LYS5_SCHPO
ID LYS5_SCHPO Reviewed; 258 AA.
AC Q10474;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE Short=AASD-PPT;
DE EC=2.7.8.7 {ECO:0000305|PubMed:15546125};
GN Name=lys7; ORFNames=SPAC17C9.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 79-GLY--PRO-81;
RP 93-PHE--ASN-96; 124-GLY--ASP-126; 172-LYS-GLU-173 AND LYS-177.
RC STRAIN=972 / ATCC 24843;
RX PubMed=15546125; DOI=10.1002/yea.1179;
RA Guo S., Bhattacharjee J.K.;
RT "Posttranslational activation, site-directed mutation and phylogenetic
RT analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase
RT Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from
RT Schizosaccharomyces pombe.";
RL Yeast 21:1279-1288(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:15546125}.
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:0000305|PubMed:15546125};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA97348.1; -; Genomic_DNA.
DR PIR; T11582; T11582.
DR RefSeq; NP_594603.1; NM_001020031.2.
DR AlphaFoldDB; Q10474; -.
DR SMR; Q10474; -.
DR BioGRID; 278594; 1.
DR STRING; 4896.SPAC17C9.02c.1; -.
DR PaxDb; Q10474; -.
DR EnsemblFungi; SPAC17C9.02c.1; SPAC17C9.02c.1:pep; SPAC17C9.02c.
DR GeneID; 2542118; -.
DR KEGG; spo:SPAC17C9.02c; -.
DR PomBase; SPAC17C9.02c; lys7.
DR VEuPathDB; FungiDB:SPAC17C9.02c; -.
DR eggNOG; KOG0945; Eukaryota.
DR HOGENOM; CLU_1023625_0_0_1; -.
DR InParanoid; Q10474; -.
DR OMA; DFNVSHY; -.
DR PhylomeDB; Q10474; -.
DR PRO; PR:Q10474; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009085; P:lysine biosynthetic process; IDA:PomBase.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:PomBase.
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 Amino-acid biosynthesis; Cytoplasm; Lysine biosynthesis; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..258
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000116616"
FT MUTAGEN 79..81
FT /note="GRP->AKA: No activity."
FT /evidence="ECO:0000269|PubMed:15546125"
FT MUTAGEN 93..96
FT /note="FDFN->WEWI: No activity."
FT /evidence="ECO:0000269|PubMed:15546125"
FT MUTAGEN 124..126
FT /note="GVD->AIE: No activity."
FT /evidence="ECO:0000269|PubMed:15546125"
FT MUTAGEN 172..173
FT /note="KE->RD: No activity."
FT /evidence="ECO:0000269|PubMed:15546125"
FT MUTAGEN 177
FT /note="K->R: No activity."
FT /evidence="ECO:0000269|PubMed:15546125"
SQ SEQUENCE 258 AA; 29320 MW; 101453D340F5374B CRC64;
MKQKVYRLLI DTQEAWPFER TRIPSFKKLS DSERQQIERY YFDMDAKMAL ASILIKRHLV
STALECSPNE VQISVTKAGR PYCQSAHCPP IIFDFNVSHY GGIVIVVGAW LPSDPSGMRP
INIGVDIVEC KPLAFEASWM EDFMSVFTPC EWKLIKSSIS SIDVFFLLWT CKEAILKALG
IGLSGNPLDI VVTFHKLNEL LNSEEVSLRR AATAVYSGYS WDLEIHKLIL HSSTFYVSVA
FPQDCVIMDL NWETLNDL
