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Database: UniProt
Entry: A0A080LRG5_9PROT
LinkDB: A0A080LRG5_9PROT
Original site: A0A080LRG5_9PROT 
ID   A0A080LRG5_9PROT        Unreviewed;       487 AA.
AC   A0A080LRG5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KFB70763.1};
DE            EC=1.7.99.4 {ECO:0000313|EMBL:KFB70763.1};
GN   Name=narB {ECO:0000313|EMBL:KFB70763.1};
GN   ORFNames=AW09_004124 {ECO:0000313|EMBL:KFB70763.1};
OS   Candidatus Accumulibacter phosphatis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB70763.1, ECO:0000313|Proteomes:UP000020077};
RN   [1] {ECO:0000313|EMBL:KFB70763.1, ECO:0000313|Proteomes:UP000020077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFB70763.1}.
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DR   EMBL; JDVG02000651; KFB70763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080LRG5; -.
DR   Proteomes; UP000020077; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KFB70763.1}.
FT   DOMAIN          4..63
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          163..273
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   DOMAIN          428..475
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   487 AA;  52836 MW;  09B9D5EE49592835 CRC64;
     MLQEAYANTD TAAYADLLLP ATTWGEKEGT VTNSERCITH LTPALAPPGE ARHDWQIAVD
     FARRLGARLD QPLTGKLFPY ADAEAIFNEH RESTRGRDLD ITGLSYALLD AAGPQQWPMP
     EGASRGRQRL YEDGVFATPG GRARFVQVEH QPTAESTDAA RPLSLLSGRL RDQWHGMSRT
     GSVARLFNLD DEPLLSMHPD DLQQRGLVAG DLAQVDSARG DIVVRVKSDA GLNRGSAWLP
     MHWGSQFMNS AGVNALTTSA RDPYSHQPEL KHAAVAVNKA ELPWQLVILR KAGVGELAAL
     ALLARARTLL GEFAFASVGL YGRDEPLVIF RAAHPQALPE SRLQEIDSLF GLGDEAAAIV
     YVDQRRQISK RALAPEGKLI GVRLAGETQA EVWLKEVMAD DTLDAELIRW AVAPIGKRPG
     KLPVRSRVVC KCADVTAAQI ATDIASGATL AVLQEQRKCG TFCGSCLPEL RQMISDQAQH
     ASDAAVL
//
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