ID H8G5A2_9PSEU Unreviewed; 1233 AA.
AC H8G5A2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SacazDRAFT_00168 {ECO:0000313|EMBL:EHY87156.1};
OS Saccharomonospora azurea NA-128.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY87156.1};
RN [1] {ECO:0000313|EMBL:EHY87156.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY87156.1};
RX PubMed=22768365; DOI=10.4056/sigs.2635833;
RA Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N.,
RA Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G.,
RA Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the soil bacterium Saccharomonospora azurea type strain
RT (NA-128(T)).";
RL Stand. Genomic Sci. 6:220-229(2012).
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; CM001466; EHY87156.1; -; Genomic_DNA.
DR RefSeq; WP_005437746.1; NZ_CM001466.1.
DR AlphaFoldDB; H8G5A2; -.
DR HOGENOM; CLU_000422_14_1_11; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000004705; 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}.
FT DOMAIN 47..111
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1233 AA; 135964 MW; 249B064E3FE567FD CRC64;
MDNELTDALV RTRRFFTRGT VSDDLRTLEH TGGRDADTFY RDRWRHDKVV RSTHGVNCTG
SCSWKVYVSD GIITWEAQQT DYPSVGPDRP EYEPRGCPRG AAFSWYTYSP TRVRYPYVRG
VLLELYRRAR QRTGDPVAAW AEIVEDPEAA RLYKSARGHG GLVRASWDEA TEIVAAAHVY
TVKQYGPDRV AGFSPIPAMS MVSYASGSRF LSLLGAPMLS FYDWYADLPV ASPQVFGDQT
DVPESGDWWD AAYLIMWGSN LPVTRTPDAH WMVEARYRGQ KVVAVSPDYA DNVKFADDWL
AIRPGTDGAL AMAMGHVVLR EFFVDRRTPA FEDYVTRFTD LPFLVRLDEH TDGHVPGKFL
TAADLSLDAA AAEADEHAAF KTVLLDSATS EPVVPNGSVG FRYGESGIGR WNLDLDGVDP
MLSASGPGSE PVTVLLPRFD GHTGHPDGDS AVAATLRRGV PARRVGGQLV TTVFDLLLAQ
YGVQRDGLPG DWPGGYDDPT TPYTPAWQES ITGVPASATT RIAREFAATA EATGGRSMII
MGAGTNHWFH SDTIYRAFLT LTMLTGGQGV NGGGWAHYVG QEKCRPITGW SNLAFGLDWS
RPARQTIQTA YWYLHTDQFR YDHSGADAHN ATTARGVLAG HTTADLLAQS ARMGWMPSAP
TFDRNPLDLA DEAERAGTDP AEYVVAELQA GRLKFACEDP DAPQNIPRVL SVWRANLLGS
SAKGNEYFLK HLLGSDSSLR AEEVPPHARP REVVWHDEAP VGKLDLLLSL DFRMTSTTLF
SDVVLPSATW YEKHDLNTTD MHPFVHSFNP AIAPPWQTRS DWAAFQAIAE TFSRLAVDHL
GTRRDVVATP LLHDTADELA TPHGIVRDWK KGECDPVPGL TMPRLTVVER DYTAIAAKMN
ALGPMLESHG ATTKGVTFSV DREVAYLREK NGMVRGGPAH GRPSLAREVD MCEAILALSG
TTNGRLATQG FRTLEERTGT RLADLAAEHA GKQITFSDTQ KAPVPVITSP EWSGSEAGGR
RYSPFTINVE RGKPWHTLTG RQHFYLDHDW MSELGENLPV FRPPLDLTAL FSDPRPGTQD
GSGLAVRYLT PHSKWSIHSE YQDNLLMLSL SRGGPTIWMS VEDAGAIGVA DNDWIEAVNR
NGVVVARAIV SHRMPRGTVY MYHAQERLID VPRAETSGKR GGIHNSLTRL LIKPTHLIGG
YAQLSFAFNY LGPTGNQRDE ITVIRRRSQE VTY
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