ID E6KSG4_9ACTO Unreviewed; 1256 AA.
AC E6KSG4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narG {ECO:0000313|EMBL:EFU61055.1};
GN ORFNames=HMPREF9006_1166 {ECO:0000313|EMBL:EFU61055.1};
OS Actinomyces sp. oral taxon 180 str. F0310.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=888052 {ECO:0000313|EMBL:EFU61055.1, ECO:0000313|Proteomes:UP000006252};
RN [1] {ECO:0000313|EMBL:EFU61055.1, ECO:0000313|Proteomes:UP000006252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0310 {ECO:0000313|EMBL:EFU61055.1,
RC ECO:0000313|Proteomes:UP000006252};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (NOV-2010) 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:EFU61055.1}.
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; AEPP01000023; EFU61055.1; -; Genomic_DNA.
DR RefSeq; WP_009212625.1; NZ_GL622194.1.
DR AlphaFoldDB; E6KSG4; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000006252; 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 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:EFU61055.1}.
FT DOMAIN 63..127
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1256 AA; 139553 MW; 1BFA05199CF194FB CRC64;
MTNLESDMTF PTYGGEVKPA TGATLFALGS WLRRGKASAD ARQLFLEGGR EGDSFYRERW
SYDKIVRSTH GVNCTGSCSW KIYVKDGVIT WETQQTDYPS TGADMPEYEP RGCPRGAAFS
WYEYSPTRIK YPYVRGVLLD MFREAKNRLG DPVDAWAAVV EDPEKARAYK SQRGRGGMVR
VTWEEAMEIV ASAYVHTIKQ YGPDRIAGFS VIPAMSMISY GAGARFHELI GATMLSFYDW
YADLPPASPQ VFGDQTDVPE AGDWFNSQYL IMWGTNLPLT RTPDAHFMAE ARYHGQKVVV
VSPDFADNTK FADDWLRVQP GTDGALAQAM GHVILKEFHV GKREPMFLDY MRRYTDSPFL
VEIGEVGEGA HEGIDPTTLV PGKFLTAAKM PEGTTERTEN NEFRPLVIEA DGTVKDPGGT
LADRFGEEGA GHWNLNLDGV EPVLSVMDTD EWEGVEIALP RFDLPAAPGQ ASIGGGYVLR
GVPVRRVNGR LVTTVYDILL AHYAVEREGL PGQWPADYMD ASTPGTPAWQ EEFTSVPAGA
AIKIGREFAA NAVETQGRSM ILMGAGTNHY YHSDEMYRTF LALTEMCGTQ GRNGGGWAHY
VGQEKVRPIM GWGSFTFALD WARPPRQMIS TGWYYMTTDQ WRYDGAPASA MANPIKSSHL
DGKQLVDTLV ESVQRGWMPC YPTFSKGSTQ LGREAAEAGM APAQYVSQEL REGRLHFAIE
DPDAHHNVPK ILANWRTNLL GSSAKGTEFF LRHMLGTGNE VNAEELDEGN RPASVNWREA
HPGKLDLMWV ADFRNTSTTL HSDVVLPAAT WYEKHDLSST DMHPFMHCFD EAVNPPWEAR
TDFEVFQTLA HLVGRLAGDH LGTQTDVVAV PLGHDSPDAM TMADGVVPEQ TWTPGKTMPK
LVPIERDYTQ VGYKFDRMGP LLAKAGLAAK GVAYNVQEAL DQLGDLNGRA PMDGNAGEGA
PLCDTAIKAA NMALRFSGTT NGSLAVQGFR TLEKRVGNEM AFLAEGDEEK KITYQDTVLQ
PRSVITSPEW SGSEHGGRRY SAFVQNVECR KPWHTLTGRP QFYVDHDWMM DMGEALPIFR
PPLDLAHIYG ERPVGDHRPG QPGQAEVAVR YLTIHNKWAI HSQYYDNPYM LTLGRGGQTV
WMSPADAEKI GVRDNEWIEA KNRNGTVSAR AVVSHRIPEG TVFMHHAQDR QINTPLNEES
GKRGGTHNSL TRIFIKPTHL AGGYAQFAYA FNYYGPTGNN RDEVTVIRRR SQEVQF
//
