NIA_PICAN
ID NIA_PICAN Reviewed; 859 AA.
AC P49050;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Nitrate reductase [NADPH];
DE Short=NR;
DE EC=1.7.1.3;
GN Name=YNR1;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL
RC Y-1798 / VKM Y-1397;
RX PubMed=7789531; DOI=10.1016/0014-5793(95)00511-7;
RA Avila J., Perez M.D., Brito N., Gonzalez C., Siverio J.M.;
RT "Cloning and disruption of the YNR1 gene encoding the nitrate reductase
RT apoenzyme of the yeast Hansenula polymorpha.";
RL FEBS Lett. 366:137-142(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-478 IN COMPLEX WITH
RP MO-MOLYBDOPTERIN, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=15772287; DOI=10.1105/tpc.104.029694;
RA Fischer K., Barbier G.G., Hecht H.J., Mendel R.R., Campbell W.H.,
RA Schwarz G.;
RT "Structural basis of eukaryotic nitrate reduction: crystal structures of
RT the nitrate reductase active site.";
RL Plant Cell 17:1167-1179(2005).
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 + NADP(+) + nitrite = H(+) + NADPH + nitrate;
CC Xref=Rhea:RHEA:19061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.7.1.3;
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;
CC Evidence={ECO:0000269|PubMed:15772287};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:15772287};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15772287}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; Z49110; CAA88925.1; -; Genomic_DNA.
DR PIR; S65938; S65938.
DR PDB; 2BIH; X-ray; 2.60 A; A=19-478.
DR PDB; 2BII; X-ray; 1.70 A; A/B=59-478.
DR PDBsum; 2BIH; -.
DR PDBsum; 2BII; -.
DR AlphaFoldDB; P49050; -.
DR SMR; P49050; -.
DR BRENDA; 1.7.1.3; 2587.
DR EvolutionaryTrace; P49050; -.
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; IDA:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW Molybdenum; NADP; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..859
FT /note="Nitrate reductase [NADPH]"
FT /id="PRO_0000166044"
FT DOMAIN 502..578
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 602..713
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 137
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:15772287,
FT ECO:0007744|PDB:2BII"
FT BINDING 538
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 561
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 655..658
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 672..676
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 677
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 687..689
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 737
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 740
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 829..838
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 383
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2BIH"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2BIH"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2BIH"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:2BII"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:2BII"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2BII"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:2BII"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:2BII"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2BIH"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:2BII"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:2BII"
SQ SEQUENCE 859 AA; 98534 MW; 79569977B01E3967 CRC64;
MDSIVTEVTY GLEIKKIKDI TELPFPVRQD SPLTEVLPTD LKTKDNFVAR DPDLLRLTGS
HPFNSEPPLT KLYDSGFLTP VSLHFVRNHG PVPYVPDENI LDWEVSIEGM VETPYKIKLS
DIMEQFDIYS TPVTMVCAGN RRKEQNMVKK GAGFNWGAAG TSTSLWTGCM LGDVIGKARP
SKRARFVWME GADNPANGAY RTCIRLSWCM DPERCIMIAY QQNGEWLHPD HGKPLRVVIP
GVIGGRSVKW LKKLVVSDRP SENWYHYFDN RVLPTMVTPE MAKSDDRWWK DERYAIYDLN
LQTIICKPEN QQVIKISEDE YEIAGFGYNG GGVRIGRIEV SLDKGKSWKL ADIDYPEDRY
REAGYFRLFG GLVNVCDRMS CLCWCFWKLK VPLSELARSK DILIRGMDER MMVQPRTMYW
NVTSMLNNWW YRVAIIREGE SLRFEHPVVA NKPGGWMDRV KAEGGDILDN NWGEVDDTVK
QAERRPHIDE DLEMMCNREK MDVVIKYSEF EAHKDSETEP WFAVKGQVFD GSSYLEDHPG
GAQSILMVSG EDATDDFIAI HSSFAKKLLP SMHLGRLEEV SSVTKVKSVE QNVKREVLLD
PRKWHKITLA EKEVISSDSR IFKFDLEHSE QLSGLPTGKH LFLRLKDSSG KYVMRAYTPK
SSNSLRGRLE ILIKVYFPNR EYPNGGIMTN LIENLQVGNQ IEVKGPVGEF EYVKCGHCSF
NNKPYQMKHF VMISGGSGIT PTYQVLQAIF SDPEDRTSVQ LFFGNKKVDD ILLREELDHI
QEKYPEQFKV DYSLSDLDHL PENWSGVRGR LTFDILDTYV RGKKMGEYML LVCGPPGMNG
VVENWCNARK LDKQYVVYF
