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NCB5R_YARLI
ID   NCB5R_YARLI             Reviewed;         290 AA.
AC   Q6CA86;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=NADH-cytochrome b5 reductase 1;
DE            EC=1.6.2.2 {ECO:0000250|UniProtKB:P38626};
DE   AltName: Full=Microsomal cytochrome b reductase;
GN   Name=CBR1; OrderedLocusNames=YALI0D04983g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: NADH-dependent reductase for DPH3 and cytochrome b5. Required
CC       for the first step of diphthamide biosynthesis, a post-translational
CC       modification of histidine which occurs in elongation factor 2. DPH1 and
CC       DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-
CC       methionine (SAM) to a histidine residue, the reaction is assisted by a
CC       reduction system comprising DPH3 and a NADH-dependent reductase,
CC       predominantly CBR1. By reducing DPH3, also involved in the formation of
CC       the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-
CC       thiouridine), mediated by the elongator complex. The cytochrome b5/NADH
CC       cytochrome b5 reductase electron transfer system supports the catalytic
CC       activity of several sterol biosynthetic enzymes.
CC       {ECO:0000250|UniProtKB:P38626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC         H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P38626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(3+)-[Dph3] + NADH = 2 Fe(2+)-[Dph3] + H(+) + NAD(+);
CC         Xref=Rhea:RHEA:71231, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:P38626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71232;
CC         Evidence={ECO:0000250|UniProtKB:P38626};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000250|UniProtKB:P38626}.
CC   -!- SUBUNIT: Monomer. Component of the 2-(3-amino-3-carboxypropyl)histidine
CC       synthase complex composed of DPH1, DPH2, DPH3 and a NADH-dependent
CC       reductase, predominantly CBR1. {ECO:0000250|UniProtKB:P38626}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P38626}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000305}.
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DR   EMBL; CR382130; CAG80614.1; -; Genomic_DNA.
DR   RefSeq; XP_502426.1; XM_502426.1.
DR   AlphaFoldDB; Q6CA86; -.
DR   SMR; Q6CA86; -.
DR   STRING; 4952.CAG80614; -.
DR   EnsemblFungi; CAG80614; CAG80614; YALI0_D04983g.
DR   GeneID; 2910663; -.
DR   KEGG; yli:YALI0D04983g; -.
DR   VEuPathDB; FungiDB:YALI0_D04983g; -.
DR   HOGENOM; CLU_003827_9_0_1; -.
DR   InParanoid; Q6CA86; -.
DR   OMA; KDMRFSF; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001300; Chromosome D.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; ISS:UniProtKB.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR001834; CBR-like.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19370; PTHR19370; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   NAD; Oxidoreductase; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..290
FT                   /note="NADH-cytochrome b5 reductase 1"
FT                   /id="PRO_0000330166"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..151
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         131..146
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..189
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  31939 MW;  DFE44F6E2184F36B CRC64;
     MRSSSSRQPQ MQSYYAIATV WALIIGAATY YFFSNSKPKA VLQRGDTAFK EFPLIQKTVL
     SHNSAIYRFG LPRPSHVLGL PIGQHVSLSA NIGGKEVLRS YTPTSSDLYD KGYFDILIKT
     YPQGNISKYV SELAIGDTMK VRGPKGNFVY NHGLVESFGM VCGGTGITPM YQILRHIAAD
     PADNTKVNLV YANVNHDDIL LKKELDAIAA ENDNIKIHYV LNNAPEDWTG SVGFVTKEIL
     EKHCPPPGPN TKLLLCGPPP MISALKKASV ELGYEKARPV SKLEDQVFAF
 
 
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