ID A0A2A2F9R8_9GAMM Unreviewed; 884 AA.
AC A0A2A2F9R8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:PAU81698.1};
GN ORFNames=CK501_00670 {ECO:0000313|EMBL:PAU81698.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU81698.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU81698.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU81698.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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:PAU81698.1}.
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DR EMBL; NSKD01000001; PAU81698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2F9R8; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000218896; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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 GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218896}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 884 AA; 96368 MW; EF4D9BA04287579D CRC64;
MGCKTTCPYC GVGCGVDATI NGNGLDPVRG DPDHPANTGR LCVKGSALHE TLGSQGRLTR
PRIQGRDTDW DQAIQYLGTE LTRLRDERGG DSIAFYLSGQ LLTEDYYVAN KFAKGFIGTP
HVDTNSRLCM SSAVAAHKRA FGEDAVPGCY EDLELADLVV LAGANPAWNH PILYQRMQKA
GAERPERRMV VIDPRRTASR EQADLHLALR PGTDTILWNG LLVWLADSGA WDHAWVEAHC
SSPEAALEAA RESAPNPETV AERCDLAVAD VQTFYEWFAT TPRTTSFWSQ GLNQSRSGTD
RANAIINCHL ATGRIGRPGA TPFSVTGQPN AMGGREVGGL ANQLAAHMDY DTPGAREALA
HFWQAPALPE EPGHKAVALF EAIERGDIQC VWIMATNPLV SLPDPERARH ALAQCPLVIV
SDCVADTDTL ALADVALPAM GWAEKDGTVT NSERCISRQR GLIPAVGEAR PDWWIISAVA
RAMGFNAAFD YAGPAAIFRE HALVSTLSGD PKQQFNLGAL ATLSDRDYDA MTPIQWPVTP
EHPRGRERLF QDGVFATPDG HACFIPIHPK GPARGPTVTT PLRVTSGRIR DQWHTMTRTG
RAARLLQHLC EPFIEAHPDD LAAHDLADGD LAWLSNGQGR YLGRTRASDG MRPGEVFVPI
HWNHQFTTNG LASALFPRVI DPLSGQPETK HATAALLPFN ARWHARLLGG QPEQWPEGLY
WARVPMEQTT CWHLAGNSPI PDWPGTARQW LGGEPDSEMR DPRAGRYRAA WYHGDQLQAV
LLVEPGNDFP GLDWLDSLFQ AQPLDDGTRR RVLAGRDSDQ PDPGPIICSC YQVGERRIEE
ALAEGCDSVS DLGKELGCGT NCGSCVPELR QLVEQSLPEP SGDG
//
