ID C8XFL0_NAKMY Unreviewed; 1225 AA.
AC C8XFL0;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN OrderedLocusNames=Namu_3675 {ECO:0000313|EMBL:ACV79987.1};
OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV79987.1, ECO:0000313|Proteomes:UP000002218};
RN [1] {ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nakamurella multipartita DSM 44233.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV79987.1, ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RX PubMed=21304699;
RA Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Chen F.;
RT "Complete genome sequence of Nakamurella multipartita type strain (Y-
RT 104).";
RL Stand. Genomic Sci. 2:168-175(2010).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001737; ACV79987.1; -; Genomic_DNA.
DR RefSeq; WP_015748827.1; NC_013235.1.
DR AlphaFoldDB; C8XFL0; -.
DR STRING; 479431.Namu_3675; -.
DR KEGG; nml:Namu_3675; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR InParanoid; C8XFL0; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000002218; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
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 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; PS00490; MOLYBDOPTERIN_PROK_2; 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 Oxidoreductase {ECO:0000313|EMBL:ACV79987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002218}.
FT DOMAIN 51..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1225 AA; 135098 MW; 1E293BED28ADCE9B CRC64;
MNAGTDGPVA DLLLRSGRFF TTGEVSADRR TITKSGGREG DVFYRDRWSH DKVVRSTHGV
NCTGSCSWKV YVKDGIITWE TQETDYPSVG PDRPEYEPRG CPRGAAFSWY TYSPTRVRYP
YARGVLVQMF REARTRLGDP VLAWAEIQDD PERRRRYQQA RGKGGLVRVS WDEACEMIAA
AHVHTIKRYG PDRIAGFSPI PAMSMVSHAA GSRFVELMGG AMTSFYDWYA DLPVASPQVF
GDQTDVPESG DWWDASYLML WGSNVPVTRT PDAHWMAEVR YRGTKVVTVS PDYADNTKFA
DEWMPCAAGT DGALGMAMGH VILREFLVEK RTPFFVDYVR QYTDLPFLIA LEERDGAYVP
GKNLTAADLG DESEGAAFKP VLVDGRTGEV VAPHGSLGFR YTDSGVGKWN LDLAGVVPQL
TVLADPGESV PVLLTRFDTP DGRAAVLTRG VPVRRVGDRL CCTVFDLMLA QYGVHRSGLP
GSWPAGYDDA AEPYTPAWQE PITGVSAAQA IRVAREFARN AEESGGRSMI IMGAGICQWF
HGDATYRAIL AMLILTGSMG RNGGGWAHYV GQEKCRPITG WATMAMASDW VRPPRQMIGT
GYWYAHTDQW RYDGYRADAL ASPLGRGRFA GMHTMDVLAA SVAMGWMPFF PQFDRSSLDL
ADEAAAAGVP APQYVAAQLA SGQLKLAVTD PDDPGNWPRV LTAWRANLLG SSSKGNEYFL
RHLLGTTSNL RADPTPEPLR PRDVTWVDRT PAGKLDLMLS LDFRMTSTTL LSDVVLPAAT
WYEKADLSST DMHPYVHAFS PAIDPPWETR SDFDAFHTIA RVFSRLAATH LGVRQDVVMT
PLQHDTPGET AYPHGTQRDW RATGEVPVPG RTMGQIAVVT RDYPALAQQW ETLGPLVDTL
GVTTKAVTVI PDREVGELAA RHGVMDHGAG AGRPAIDTAV KMADTILALA GTTNGRLAVE
GFRQLERRTG RPLVHLAEGS EEKRISYADT AARPVPVITS PEWSGSETGG RRYAPFTVNV
EELKPWHTLT GRMHFYVDHD WMEELGEQLP VFRPPLDIQG LFGEPRIGDT TEGLGLCVRY
LTPHSKWSIH SEYQDNLFML SLSRGGPTMW ISGADAAKIG VADNDWVEAV NRNGVMVLRA
IVSHRMPEGV VYVHHAQERT IDMPLTETTG TRGGIHNSLT RLLVKPTHLA GGYAQMSFAF
NYLGPTGNQR DEVTMVRRRS QEVQY
//
