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Database: UniProt
Entry: A0A1H8T7R7_9PROT
LinkDB: A0A1H8T7R7_9PROT
Original site: A0A1H8T7R7_9PROT 
ID   A0A1H8T7R7_9PROT        Unreviewed;       870 AA.
AC   A0A1H8T7R7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Assimilatory nitrate reductase catalytic subunit {ECO:0000313|EMBL:SEO87199.1};
GN   ORFNames=SAMN02990966_03162 {ECO:0000313|EMBL:SEO87199.1};
OS   Rhodospirillales bacterium URHD0017.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX   NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEO87199.1, ECO:0000313|Proteomes:UP000198826};
RN   [1] {ECO:0000313|EMBL:SEO87199.1, ECO:0000313|Proteomes:UP000198826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URHD0017 {ECO:0000313|EMBL:SEO87199.1,
RC   ECO:0000313|Proteomes:UP000198826};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FODP01000006; SEO87199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8T7R7; -.
DR   STRING; 1380357.SAMN02990966_03162; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000198826; 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}.
FT   DOMAIN          1..55
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   870 AA;  93708 MW;  81DE6A0D13B72567 CRC64;
     MIRTTCPYCG VGCGLKITPD GKGGADVVGD PDHPANRGRI CSKGAALGET LSLEDRLLHP
     EVDGRHVSWD SALDTVADGF REIVTRHGPD TVAFYVSGQL LTEDYYAANK LIKGFIGTAN
     IDTNSRLCMA SSVAGHKRAF GSDTVPGLYE DFELADLVVL VGSNLAWCHP VLFQRLEAAK
     RVRPAMRIVV VDPRRTETCD IADLHLGLRP GSDVALFNAL LAELQRRGAT AKRFVDKHTV
     GMDDALIAAR ASDVGQCDLP KADLETFFDW FARTEKTVTL YSQGVNQSSA GVDKVNALIN
     CHLLTGRIGR PGMGPFSITG QPNAMGGREV GALSNTLAAH MDFALEDVGR VGRFWNTNRV
     PRKAGLKAVE LFEAVRAGRV KAVWIMATNP VASLPNADAV RAALAACELS VVSEAIRASD
     TVDACRVRLP ALAWAEKNGT VTNSERGISR QRPFLPPPGE ARQDWWIIAE VARRLGHGEA
     FAWKGVADIF REHARLSAFE NDGQRDFDIG AYADIDDSAY DSLKPFVWPA AKGSHPTTTR
     FFADGGFFHS DGRARFIATA AREPLHAPST EWPIRLNTGR VRDQWHTMTR TAKSPRLAGH
     RPEPTIELNA IDAAQRGLQD GDIAEVISAW GRAALRVHLS RALRQGEAFA PMHWTAQLSR
     AGRINAAVNP AVDPISGQPE LKHTPVEVRR VAVQWHGTIL ARRPIMLPAV TYWARIRGAG
     CHAYLLAGEQ PLASARRALS AAMRTANPGP WVDGEDALGA VISDGRLEAV MRIGKAHDET
     ARDRLAPFMA VAQLDSEQRC VLLHGGDAAD RGGEICACLG VSNASVQAAI ANGAMTLDAV
     GAVTKAGTSC GSCRPEIRAL LRAARPRQAA
//
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