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Database: UniProt
Entry: A0A1H5TF19_9EURY
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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
//
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