ID A8H064_SHEPA Unreviewed; 826 AA.
AC A8H064;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000256|HAMAP-Rule:MF_01630};
DE EC=1.9.6.1 {ECO:0000256|HAMAP-Rule:MF_01630};
GN Name=napA {ECO:0000256|HAMAP-Rule:MF_01630};
GN OrderedLocusNames=Spea_0623 {ECO:0000313|EMBL:ABV85951.1};
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV85951.1, ECO:0000313|Proteomes:UP000002608};
RN [1] {ECO:0000313|EMBL:ABV85951.1, ECO:0000313|Proteomes:UP000002608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-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 reduction
CC of nitrate to nitrite. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01630};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000256|HAMAP-Rule:MF_01630};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01630};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01630}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747, ECO:0000256|HAMAP-Rule:MF_01630}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01630}.
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DR EMBL; CP000851; ABV85951.1; -; Genomic_DNA.
DR RefSeq; WP_012153889.1; NC_009901.1.
DR AlphaFoldDB; A8H064; -.
DR STRING; 398579.Spea_0623; -.
DR KEGG; spl:Spea_0623; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000002608; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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 CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 NCBIfam; TIGR01706; NAPA; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01630};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01630};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01630};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01630};
KW Reference proteome {ECO:0000313|Proteomes:UP000002608};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01630};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01630}.
FT DOMAIN 39..95
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 83
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 150
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 175
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 179
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 212..219
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 262..264
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 372
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 376
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 482
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 508..509
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 531
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 558
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 716..725
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 792
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 800
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT BINDING 817
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
SQ SEQUENCE 826 AA; 92363 MW; 267FAC0044F32E51 CRC64;
MSISRREFLK ANAAVAAATA VGATLPVKIV EAAEQKDNIK WDKAPCRFCG VGCSVLVGTD
NGKVVATKGD PESPVNKGLN CIKGYFLSKI MYGKDRLTTP LLRMKDGQYD KEGEFTPISW
DSAFDIMADK WKNTLKTKGP TAIGMFGSGQ WTVWEGYAAS KLHKAGFLTN NIDPNARHCM
ASAVVGFMRT FGIDEPMGCY DDLEAADQFV LWGANMAEMH PILWARLSDR RLSSPTSRVH
VLSTFENRSF DLADNAMVFR PQSDLVILNY IANYIIQNDA VNKDFVNEHT TFALGTTDIG
YGLRPDHPLE KKAKNPGNGK FAPISFDEYA KFVSTYTLEY AAEMSGVEPE KLELMAKAYA
DPNVKMMSLW TMGINQHTRG VWANNMLYNI HLLTGKIATP GNSPFSLTGQ PSACGTAREV
GTFAHRLPAD MVVMNPKHRA IAEKLWQLPE GTIPPKPGFH AVLQSRMLKD GKLNCYWTMC
TNNMQAGPNI NDEMYPGFRN PENFIVVSDP YPTVTAMAAD LILPTAMWVE KEGAYGNAER
RTHMWHQQVK APEGAKSDLW QLMEFSKRFK VSEVWPAELI AKQPEVADKT LFDVLYANGV
VNKFPASDCK AELNDESDAF GFYVQKGLFE EYAQFGRGHA HDLADFDTYH ETRGLRWPVV
DGKETLRRFS KGDPYVKGDK EFDFYGKPDG KAVIFALPFE PAAEEPNEEY DLWLSTGRVL
EHWHTGSMTA RVPELYRAYP DAQIFMHPED AKARGLKRGD EVIVASPRGE VKTRVETKGR
NKPPRGVAFM PFFDARQLVN KLILDATDPL SKETDFKKCP VKVMKA
//
