LYS5_YEAST
ID LYS5_YEAST Reviewed; 272 AA.
AC P50113; D6VTZ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase {ECO:0000303|PubMed:10320345};
DE Short=AASD-PPT {ECO:0000303|PubMed:10320345};
DE EC=2.7.8.7 {ECO:0000269|PubMed:10320345};
GN Name=LYS5 {ECO:0000303|PubMed:17322287}; OrderedLocusNames=YGL154C;
GN ORFNames=G1867;
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=8654981; DOI=10.1016/0378-1119(96)00105-9;
RA Miller K.G., Bhattacharjee J.K.;
RT "The LYS5 gene of Saccharomyces cerevisiae.";
RL Gene 172:167-168(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10320345; DOI=10.1021/bi9829940;
RA Ehmann D.E., Gehring A.M., Walsh C.T.;
RT "Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-
RT aminoadipate reductase (Lys2) involves posttranslational
RT phosphopantetheinylation by Lys5.";
RL Biochemistry 38:6171-6177(1999).
RN [7]
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: Catalyzes the transfer of a 4'-phosphopantetheine moiety from
CC coenzyme A to a serine residue of acceptor proteins, such as alpha-
CC aminoadipate reductase. Necessary for alpha-aminoadipate reductase
CC activity. {ECO:0000269|PubMed:10320345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000269|PubMed:10320345};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for CoA {ECO:0000269|PubMed:10320345};
CC KM=1 uM for alpha-aminoadipate reductase PCP fragment
CC {ECO:0000269|PubMed:10320345};
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
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DR EMBL; U32586; AAC49449.1; -; Genomic_DNA.
DR EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72676; CAA96866.1; -; Genomic_DNA.
DR EMBL; AY692861; AAT92880.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07958.1; -; Genomic_DNA.
DR PIR; S59762; S59762.
DR RefSeq; NP_011361.1; NM_001181019.1.
DR AlphaFoldDB; P50113; -.
DR SMR; P50113; -.
DR BioGRID; 33100; 10.
DR DIP; DIP-1426N; -.
DR IntAct; P50113; 3.
DR MINT; P50113; -.
DR STRING; 4932.YGL154C; -.
DR PaxDb; P50113; -.
DR PRIDE; P50113; -.
DR EnsemblFungi; YGL154C_mRNA; YGL154C; YGL154C.
DR GeneID; 852723; -.
DR KEGG; sce:YGL154C; -.
DR SGD; S000003122; LYS5.
DR VEuPathDB; FungiDB:YGL154C; -.
DR eggNOG; KOG0945; Eukaryota.
DR HOGENOM; CLU_075352_1_0_1; -.
DR InParanoid; P50113; -.
DR OMA; YYWSLKE; -.
DR BioCyc; YEAST:G3O-30645-MON; -.
DR SABIO-RK; P50113; -.
DR PRO; PR:P50113; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P50113; protein.
DR GO; GO:0005737; C:cytoplasm; TAS:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:SGD.
DR Gene3D; 3.90.470.20; -; 2.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..272
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175742"
SQ SEQUENCE 272 AA; 30683 MW; 3722252E7EC97787 CRC64;
MVKTTEVVSE VSKVAGVRPW AGIFVVEIQE DILADEFTFE ALMRTLPLAS QARILNKKSF
HDRCSNLCSQ LLQLFGCSIV TGLNFQELKF DKGSFGKPFL DNNRFLPFSM TIGEQYVAMF
LVKCVSTDEY QDVGIDIASP CNYGGREELE LFKEVFSERE FNGLLKASDP CTIFTYLWSL
KESYTKFTGT GLNTDLSLID FGAISFFPAE GASMCITLDE VPLIFHSQWF NNEIVTICMP
KSISDKINTN RPKLYNISLS TLIDYFIEND GL
