ID   LYS2_SCHPO              Reviewed;        1419 AA.
AC   P40976; Q9P770;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 3.
DT   02-SEP-2026, entry version 183.
DE   RecName: Full=L-2-aminoadipate reductase;
DE            EC=1.2.1.31 {ECO:0000250|UniProtKB:P07702};
DE            EC=1.2.1.95 {ECO:0000250|UniProtKB:P07702};
DE   AltName: Full=Alpha-aminoadipate reductase;
DE            Short=Alpha-AR;
DE   AltName: Full=L-aminoadipate-semialdehyde dehydrogenase;
GN   Name=lys1; ORFNames=SPAP7G5.04c;
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 [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8590464; DOI=10.1007/bf00315779;
RA   Ford R.A., Bhattacharjee J.K.;
RT   "Molecular properties of the lys1+ gene and the regulation of alpha-
RT   aminoadipate reductase in Schizosaccharomyces pombe.";
RL   Curr. Genet. 28:131-137(1995).
RN   [2]
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   [3]
RP   MUTAGENESIS OF GLY-913 AND SER-916.
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   [4]
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 activation of alpha-aminoadipate by ATP-
CC       dependent adenylation and the reduction of activated alpha-aminoadipate
CC       by NADPH. The activated alpha-aminoadipate is bound to the
CC       phosphopantheinyl group of the enzyme itself before it is reduced to
CC       (S)-2-amino-6-oxohexanoate. {ECO:0000250|UniProtKB:P07702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + NADP(+) + H2O = L-2-aminoadipate
CC         + NADPH + 2 H(+); Xref=Rhea:RHEA:12304, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + NAD(+) + H2O = L-2-aminoadipate +
CC         NADH + 2 H(+); Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = L-
CC         2-aminoadipate + ATP + NADPH + H(+); Xref=Rhea:RHEA:46936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58672, ChEBI:CHEBI:456215; EC=1.2.1.95;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC       Note=Binds 1 phosphopantetheine covalently.
CC       {ECO:0000250|UniProtKB:P07702};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U15923; AAC15909.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB88271.1; -; Genomic_DNA.
DR   PIR; S57264; S57264.
DR   RefSeq; NP_594314.1; NM_001019737.3.
DR   AlphaFoldDB; P40976; -.
DR   SMR; P40976; -.
DR   BioGRID; 278556; 5.
DR   FunCoup; P40976; 103.
DR   STRING; 284812.P40976; -.
DR   iPTMnet; P40976; -.
DR   PaxDb; 284812-P40976; -.
DR   GeneID; 2542079; -.
DR   KEGG; spo:2542079; -.
DR   PomBase; SPAP7G5.04c; lys1.
DR   VEuPathDB; FungiDB:SPAP7G5.04c; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_19_0_1; -.
DR   InParanoid; P40976; -.
DR   OMA; ENDKFTM; -.
DR   PhylomeDB; P40976; -.
DR   BRENDA; 1.2.1.95; 5613.
DR   UniPathway; UPA00033; UER00032.
DR   PRO; PR:P40976; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity; IDA:PomBase.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009085; P:L-lysine biosynthetic process; IDA:PomBase.
DR   CDD; cd05235; SDR_e1; 1.
DR   FunFam; 3.30.559.30:FF:000068; L-2-aminoadipate reductase; 1.
DR   FunFam; 3.40.50.720:FF:000787; L-2-aminoadipate reductase; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_dom.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-b_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR001242; Condensation_dom.
DR   InterPro; IPR013120; FAR_NAD-bd.
DR   InterPro; IPR014397; Lys2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR03443; alpha_am_amid; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44845:SF1; L-2-AMINOADIPATE REDUCTASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Lysine biosynthesis; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1419
FT                   /note="L-2-aminoadipate reductase"
FT                   /id="PRO_0000193152"
FT   DOMAIN          880..956
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         916
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MUTAGEN         913
FT                   /note="G->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:15546125"
FT   MUTAGEN         916
FT                   /note="S->A,T: No activity."
FT                   /evidence="ECO:0000269|PubMed:15546125"
FT   CONFLICT        90..91
FT                   /note="MT -> IA (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="Missing (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="D -> DG (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500
FT                   /note="R -> G (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        600..602
FT                   /note="Missing (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620..621
FT                   /note="AR -> GP (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="Y -> S (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        926..928
FT                   /note="LRK -> PSQ (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1203..1205
FT                   /note="VVV -> AAA (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1225..1228
FT                   /note="LVRM -> WSK (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1239
FT                   /note="P -> A (in Ref. 1; AAC15909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1419 AA;  156894 MW;  09AFBEFE09F21A0C CRC64;
     MSQTAPSDTE YNQRLERWSE RLKSQTISHL PTDYSRPVPS RLVEAVFERT LPEDAKTALI
     KVYVAAQAKG ILVTPFNILL TIFIILVSRM TGDEDISIGT SSENAIPFVL RTFIQPSDSF
     LDLLAKVCDL EKEGSSDAVD FSDLINFLNA KLSKKDDPRK TLVHLRFYNA PDAPSENFLS
     TTGLDVDLTV LVSVKKPSDQ LTSLRSQFTF PDLQLKLIYN QLLFSESRVN IVADQLLKLV
     VSASKDVTGP IGALDLMTPT QMNVLPDPTV DLDWSGYRGA IQDIFASNAA KFPDRECIVV
     TPSVTIDAPV TSYTYRQIDE SSNILAHHLV KNGIERGDVV MVYAYRGVDL VVAVMGVLKA
     GATFSVIDPA YPPARQIIYL SVAKPRALVV LEDAGVLSPT VVEYVEKSLE LKTYVPALKL
     AKDGSLTGGS VSKGADDILQ HVLHLKSEQT GVVVGPDSTP TLSFTSGSEG IPKGVKGRHF
     SLAYYFDWMA QEFNLSESDR FTMLSGIAHD PIQRDIFTPL FLGASLIVPT AEDIGTPGQL
     AQWANKYKVT VTHLTPAMGQ LLAAQADEPI PSLHHAFFVG DILTKRDCLR LQVLANNVNV
     VNMYGTTETQ RSVSYFVVPA RSQDQTFLES QKDVIPAGRG MKNVQLLVIN RFDTNKICGI
     GEVGEIYLRA GGLAEGYLGN DELTSKKFLK SWFADPSKFV DRTPENAPWK PYWFGIRDRM
     YRSGDLGRYL PTGNVECSGR ADDQIKIRGF RIELGEINTH LSRHPNVREN ITLVRRDKDE
     EPTLVAYIVP QGLNKDDFDS ATESEDIVVN GLKKYRKLIH DIREYLKTKL PSYAIPSVIV
     PLHKMPLNPN GKIDKPALPF PDTSQLAAAS RSHSKHGVDE TLTATERDIR DIWLRIIPHA
     TDVNKKASFF DIGGHSILAT RLIFELRKKF AVNVPLGLVF SEPTIEGLAK EIERMKSGEM
     ISVMDIGKEE TREPEIEYGK DALDLVDLIP KEFPTSKDLG IDEPKTVFLT GANGYLGVFI
     LRDLMTRSSN LKVIALVRAS SEEHGLKRLK DSCTAYGVWD ESWAQKISVV NGDLALENWG
     IEERKWNKLT EVVDYVIHNG ALVHWVYPYS KLRGPNVMGT ITALKLCSLG KGKSLSFVSS
     TSTVDTEYYV NLSNEITSKG GNGIPESDPL QGSSKDLHTG YGQSKWVSEY LVRQAGLRGL
     RGVVVRPGYI LGDSKSGAIN TDDFLVRMVK GCIELGLYPN INNTVNMVPA DHVARVVTAS
     AFHPEQGVIV AHVTSHPRLR FNQFLGTLST FGFNTKLSEY VNWRIALERF VINESHDSAL
     YPLLHFVLDN LPANTKAPEL DDTNTREILK RDASWTNVDV SNGAAILEHE MGLYLSYLVA
     IGFLPKPTLE GKKLPEVKIN EATLEKLASA GGRGGAPTH
//