ID A0A1W2E5R1_9SPHN Unreviewed; 849 AA.
AC A0A1W2E5R1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:SMD04398.1};
GN ORFNames=SAMN06272759_12615 {ECO:0000313|EMBL:SMD04398.1};
OS Novosphingobium sp. B1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1938756 {ECO:0000313|EMBL:SMD04398.1, ECO:0000313|Proteomes:UP000192500};
RN [1] {ECO:0000313|Proteomes:UP000192500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|Proteomes:UP000192500};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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}.
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DR EMBL; FWXL01000026; SMD04398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2E5R1; -.
DR STRING; 1938756.SAMN06272759_12615; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000192500; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
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}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 849 AA; 90821 MW; 4D5A71E186FE2D9D CRC64;
MRQVRTTCAY CGVGCGIRAE VTGDRSVFIK GDPEHPANFG KLCSKGTHLG ETVGLEGRLL
HPMIGERRAG WDEALDLVAG KMRDCIELHG PDSVALYVSG QLLTEDYYVA NKLMKGFVGS
ANIDTNSRLC MASAVAAHNR AFGEDVVPVT YDDLDEADLI LLVGSNTAWC HPVIWQRIEA
AREMRGTKIV VIDPRRTETA EQADLHVPVA PDGDVALFNA LLVEMVRRGV AEEDAPPLPH
RPAAGEKGGV GPETFAALAD LVAAHSRMVT VFSMGANQSI AGTDKGNAII NLHLATGRIN
APGMGPFSMT GQPNAMGGRE VGGLANMLAC HLGFSDAERA DVAEFWQAPH LCSGPGLKAV
DLFRAVHDGR VRFLWIMATN PAVSMPDAGF VREALARCET VVVSDVIVDT DTARFAHVRL
PALAWGEKDG TVTNSERRVS RQRALFAAPG EARADWAIIA DVAKRMGFAG FDWSNAVGVF
REYAAMTALS VKHGKVLDLT DKAGISDGDY EAMVPFLWGG RHPMAGRTMR HVPVEPRTRA
ADPAFPLRLN TGRYRDQWHT MTRTGLSPTL AQHRREPLLE VHPADAEAAR IVDGALARVV
TASGKSVFRV SVTDAQTLGQ IFVPMHWSDE MASGGRGNLL PDQSVDPISG QPGFKNNACQ
IEPVASDWRA FLLSGEAITP EYLGWWSRSA VAGGWLYELA GDGAVDADVL LPAGERIEAV
DMARGMRRLA VIDRGGSLIA ALFVTRTGQL PPRDWIAGQL GQNGAALPEL LAARPSMPAP
DRGPVVCVCH GIGTNLILDA AEAGAASVAD VGRACGAGTN CGSCRPAIAR MLREWRADMT
PLKEPEVAQ
//