ID   NIA_VOLCA               Reviewed;         864 AA.
AC   P36841;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-NOV-2008, entry version 62.
DE   RecName: Full=Nitrate reductase [NADH];
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=NITA;
OS   Volvox carteri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=f. Nagariensis / HK10;
RX   MEDLINE=93013022; PubMed=1398126; DOI=10.1016/0378-1119(92)90011-D;
RA   Gruber H., Goetinck S.D., Kirk D.L., Schmitt R.;
RT   "The nitrate reductase-encoding gene of Volvox carteri: map location,
RT   sequence and induction kinetics.";
RL   Gene 120:75-83(1992).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first
CC       step of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY: Nitrite + NAD(+) + H(2)O = nitrate + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- COFACTOR: Binds 1 heme group per subunit.
CC   -!- COFACTOR: Binds 1 molybdenum-pterin group per subunit.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- INDUCTION: By nitrate.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; X64136; CAA45497.1; -; Genomic_DNA.
DR   PIR; JC1422; JC1422.
DR   HSSP; P04166; 1B5M.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
DR   Gene3D; G3DSA:3.90.420.10; Oxred_molyb_bd; 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   PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   PRINTS; PR00371; FPNCR.
DR   ProDom; PD000612; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    864       Nitrate reductase [NADH].
FT                                /FTId=PRO_0000166074.
FT   DOMAIN      497    572       Cytochrome b5 heme-binding.
FT   DOMAIN      606    718       FAD-binding FR-type.
FT   METAL       139    139       Molybdenum-pterin (Potential).
FT   METAL       193    193       Molybdenum-pterin (Potential).
FT   METAL       532    532       Iron (heme axial ligand) (By similarity).
FT   METAL       555    555       Iron (heme axial ligand) (By similarity).
FT   DISULFID    376    376       Interchain (Potential).
SQ   SEQUENCE   864 AA;  96402 MW;  499529652CDDD1C7 CRC64;
     MTIPELPLGG IVSQAVELGA PYEPPLTPDH PEWKVHVPAA AVDKKDQDTP DNWVRRDPRI
     LRLTGRHPLN CEPPMDVLME YGFITPPAVH FVRNHGAAPR IPWAEHRIEI NGLVDKPLFL
     TMDELVALPS ITFPCTLVCA GNRRKEENML KKSIGFNWGP CATSTTYWTG VRLRDLLLLA
     GIKSPEQGAN FVCFRGPKGE LPRGSDGSYG TSLTYAKAMD PSSDVIIAYK QNHRWLTPDH
     GFPVRMIIPG FIGGRMVKWL SEITVTEVES QNFYHFMDNR VLPSHVDEAL AKEEGWWYKP
     EFIINDLNIN SAVARPWHDE VVRLDANKPY TMRGYAYAGG GRKIIRCEVS LDDGKTWRLG
     DIQRFEKPNE YGKYWCWVHW SLDVMTFDFL NAKEVLLRAW DETMNTQPAI ITWNVMGMMN
     NCYYRIKIHP QVDSDGVMGL RFQHPAPVEL GERGNMGWRE EDNLVAQALA AVKEGATAAA
     APAAPPPVVA AAANGGPRQY TMEEVAAHNT EESCWFVHGG KVYDATPYLD EHPGGAESIL
     IVAGADATDE FNSIHSSKAK AMLAQYYIGD LVASKPAAAG ATVPEPQPVA STSSPAVDPL
     VVLNPRQKVK LPLIERIELN RNTRIFRFGL PSPQHRIGLP VGKHVFTYAT INGENVMRAY
     TPISGDEELG RLDMLIKVYF ANEHPAFPDG GKMSQHFESL RIGDTVEFKG PLGHFVYDGR
     GSYTLNGKLH KHATHMSFVA GGTGITPCYA VIKAALRDPE DKTQISLVFA NNTEEDILLR
     EELDELANNH PDRFHLWHTV SQTNSSDWKF STGRVTLEMF KQHLFACSGP ECLALMCGPP
     AMLEHCCVPF LESMGYSKEQ MIHF
//