ID A0A1X2DHE8_9MYCO Unreviewed; 1223 AA.
AC A0A1X2DHE8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=AWC22_08585 {ECO:0000313|EMBL:ORW87460.1};
OS Mycobacterium riyadhense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW87460.1, ECO:0000313|Proteomes:UP000193087};
RN [1] {ECO:0000313|EMBL:ORW87460.1, ECO:0000313|Proteomes:UP000193087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW87460.1,
RC ECO:0000313|Proteomes:UP000193087};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORW87460.1}.
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; LQPQ01000006; ORW87460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2DHE8; -.
DR STRING; 486698.AWC22_08585; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000193087; Unassembled WGS sequence.
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 53..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 990..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 135710 MW; 0F757F8829F838C6 CRC64;
MVDLTQNQQT AADALLRFGK YFHRGEISPD YRALHKIGGR SADDFYRDRW AHDKVVRSTH
GVNCTGSCSW KIYVKDGVIT WESQQTDYPS VGADKPEYEP RGCPRGASFS WYTYSPARVR
YPYVRGVLLE YYREAKQRLN DPVLAWADIV DDPVKSRRYK AARGKGGFVR AEWWEAAEIA
AAAHVHTIKR YGPDRVAGFS PIPAMSMVSH AVGARFISLL GGSMLSFYDW YADLPVASPQ
VFGDQTDVPE SADWFDAGYL IMWGSNVPVT RTPDAHYMTE ARYRGQKVVV VSPDYADNTK
FADEWLPARP GTDAALAMSM GHVILKEFFV DRTTPYFTDY VKKYTDLPFL VTLTQRGDDW
LPGKFLTAAD LGDTGEGASS KTVLLDAQGN PVVPNGSLGH RFTASGEGHW NLDLHGVDPM
LTLHGTGSDV MAVKLPRFDG DRPGVLTRGV PTRTIAGQRV TTVFDLLLAQ YGVHRDGLAG
EWPTGYDDAT QPYTPAWQEP ITGVPAQAVA RIAREFADNA ERSRGRSMIL MGAGTNHWFH
SDQIYRSFLT LVMLTGCQGV NGGGWAHYVG QEKCRPVTGW STLAFALDWQ RPPRQMQGTV
FWYLSTDQWR YDRFTSEAMA SPLAEGRFAG RTAADNIALA SRLGWMPSYP TFNRNPLDLA
DEAARLGKDA SAHVVDGLKS GHLSFACEDP DAPENFPRCL TVWRSNLLGS SAKGNEYFLK
HLLGTDSNVA ARDEDAVRPQ EVRWRDDAPV GKLDLLLSLD FRNTSTTLFS DIVLPAATWY
EKHDLSSTDM HPFVHAFSPA ISPPWETKTD FEAFHRIARG FSWLADKHLG KRNDIVAVPL
QHDSADATAQ PGGRVLDWKA GECEPIPGKT MPRLVVVERD YPAVGEKMAA LGPMVETVGL
TTKGVTTHPD AEVEYLRGVN GAVVSGRAVG RPSLAKDTHA AEAILALSGT TNGRLAVEGF
EALQRRTGTE LADLARENEG RRITFADTQS RPVPVNTSPE WSGSETGGRR YSPFTINTER
LKPWHTLTGR QHFYLDHDWM AELGEQLPIF RPPLDMTALF DEPVVGNKAG DGGITVRYLT
PHSKWSIHSA YQDNLYMLTL SRGGQAIWMS DVDAAKIGVK DNDWIECTNR NGVVNARAIV
SHRMPEGLVF MYHAQDKAVD VPRTEKTGKR GGIHNALTRI MIKPSHLIGG YAQQSFALNY
HGPTGNQRDE VTTIRRRSQE VEY
//
