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PANB_YEAST
ID   PANB_YEAST              Reviewed;         312 AA.
AC   P38122; D6VQH1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000303|PubMed:11154694};
DE            EC=2.1.2.11 {ECO:0000305|PubMed:11154694};
DE   AltName: Full=Extracellular matrix protein 31 {ECO:0000303|PubMed:11154694};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000303|PubMed:11154694};
GN   Name=ECM31 {ECO:0000303|PubMed:11154694}; OrderedLocusNames=YBR176W;
GN   ORFNames=YBR1238;
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 [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   [2]
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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11154694; DOI=10.1074/jbc.m009804200;
RA   White W.H., Gunyuzlu P.L., Toyn J.H.;
RT   "Saccharomyces cerevisiae is capable of de novo pantothenic acid
RT   biosynthesis involving a novel pathway of beta-alanine production from
RT   spermine.";
RL   J. Biol. Chem. 276:10794-10800(2001).
RN   [4]
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).
CC   -!- FUNCTION: Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase
CC       required for pantothenic acid biosynthesis (PubMed:11154694). Acts
CC       downstream in the pantothenic acid pathway (PubMed:11154694).
CC       {ECO:0000269|PubMed:11154694}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-
CC         oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-
CC         dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57453; EC=2.1.2.11;
CC         Evidence={ECO:0000305|PubMed:11154694};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC       {ECO:0000305|PubMed:11154694}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on beta-alanine but can still
CC       utilize pantothenic acid. {ECO:0000269|PubMed:11154694}.
CC   -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
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DR   EMBL; Z36045; CAA85137.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07291.1; -; Genomic_DNA.
DR   PIR; S46047; S46047.
DR   RefSeq; NP_009735.3; NM_001178524.3.
DR   AlphaFoldDB; P38122; -.
DR   SMR; P38122; -.
DR   BioGRID; 32875; 43.
DR   DIP; DIP-1303N; -.
DR   IntAct; P38122; 1.
DR   MINT; P38122; -.
DR   STRING; 4932.YBR176W; -.
DR   MaxQB; P38122; -.
DR   PaxDb; P38122; -.
DR   PRIDE; P38122; -.
DR   EnsemblFungi; YBR176W_mRNA; YBR176W; YBR176W.
DR   GeneID; 852474; -.
DR   KEGG; sce:YBR176W; -.
DR   SGD; S000000380; ECM31.
DR   VEuPathDB; FungiDB:YBR176W; -.
DR   eggNOG; KOG2949; Eukaryota.
DR   HOGENOM; CLU_036645_0_1_1; -.
DR   InParanoid; P38122; -.
DR   OMA; VLVWTDM; -.
DR   BioCyc; MetaCyc:MON3O-90; -.
DR   BioCyc; YEAST:MON3O-90; -.
DR   UniPathway; UPA00028; UER00003.
DR   PRO; PR:P38122; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38122; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IMP:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR   CDD; cd06557; KPHMT-like; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_00156; PanB; 1.
DR   InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR20881; PTHR20881; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR00222; panB; 1.
PE   1: Evidence at protein level;
KW   Pantothenate biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..312
FT                   /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT                   /id="PRO_0000184927"
SQ   SEQUENCE   312 AA;  34465 MW;  42A15F8A7A8CF291 CRC64;
     MNIMKRQLCT SSKRFFSTAK NVVKYNTIQD IRNKYFTGTP LSMCTAYDFI TATWVNKANC
     DLLLVGDSLA MTSLGYDSTI TLSLNEFKYH VASVCRAEGS SMVVVDMPFG TFESGISDGL
     KNAIDIMKLD SKVTSVKVEV GSYTKDKYAM KFIEELCSRG IPVMAHIGLT PQKVHSLGGY
     KVQGSKSLLQ MQELYETAMQ LQKIGCWSIL IECVPHKMAQ FITSKLSVPT IGIGAGNGTS
     GQVLVISDLL GMQGDSVPKF VKQAVNMTDI ATQGLKEYIA SVEDRTFPER GTHTFKVKED
     LWNEFLSSIN EK
 
 
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