LYS5_ASHGO
ID LYS5_ASHGO Reviewed; 276 AA.
AC Q74Z24;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE Short=AASD-PPT;
DE EC=2.7.8.7;
GN Name=LYS5; OrderedLocusNames=AGR382W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 58-59.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
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DR EMBL; AE016820; AAS54872.2; -; Genomic_DNA.
DR RefSeq; NP_987048.2; NM_212110.2.
DR AlphaFoldDB; Q74Z24; -.
DR SMR; Q74Z24; -.
DR STRING; 33169.AAS54872; -.
DR PRIDE; Q74Z24; -.
DR EnsemblFungi; AAS54872; AAS54872; AGOS_AGR382W.
DR GeneID; 4623352; -.
DR KEGG; ago:AGOS_AGR382W; -.
DR eggNOG; KOG0945; Eukaryota.
DR HOGENOM; CLU_075352_0_0_1; -.
DR InParanoid; Q74Z24; -.
DR OMA; YYWSLKE; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175740"
SQ SEQUENCE 276 AA; 29922 MW; 09DA3DB1DCDD9514 CRC64;
MAQGSPATVA ACAFCGARRT RSGMVLSTSA ADGYLDDEAQ FETALRLLPA ADQAAVRRRR
AGRAVVLASR LLRTLGCAVH TGCAPALLAF DYSRAGKPYL RSRPAPAFSV SRSDCIAVIY
VREGGAVGAD LASVAECLSW APDEILQLHD VFSAAELGRL RAAAPGRARA ELFAYYWSLK
EAYGKFRGTG LAGDLRLADM GELDPLRRGE LRTLRRTLQG KHVCLSSRWH DAGHVLSLCE
AREPSPTEEI CLHKVPMEEV VRLCRPSLGM EKCHVR
