NIA1_PHAVU
ID NIA1_PHAVU Reviewed; 881 AA.
AC P39865;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Nitrate reductase [NADH] 1;
DE Short=NR-1;
DE EC=1.7.1.1;
GN Name=NIA1; Synonyms=NR1;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Saxa; TISSUE=Shoot;
RA Hoff T., Stummann B.M., Henningsen K.W.;
RT "Cloning and expression of a gene encoding a root specific nitrate
RT reductase in bean (Phaseolus vulgaris).";
RL Physiol. Plantarum 82:197-204(1991).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate;
CC Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group. The heme group is called cytochrome b-557.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; X53603; CAA37672.1; -; Genomic_DNA.
DR PIR; S25445; S25445.
DR AlphaFoldDB; P39865; -.
DR SMR; P39865; -.
DR STRING; 3885.XP_007137362.1; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001834; CBR-like.
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; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; IPR012137; Nitr_rd_NADH.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 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; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR SUPFAM; SSF81296; SSF81296; 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 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum;
KW NAD; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..881
FT /note="Nitrate reductase [NADH] 1"
FT /id="PRO_0000166067"
FT DOMAIN 515..590
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 625..737
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P49050"
FT BINDING 550
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 573
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 677..680
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 694..698
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 699
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 706
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 711..713
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 764
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 406
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 881 AA; 99223 MW; A212A1288B4EE661 CRC64;
MAASVEHRPF TSHQHGVVRS FKSYPDVPRP KKLPLPQPLS DSTNDNDEEA AVWKELVLKS
SAGVEPSIFD PRDDGTSDQW IKRNASMIRL TGKHPFNAEP PLPRLMQHGF ITPSPIHYVR
SHGPVPHARW EDWTVEVTGL VTRPTCFTME QLVNDFPSHE FPATLVCAGN RRKEQNMVKQ
SIGFNWGAGG VSTSVWRGVS LRSLLKRCGI YSRAKGALHV CFEGAEDLPG GGGSNYGTSL
MREVALDPSR DIILAYMQNG ELLSPDHGFP VRMIIPGFIG GRMVKWLKRI VVSNQQSQSH
YHYKDNKLFP SHVDAELANE EDWWYKPEYI INEVNINSVI TTPSHQEILP INSWTTQMPY
SMRGYAYSGG GRKVTRVEVT LDGGETWQVC SVERLEKPNK YGKYWCWCFW SLEVEVLDIL
GAKEIAVRAW DEAQNTQPEK LIWNTMGMIN NCWFRVKTNV CKPKKGEIGI VFEHPTQPGN
QSGGWMAREK QLEKSSESNP ILKKSVSSPF MNTATKSYSL SEVRRHNNRD SAWIIVNGHV
YDCTRFLKDH PGGEDSILLN AGTDCTEEFE AIHSDKAKKM LEDYRIGELM TTDYTSDSSS
SNNSVHGNSE TTHLAPIREV ALNPREKIPC KLLSKTSISH DVRLLRFALP AEDQVMGLPV
GNHVFLCATV DEKLCMRAYT PTSSVDEVGF FDLVVKVYFK GVHPNFPNGG IMSQHLDSLP
IGSVVDVKGP LGHIEYTGRG NFLVHGKPRF AKRLTMLAGG TGITPIYQVV QAILKDPEDR
TEMYVVYANR TEDDILLKEE LDEWAKKHDR LKVWYVLQAN IREGWEYSVG FITESILREH
VPLASPDTLA LTCGPPPMIQ FAVQPNLEKL GYDIQNDLLV F
