ID A4S3H7_OSTLU Unreviewed; 866 AA.
AC A4S3H7;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 08-NOV-2023, entry version 97.
DE RecName: Full=Nitrate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=OSTLU_37938 {ECO:0000313|EMBL:ABO98391.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO98391.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO98391.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO98391.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC {ECO:0000256|ARBA:ARBA00003838}.
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family.
CC {ECO:0000256|ARBA:ARBA00006253}.
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DR EMBL; CP000590; ABO98391.1; -; Genomic_DNA.
DR RefSeq; XP_001420098.1; XM_001420061.1.
DR AlphaFoldDB; A4S3H7; -.
DR STRING; 436017.A4S3H7; -.
DR EnsemblPlants; ABO98391; ABO98391; OSTLU_37938.
DR GeneID; 5004252; -.
DR Gramene; ABO98391; ABO98391; OSTLU_37938.
DR KEGG; olu:OSTLU_37938; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_1_1; -.
DR OMA; KAMMPDY; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000001568; Chromosome 10.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 2.60.40.650; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00407; EUMOPTERIN.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
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:UP000001568}.
FT DOMAIN 487..564
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 598..710
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 866 AA; 96270 MW; 001E21B60F8241A1 CRC64;
MDDVDVQRAL LACDGHRGAL TRAKAEGARA DGRDLNTPDH WVARHPSLVR LTGTHPFNCE
PPLRALMEAG SVTPAELHFV RNHGAAQNIA WDAHEVRVEV SDSGKGRTYG MDALLRKPAM
TMPCLLVCAG NRRKEQNMYE KTIGFGWGAA GLSNSLWTGV PLRILLAECG VTEVTAKRRF
VCFEGPKGEL PKGKDGTYGT SIPLSKALDP AQDVMVCYAQ NGEALRPDHG FPVRLIIPGY
IGGRMIKYLT TIRVTEHPSD NFYHFRDNRI MPPGVDAAMA DKQNWWEKPE YIFNELNINS
AIASPAHDEC VPLDRERYEV KGYAYTGGGR AITRVEVSLD GGYTWRLANI RRPFAPTMYG
KHWCWIFWDL DVATVELASA KEVMCRAWDE ANNTQPRDFT WNLMGMGNNC YFRVKLSVAA
LSDRAQKYIR CEHPTEPGAL KGGWMGNEAG GWKPVIEALE AARAGEERHN DAADEAPVVA
AAPKKNVRYI TMEEVEKHNT EDDCWIVVKG KVYDVNAYLK EGLHPGGNAS ITMNAGEDTT
EDFEAVHSAK AWKQLEPFYI GDVGSAEDQA ASTAAFDRMW AGAKHIVPEN APLGLNPKKW
LQLKIENKIP LSHDSILLRL KLESDEHQCG MPVGYHVYLR GEWNGKKVMR AYTPSSLNGT
LGAVELVIKI YYSDVHEAYP EGGALTQYLH HLNEGDKIDV KGPVGHIKYL GQGLFSIDKK
DLPPVKKMTL LGGGTGVAPM LQLIVAVLAD EKDETELSFI YANKTEDDVL LKYTLDRLER
EHKGRFKVHY MISKETWAAD RKTGPEWSSD RVTYGRISLP IIQQHGFPSN GSSHIAVMCG
PPAFEEDTCI PALKALGYPE DAIIRY
//
