ID A0A1H5TF19_9EURY Unreviewed; 1028 AA.
AC A0A1H5TF19;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SAMN04488133_0242 {ECO:0000313|EMBL:SEF60617.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEF60617.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEF60617.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEF60617.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FNVN01000001; SEF60617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5TF19; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; -; 5.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR03479; DMSO_red_II_alp; 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; PS51318; TAT; 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:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000236740};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 78..142
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 957..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 115397 MW; 6C9DBE6ADC489A3D CRC64;
MSDSHDFHDD SESTTGGIDA ARRDFLKGIG LGAVLGLGGV SVADRQLDMD GLEVVDDPIG
SYAYRDWEDL YREEWDWDST ARSTHSVNCT GSCSWEVYVR NGQVWRESQA GDYPQFDESL
PDPNPRGCQK GACYSDYVNA DHRVLHPLRR TGERGEGMWE RISWDEALTE IAEEVVDTVR
AGEYDAISGF TPIPAMSPVS FASGSRLINL LGGVSHSFYD WYSDLPPGQP ITWGTQTDNA
ESADWYNADY IIAWGSNVNV TRIPDAKYFL EAAYNGTKRV GVFTDYSQTA IHCDEWLSPE
PGTDTALALG MARTIVDEGL HDEAHLKEQT DMPLLVREDT GKFLRASEVS GVGGGADDPE
KVFVMRDASG NLRAAPGSLG DRDGQHDASA SIELGFDPQL SAEGSVSTTD SGQVSVRTVW
DNLREELATY TPEHVNEVTG VGRETHQEVA REFAEVDRAK IIHGKGVNDW YHNDLGNRAI
QLLVTLTGNL GRQGTGLDHY VGQEKIWTYS GWQSLSFPTG SVRGVPTTLW TYYHSDIIDN
VDEETADRIR EAIDRDWMPV YPEERDDGSR PDPSVLFMWR GNYFNQSKGN VAIEERLWPK
LDLIVDINFR MDSSALYSDI VLPTASHYEK HDLSMTDMHS YVHPFTPAVE PLGESKTDWQ
IFRELAAKIQ EVATERGIDP IEDRSFDREI DLQSVHDDYV RDWETGEAGA LAEDRAACEY
ILENSEETNP SDSDERITFE DIDEQPRRFP KAGDHWTSDI EDGEAYTPWQ SYVQDKEPWP
TFTGRQQYYI DHDWFLDLGE ELPTHKDAPT LQDKSEYPLR YNTPHGRWSI HSTWRDSEKM
LRLQRGEPIV YLNPEDMDER GIEDGDTVRI YNDVGEVEIQ AKRYPSGEPG TARMYFAWER
FQFPDRNNFN SLVSMYMKPT QLVQYPEDTG EHLHFFPNYW GPTGVNSDVR VEVEKVADAD
QEGSGSDERI DGAPTDAETA GTESVDGEPA DTAGDEPEAD LTVGTDGGPG GRSDAAWDTA
DDPGGERR
//