRSFDL ADQTIIFTPQ SDLAILNYIA NYIIRNGNVN RDFVNRHTVF KQGNADIGYG
     LRPDNPLQKT ARNAGDPNGS QPITFDEFAK FVSKYDAAYV TKLSGVPQNK LDQLARLYAD
     PKVKVMSFWT MGFNQHTRGT WANNMVYNLH LLTGKIATPG NSPFSLTGQP SACGTAREVG
     TFSHRLPADM VVTNPKHREE AEHIWKLPAG TIPDKPGYHA VLQNRMLRDG KLNAYWVQVN
     NNVQAAANIN GEALPGYRNP QAFVVVSDVY PTVTAVAADL ILPSAMWVEK EGAYGNAERR
     TQFWHQLVDA PAGARSDLWQ LVEFSKRFKV EEVWPADLLA KKPEYRGKTL YDVLYRNGQV
     DRFALTETDS HYRNDEAKAF GFYIQKGLFE EYASFGRGHG HDLAPFDAYH KARGLRWPVV
     NGKETRWRYK EGSDPYVKTG TGWQFYGNPD GRAVIYALPY EPPPEVPDKE YPFWLATGRV
     LEHWHSGSMT RRVPELYRAF PNAVCFMHPD DAKAMGVRRG VEVKVMSRRG YILTRVETRG
     RDKPPRGLVF VPWFDSSQLI NKVTLDATDP ISLQTDYKKC AVKIVKV
//

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