位置:首页 > 蛋白库 > PDX3_YEAST
PDX3_YEAST
ID   PDX3_YEAST              Reviewed;         228 AA.
AC   P38075; D6VQ35;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=Pyridoxamine 5'-phosphate oxidase;
DE            EC=1.4.3.5;
DE   AltName: Full=PNP/PMP oxidase;
DE            Short=PNPOx;
GN   Name=PDX3; OrderedLocusNames=YBR035C; ORFNames=YBR0321;
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].
RX   PubMed=7896706; DOI=10.1128/jb.177.7.1817-1823.1995;
RA   Loubbardi A., Karst F., Guilloton M., Marcireau C.;
RT   "Sterol uptake induced by an impairment of pyridoxal phosphate synthesis in
RT   Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding
RT   pyridoxine (pyridoxamine) phosphate oxidase.";
RL   J. Bacteriol. 177:1817-1823(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091864; DOI=10.1002/yea.320100010;
RA   Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT   "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT   II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT   ten new open reading frames, five previously identified genes and a
RT   homologue of the SCO1 gene.";
RL   Yeast 10:S75-S80(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
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   [6]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA   Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA   Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT   "Intermembrane space proteome of yeast mitochondria.";
RL   Mol. Cell. Proteomics 11:1840-1852(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH FMN.
RG   New York structural genomix research consortium (NYSGXRC);
RT   "The structure of PNP oxidase from S. cerevisiae.";
RL   Submitted (JAN-2005) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC       (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC       (PLP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC         pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:22984289}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC       {ECO:0000305}.
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; X76078; CAA53690.1; -; Genomic_DNA.
DR   EMBL; X76992; CAA54295.1; -; Genomic_DNA.
DR   EMBL; Z35904; CAA84977.1; -; Genomic_DNA.
DR   EMBL; AY557712; AAS56038.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07155.1; -; Genomic_DNA.
DR   PIR; S41301; S41301.
DR   RefSeq; NP_009591.1; NM_001178383.1.
DR   PDB; 1CI0; X-ray; 2.70 A; A/B=1-228.
DR   PDBsum; 1CI0; -.
DR   AlphaFoldDB; P38075; -.
DR   SMR; P38075; -.
DR   BioGRID; 32736; 268.
DR   DIP; DIP-4324N; -.
DR   IntAct; P38075; 2.
DR   STRING; 4932.YBR035C; -.
DR   iPTMnet; P38075; -.
DR   MaxQB; P38075; -.
DR   PaxDb; P38075; -.
DR   PRIDE; P38075; -.
DR   EnsemblFungi; YBR035C_mRNA; YBR035C; YBR035C.
DR   GeneID; 852323; -.
DR   KEGG; sce:YBR035C; -.
DR   SGD; S000000239; PDX3.
DR   VEuPathDB; FungiDB:YBR035C; -.
DR   eggNOG; KOG2586; Eukaryota.
DR   GeneTree; ENSGT00390000011219; -.
DR   HOGENOM; CLU_032263_2_0_1; -.
DR   OMA; PEPNAMV; -.
DR   BioCyc; MetaCyc:YBR035C-MON; -.
DR   BioCyc; YEAST:YBR035C-MON; -.
DR   Reactome; R-SCE-964975; Vitamins B6 activation to pyridoxal phosphate.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   EvolutionaryTrace; P38075; -.
DR   PRO; PR:P38075; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38075; protein.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR   GO; GO:0010181; F:FMN binding; IDA:SGD.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:SGD.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IC:SGD.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.110.10; -; 1.
DR   HAMAP; MF_01629; PdxH; 1.
DR   InterPro; IPR000659; Pyridox_Oxase.
DR   InterPro; IPR019740; Pyridox_Oxase_CS.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR10851; PTHR10851; 1.
DR   Pfam; PF10590; PNP_phzG_C; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   TIGRFAMs; TIGR00558; pdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Flavoprotein; FMN; Isopeptide bond; Mitochondrion;
KW   Oxidoreductase; Pyridoxine biosynthesis; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..228
FT                   /note="Pyridoxamine 5'-phosphate oxidase"
FT                   /id="PRO_0000167787"
FT   BINDING         20..23
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         73..76
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         78
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         88..89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         95..96
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         118
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         136
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         140
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         144
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT   BINDING         153..154
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         199
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         205..207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   BINDING         209
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   HELIX           35..48
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   HELIX           95..102
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          117..127
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   HELIX           130..139
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   HELIX           142..150
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   HELIX           160..173
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          186..200
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:1CI0"
FT   STRAND          222..226
FT                   /evidence="ECO:0007829|PDB:1CI0"
SQ   SEQUENCE   228 AA;  26908 MW;  8B648A219763160E CRC64;
     MTKQAEETQK PIIFAPETYQ YDKFTLNEKQ LTDDPIDLFT KWFNEAKEDP RETLPEAITF
     SSAELPSGRV SSRILLFKEL DHRGFTIYSN WGTSRKAHDI ATNPNAAIVF FWKDLQRQVR
     VEGITEHVNR ETSERYFKTR PRGSKIGAWA SRQSDVIKNR EELDELTQKN TERFKDAEDI
     PCPDYWGGLR IVPLEIEFWQ GRPSRLHDRF VYRRKTENDP WKVVRLAP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025