LYS5_CANGA
ID LYS5_CANGA Reviewed; 258 AA.
AC Q6FV34;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE Short=AASD-PPT;
DE EC=2.7.8.7;
GN Name=LYS5; OrderedLocusNames=CAGL0E05104g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380951; CAG58829.1; -; Genomic_DNA.
DR RefSeq; XP_445910.1; XM_445910.1.
DR AlphaFoldDB; Q6FV34; -.
DR SMR; Q6FV34; -.
DR STRING; 5478.XP_445910.1; -.
DR EnsemblFungi; CAG58829; CAG58829; CAGL0E05104g.
DR GeneID; 2887362; -.
DR KEGG; cgr:CAGL0E05104g; -.
DR CGD; CAL0128802; CAGL0E05104g.
DR VEuPathDB; FungiDB:CAGL0E05104g; -.
DR eggNOG; KOG0945; Eukaryota.
DR HOGENOM; CLU_075352_0_0_1; -.
DR InParanoid; Q6FV34; -.
DR OMA; YYWSLKE; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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..258
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175741"
SQ SEQUENCE 258 AA; 29842 MW; 45D6E4D78F708893 CRC64;
MSDWLSLAKS NDPHIVVLTM DVHLSYFRDE YNFEEALRLL PFEWQCRVIQ KRAHKDKVTA
LCNRLLQLYG CRLELNTQAI DFTQGKYGKP FVKNTESFNF SMTNGENFVS IIMANLFQTE
VGIDLASIND FTSEGDLKIY EDVLSTEEYE KINNQTNLLD MKRLFAFYWS VKECYTKYLG
VGLNGDLKII NVSLFSAPLI NEAVSTFKLK DITFHSRWVS DNEILTYCFP AQYDFLKPIH
AILNVVSVIE GIKTQFLT