NAPA_SHIFL
ID NAPA_SHIFL Reviewed; 828 AA.
AC Q83QV0; Q7C0T3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=SF2290, S2420;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC of nitrate to nitrite. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC 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; Evidence={ECO:0000255|HAMAP-Rule:MF_01630};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-Rule:MF_01630};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000255|HAMAP-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 the
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_01630}.
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DR EMBL; AE005674; AAN43809.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17626.1; -; Genomic_DNA.
DR RefSeq; NP_708102.1; NC_004337.2.
DR RefSeq; WP_000778072.1; NZ_WPGW01000022.1.
DR AlphaFoldDB; Q83QV0; -.
DR SMR; Q83QV0; -.
DR STRING; 198214.SF2290; -.
DR EnsemblBacteria; AAN43809; AAN43809; SF2290.
DR EnsemblBacteria; AAP17626; AAP17626; S2420.
DR GeneID; 1026754; -.
DR GeneID; 58388753; -.
DR KEGG; sfl:SF2290; -.
DR KEGG; sfx:S2420; -.
DR PATRIC; fig|198214.7.peg.2741; -.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OMA; KIVSFWT; -.
DR OrthoDB; 323168at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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 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;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Nitrate assimilation; Oxidoreductase; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT CHAIN 32..828
FT /note="Periplasmic nitrate reductase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT /id="PRO_0000046006"
FT DOMAIN 39..95
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 83
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 150
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 175
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 179
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 212..219
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 243..247
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 262..264
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 372
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 376
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 482
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 508..509
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 531
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 558
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 718..727
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 802
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 819
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
SQ SEQUENCE 828 AA; 92987 MW; 2220AA280D52DE26 CRC64;
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW
DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNS RLSNQNVTVA
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEELL AKKPELRGKT LYEVLYATPE
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV
