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NCB5R_PICST
ID   NCB5R_PICST             Reviewed;         284 AA.
AC   A3GF86;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   03-AUG-2022, entry version 86.
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; ORFNames=PICST_68997;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63709.2; -; Genomic_DNA.
DR   RefSeq; XP_001387732.2; XM_001387695.1.
DR   AlphaFoldDB; A3GF86; -.
DR   SMR; A3GF86; -.
DR   STRING; 4924.XP_001387732.2; -.
DR   EnsemblFungi; EAZ63709; EAZ63709; PICST_68997.
DR   GeneID; 4850935; -.
DR   KEGG; pic:PICST_68997; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   HOGENOM; CLU_003827_9_0_1; -.
DR   InParanoid; A3GF86; -.
DR   OMA; KDMRFSF; -.
DR   OrthoDB; 1311668at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002258; Chromosome 1.
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: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..284
FT                   /note="NADH-cytochrome b5 reductase 1"
FT                   /id="PRO_0000330163"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          41..144
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         124..139
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..182
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  31274 MW;  0B825044D2C04489 CRC64;
     MADTEPSPLF VFSTIAIIIS TFVIFYFVQQ SKKNTPVLKP DTFQKFPLIE KTRVSHNSSV
     YRFGLPKSTD RLGLPIGQHI SIGATIGGKE VVRSYTPIST DDELGYFDLL IKTYENGNIS
     KHVDSKKVGE YVEIRGPKGF FTYTPNMVKS FGMIAGGTGI APMYQIITAI LRNPADKTKI
     SLIYANVTES DILLKSELDK WAEEHPDNFS VHYVLNEAPE NWKGSVGFVT PEIIDSKLPK
     ASDDSNLLLC GPPPMISAMK KAAVGLGFAK AKPVSKLGDQ VFVF
 
 
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