LYS2_SCHPO
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 25-MAY-2022, entry version 168.
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 + H2O + NADP(+) = 2 H(+) + L-2-
CC aminoadipate + NADPH; 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 + H2O + NAD(+) = 2 H(+) + L-2-
CC aminoadipate + NADH; 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(+) = ATP
CC + H(+) + L-2-aminoadipate + NADPH; 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_001019737.2.
DR AlphaFoldDB; P40976; -.
DR SMR; P40976; -.
DR BioGRID; 278556; 5.
DR STRING; 4896.SPAP7G5.04c.1; -.
DR iPTMnet; P40976; -.
DR MaxQB; P40976; -.
DR PaxDb; P40976; -.
DR PRIDE; P40976; -.
DR EnsemblFungi; SPAP7G5.04c.1; SPAP7G5.04c.1:pep; SPAP7G5.04c.
DR GeneID; 2542079; -.
DR KEGG; spo:SPAP7G5.04c; -.
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 activity; IDA:PomBase.
DR GO; GO:0031177; F:phosphopantetheine 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 CDD; cd05235; SDR_e1; 1.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR001242; Condensatn.
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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR TIGRFAMs; TIGR03443; alpha_am_amid; 1.
DR TIGRFAMs; TIGR01746; Thioester-redct; 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
