ID B4SL59_STRM5 Unreviewed; 1247 AA.
AC B4SL59;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN OrderedLocusNames=Smal_2236 {ECO:0000313|EMBL:ACF51940.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF51940.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF51940.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF51940.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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 -!- 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; CP001111; ACF51940.1; -; Genomic_DNA.
DR RefSeq; WP_012511274.1; NC_011071.1.
DR AlphaFoldDB; B4SL59; -.
DR STRING; 391008.Smal_2236; -.
DR KEGG; smt:Smal_2236; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_6; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000001867; 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:0045333; P:cellular respiration; IEA:UniProt.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1247 AA; 139911 MW; 5AC1BD4D015ED788 CRC64;
MSYFLDRLQF FKRDPQTFAD GHGFAKSEGR DWENSYRARW QYDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPLIRGTLLR
LWREARKSKA PVDAWASIVE DKEKARSYKT RRGMGGFVRL QWEEANEIIA ASNLYTVKQY
GPDRVVGFSP IPAMSMVSYA AGARYLSLLG GACLSFYDWY CDLPPASPQI WGEQTDVPES
ADWYNSRYII AWGSNVPQTR TPDAHFFTEA RYNGTKTVAI CPDYSELAKL TDHWLHPKQG
TDAALAFAFG HVILREFHVD SPSQYFQDYC RQYSDMPMLV RLERRDDGRL VAGRFLRASE
LGGLGEANNP DWKTLALDES SGQIVVPNGS IGFRWGEKGK WNIEEKESNG ADTRLRLSLA
DAHEGIEAVS FPYFGGIESE GWTAAPADDV LERNIPVRRL ALAEGGETLV ATVYDLLLAQ
YGVDRGFGGS NVASSFDDMV PGTPAWQERI TGVSRAEVIE IAREFARTAD KTHGRSMIIV
GAGMNHWFHN DMNYRGLINM LIMCGCVGQT GGGWAHYVGQ EKLRPQTGWQ PLAFGLDWSR
PPRHMNGTSF FYFNTGQWRY EKLQVDELLS PLADASKYSG SLADLNLRAV RMGWLPSAPQ
LDRNPLQLVR EAEAAGVAPA DYALGKFKDG SLDFAFADPD AQQNHPRMMF IWRSNLLGSS
GKGHEYMLRH LLGTRHGLQG KDLGEMGAVK PEEVKWRDEA PEGKLDLLVT LDFRMCTTAL
YSDIVLPTAT WYEKDDLNTS DMHPFIHPLS KAVDPAWESR SDWEIFKEVA RTVSEMAPGV
LGVEKDLVLV PTLHDTPNEL GMPFGVADWK KGECEAIPGQ TMPSMTVVER DYPNLYRKFT
SLGPLLDKLG NGGKGMSWDT KHEVEFLGKL NHTVHDAGVS QGRPAISTAI DAAEVILHLA
PETNGHVAVK AWESLGTFTG REHTHLAVGK EHEAIRFRDI QAQPRKIISS PIWSGLEDDN
VSYNAGYTNV HELIPWRTVT GRQQFYQDHE WMIDFGEAFM GYRPPVNTRT VEPLLNQRPN
GNKEIVLNWI TPHQKWGIHS TYSDNLIMQT LSRGGPIVWI SEDDARSAGI VDNDWIELFN
VNGAIAARAV VSQRVMPGMA MMYHAQERII NVPGSEISGT RGGIHNSVTR IVLKPTHMIG
GYAQLAYGFN YYGTCGTNRD EFVIVRKMDK VDWLDGEAVP AAAKEVV
//
