ID Q1AWQ7_RUBXD Unreviewed; 1216 AA.
AC Q1AWQ7;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN OrderedLocusNames=Rxyl_1205 {ECO:0000313|EMBL:ABG04171.1};
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04171.1, ECO:0000313|Proteomes:UP000006637};
RN [1] {ECO:0000313|EMBL:ABG04171.1, ECO:0000313|Proteomes:UP000006637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC {ECO:0000313|Proteomes:UP000006637};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001854};
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000386; ABG04171.1; -; Genomic_DNA.
DR RefSeq; WP_011564189.1; NC_008148.1.
DR AlphaFoldDB; Q1AWQ7; -.
DR STRING; 266117.Rxyl_1205; -.
DR KEGG; rxy:Rxyl_1205; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR PhylomeDB; Q1AWQ7; -.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-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; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT DOMAIN 46..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1216 AA; 136518 MW; 42264CA4DF366470 CRC64;
MSEPTNPLLR GMQYLARTER RSGGHGELSA RDREWERAYR QRWQHDRVVR STHGVNCTGS
CSWKIYVKDG IITWETQQTD YPSNGPDMPE YEPRGCPRGA SFSWYTYSPL RIKYPYVRGA
LLEAYREAKG RTGDPVEAWA SVVEDPEKAR RYKAARGKGG LERASWEEAA EIIAAAHVYT
IKKYGPDRVV GFSPIPAMSM VSYSGGTRFL SLIGGVIPSF YDWYSDWPPA SPQIWGDQTD
VPESADWWNA SYLMMWGSNV PITRTPDAHF MTEARYKGQK VVVVSPDYSD HTKFADHWLP
VQPGTDGALA MAMGHVILKE FYVERQVPYF LEYAKKHTDL PMLVTLRERG GAWVPDRFLR
ATDLGDGSEN AEWKTVLLDA AGGGPVVPNG SMGFKYGEEG EGRWNLELGA TDPLLSLLGS
HEELVEVELP RFDGAGEGAA TLRRGVPARR LGGRLVTTVY DLLLAQYGVR REGLPGEWPG
GYEDPEPYTP AWQQEITGVD AGRAARIGRE FARNAERTGG RSMIIMGAGT NHWYHSDQIY
RAMLALVLLC GCQGRNGGGW AHYVGQEKVR PITGWSTVAF ALDWNRPPRH MAGTTLWYLA
TEQWRYEHMG ADELAAPTGK GRLAGMHFAD CVALSARLGW QPSYPTFDRN PLEIAEAAER
EGVGVEEYVL RELREGRLRF ACEDPGAPEN FPRVLTLWRS NLLGSSGKGH EYFLKHLLGV
PDAAVRNEET PEGLRPKEVV WRERAAEGKL DLLTTLDFRK NGSSIYSDIV LPAATWYEKH
DLSSTDLHPF VHPFNPAITP PWEAKSDWEI FKLIARVFSG LAREHLGVRK DVVAAPLLHD
TPDEISQPFG EVRDWKKGEC EPVPGRTMPK LVTVERDYGA VAEKMTALGP LVEELGVGVK
GVSWRPVPEV EEMRTKNGAV RGGPAAGRPV MERDDQVCEA ILALSGTTNG RLAVEGFRAL
ERRTGRRLAD LAEERGDDRI TFPDITAQPR KVIASPEWSG TESRRRRYSP FTINVDRRIP
WRTLTGRQQF YVDHEWMLEY GEGLPVYRLP LNLRPHLRSI GDGEAEVVVR YLTPHSKWSI
HSEYQDNLHM LILFRGGPVI WMSVEDARSI GVRDNDWVEV YNAHGVIATR AVVSHRIPQG
TAIMYHAQDR HVNVPISELS GTRGGTDNST TKIVVKPTHM IGGYAQFSFA LNYYGPAGSQ
RDELTIIRKR RREVAY
//
