NCPR_YEAST
ID NCPR_YEAST Reviewed; 691 AA.
AC P16603; D3DKZ0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
GN Name=NCP1 {ECO:0000255|HAMAP-Rule:MF_03212}; Synonyms=CPR1, NCPR1, PRD1;
GN OrderedLocusNames=YHR042W {ECO:0000312|SGD:S000001084};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13 AND 45-62.
RX PubMed=3139648; DOI=10.1093/oxfordjournals.jbchem.a122370;
RA Yabusaki Y., Murakami H., Ohkawa H.;
RT "Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450
RT reductase deduced from nucleotide sequence of its cloned gene.";
RL J. Biochem. 103:1004-1010(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=1730736; DOI=10.1016/s0021-9258(18)46051-6;
RA Turi T.G., Loper J.C.;
RT "Multiple regulatory elements control expression of the gene encoding the
RT Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase
RT (ERG11).";
RL J. Biol. Chem. 267:2046-2056(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9368374; DOI=10.1111/j.1574-6968.1997.tb12720.x;
RA Lesuisse E., Casteras-Simon M., Labbe P.;
RT "Cytochrome P-450 reductase is responsible for the ferrireductase activity
RT associated with isolated plasma membranes of Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 156:147-152(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=9468503; DOI=10.1074/jbc.273.8.4492;
RA Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.;
RT "The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP)
RT oxidoreductase is not required for catalytic activity in sterol
RT biosynthesis or in reconstitution of CYP activity.";
RL J. Biol. Chem. 273:4492-4496(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TOPOLOGY.
RX PubMed=11485306; DOI=10.1006/bbrc.2001.5338;
RA Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.;
RT "Activities and kinetic mechanisms of native and soluble NADPH-cytochrome
RT P450 reductase.";
RL Biochem. Biophys. Res. Commun. 286:48-54(2001).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [13]
RP PHOSPHORYLATION, AND INTERACTION WITH PCL1.
RX PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
RA Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
RT "The identification of Pcl1-interacting proteins that genetically interact
RT with Cla4 may indicate a link between G1 progression and mitotic exit.";
RL Genetics 166:1177-1186(2004).
RN [14]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [15]
RP FMN-BINDING AND FAD-BINDING.
RX PubMed=20557022; DOI=10.1021/cb100055v;
RA Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.;
RT "FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the
RT surface is highly specific.";
RL ACS Chem. Biol. 5:767-776(2010).
RN [16]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN
RP AND NADP.
RX PubMed=16407065; DOI=10.1016/j.str.2005.09.015;
RA Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I.,
RA Kelly S.L., Waterman M.R., Podust L.M.;
RT "A second FMN binding site in yeast NADPH-cytochrome P450 reductase
RT suggests a mechanism of electron transfer by diflavin reductases.";
RL Structure 14:51-61(2006).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 44-211 IN COMPLEX WITH FMN.
RX PubMed=19483672; DOI=10.1038/embor.2009.82;
RA Aigrain L., Pompon D., Morera S., Truan G.;
RT "Structure of the open conformation of a functional chimeric NADPH
RT cytochrome P450 reductase.";
RL EMBO Rep. 10:742-747(2009).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450 in microsomes. It can also provide electron transfer to
CC heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
CC Has NADPH-dependent ferrireductase activity on the plasma membrane.
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11485306,
CC ECO:0000269|PubMed:1730736, ECO:0000269|PubMed:9368374,
CC ECO:0000269|PubMed:9468503}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000269|PubMed:11485306,
CC ECO:0000269|PubMed:9368374, ECO:0000269|PubMed:9468503};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9468503};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9468503};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9468503};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9468503};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.59 uM for cytochrome c {ECO:0000269|PubMed:11485306};
CC KM=1.46 uM for NADPH {ECO:0000269|PubMed:11485306};
CC Note=The Vmax of the reaction is 721 pmol/min/pmol enzyme towards
CC cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.
CC {ECO:0000269|PubMed:11485306};
CC -!- SUBUNIT: Interacts with PCL1. {ECO:0000269|PubMed:15082539,
CC ECO:0000269|PubMed:16407065}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9468503}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}. Mitochondrion outer membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16407407}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}. Cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000269|PubMed:9368374}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000305|PubMed:11485306,
CC ECO:0000305|PubMed:9468503}.
CC -!- INDUCTION: By galactose and on the plasma membrane by iron or copper
CC deficiency. Repressed by glucose. {ECO:0000269|PubMed:9368374}.
CC -!- PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85.
CC {ECO:0000269|PubMed:15082539}.
CC -!- DISRUPTION PHENOTYPE: Accumulates 20% of ergosterol of wild type.
CC {ECO:0000269|PubMed:9468503}.
CC -!- MISCELLANEOUS: Present with 46600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13788; BAA02936.1; -; Genomic_DNA.
DR EMBL; U00062; AAB68904.1; -; Genomic_DNA.
DR EMBL; AY693091; AAT93110.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06734.1; -; Genomic_DNA.
DR PIR; S46735; S46735.
DR RefSeq; NP_011908.1; NM_001179172.1.
DR PDB; 2BF4; X-ray; 3.00 A; A/B=47-691.
DR PDB; 2BN4; X-ray; 2.91 A; A/B=47-691.
DR PDB; 2BPO; X-ray; 2.90 A; A/B=47-691.
DR PDB; 3FJO; X-ray; 2.50 A; A=44-211.
DR PDBsum; 2BF4; -.
DR PDBsum; 2BN4; -.
DR PDBsum; 2BPO; -.
DR PDBsum; 3FJO; -.
DR AlphaFoldDB; P16603; -.
DR SMR; P16603; -.
DR BioGRID; 36474; 71.
DR DIP; DIP-8294N; -.
DR IntAct; P16603; 9.
DR MINT; P16603; -.
DR STRING; 4932.YHR042W; -.
DR iPTMnet; P16603; -.
DR MaxQB; P16603; -.
DR PaxDb; P16603; -.
DR PRIDE; P16603; -.
DR EnsemblFungi; YHR042W_mRNA; YHR042W; YHR042W.
DR GeneID; 856438; -.
DR KEGG; sce:YHR042W; -.
DR SGD; S000001084; NCP1.
DR VEuPathDB; FungiDB:YHR042W; -.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000156847; -.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; P16603; -.
DR OMA; QKRYQRD; -.
DR BioCyc; YEAST:YHR042W-MON; -.
DR BRENDA; 1.6.2.4; 984.
DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-5578775; Ion homeostasis.
DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR SABIO-RK; P16603; -.
DR ChiTaRS; CPR1; yeast.
DR EvolutionaryTrace; P16603; -.
DR PRO; PR:P16603; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P16603; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IDA:SGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:CACAO.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_03212; NCPR; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR023208; P450R.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000208; P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing;
KW Endoplasmic reticulum; FAD; Flavoprotein; FMN; Isopeptide bond;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3139648"
FT CHAIN 2..691
FT /note="NADPH--cytochrome P450 reductase"
FT /id="PRO_0000167608"
FT TOPO_DOM 2..7
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 61..204
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 266..529
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 67..72
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672"
FT BINDING 78
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16407065"
FT BINDING 116..119
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672"
FT BINDING 152..161
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672"
FT BINDING 187
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 187
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16407065"
FT BINDING 285
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 439..442
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 457..459
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 476..479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 543
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 610..611
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 617..621
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT BINDING 646
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16407065"
FT BINDING 691
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:16407065"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 474
FT /note="V -> G"
FT CONFLICT 423
FT /note="T -> N (in Ref. 1; BAA02936)"
FT /evidence="ECO:0000305"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3FJO"
FT TURN 139..144
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3FJO"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:3FJO"
FT HELIX 192..210
FT /evidence="ECO:0007829|PDB:3FJO"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2BN4"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2BN4"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 368..374
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2BN4"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:2BF4"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 511..515
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 546..560
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:2BN4"
FT STRAND 574..585
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 587..591
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 592..599
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 603..610
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 628..635
FT /evidence="ECO:0007829|PDB:2BPO"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 650..665
FT /evidence="ECO:0007829|PDB:2BPO"
FT HELIX 670..682
FT /evidence="ECO:0007829|PDB:2BPO"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:2BPO"
SQ SEQUENCE 691 AA; 76772 MW; 82BB847701E5438B CRC64;
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN
YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE
GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG
KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE
PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL
EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK
WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN
LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG
PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG
ILSRGKSITT DEATELIKML KTSGRYQEDV W
