ID LYS2_EREGS Reviewed; 1385 AA.
AC Q75BB3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 27-NOV-2024, entry version 122.
DE RecName: Full=L-2-aminoadipate reductase large subunit;
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=LYS2; OrderedLocusNames=ADL346W;
OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya 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 543-570; 575; 578; 587 AND
RP 591.
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 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 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE016817; AAS51573.2; -; Genomic_DNA.
DR RefSeq; NP_983749.2; NM_209102.2.
DR AlphaFoldDB; Q75BB3; -.
DR SMR; Q75BB3; -.
DR STRING; 284811.Q75BB3; -.
DR EnsemblFungi; AAS51573; AAS51573; AGOS_ADL346W.
DR GeneID; 4619884; -.
DR KEGG; ago:AGOS_ADL346W; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_1_1; -.
DR InParanoid; Q75BB3; -.
DR OMA; ENDKFTM; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd17647; A_NRPS_alphaAR; 1.
DR CDD; cd05235; SDR_e1; 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 InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..1385
FT /note="L-2-aminoadipate reductase large subunit"
FT /id="PRO_0000193148"
FT DOMAIN 843..920
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 880
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1385 AA; 151953 MW; DE96D1018986F338 CRC64;
MCAVLEPSMI RWLSEVDNIV VSSLPSDYIP SGPAGVKAES CEVELPGSFG VIDEEDSYIR
LLSAFATLVC RMSGESDVAM YSKANRLLKL AVPPGVAFQQ LRASVTEAVE GTLALPAVDF
DELSALEREK KQLDYYPQYF KVGVVTAADK TKLDQFRYHK FELLLRQVTS SRFEMVYDSE
RFSPDRIGEL GEQLVQFLTL VEAKDDADVY AISLVTSGAS RVLPDPTTDL GWGQFRGAIH
DIFQHHAETR PDRLCVVETG VGQVAARTFT YSAINCASNI VAHYLLARGI RRGDVVMIYS
TRGVDLLVSV LGVLKSGAVF SVIDPAYPPA RQNVYLGVAK PAGLIVIQAA GQLDEAVEAF
IRDNLSLKAR LPALALQTDG AILGGTLPDF HLDTLVPFAS LKNTRTDVVV GPDSNPTLSF
TSGSEGIPKG VLGRHFSLTY YFDWMAKRFG LSEDDKFTML SGIAHDPIQR DMFTPIYLGA
QLLVPQEDDI GTPGRLATWM ATHGATVTHL TPAMGQVLTA DATTPFPSLK RAFFVGDVLT
KRDCARLQSL AENVAIVNMY GSTETQRAVS YFEVPSCSSN PSYLDNLKSI IPAGRGMHNV
QLLIVNRHDR TKLCGIGEVG EIYVRAGGLS EGYRGLPEIN KEKFIDNWFV DAGHWGGLDL
SGDEPWRNYW LGVRDRLYRT GDLGRYLPNG DCECCGRADD QVKIRGFRIE LGEIDTNISQ
YPLCRENITL LRKDQNGEST LISYLVPRSD QKALASFISA VPESIATESI AGSLIKYHKL
INDIRGFLKK RLAGYAIPTL IMVMERLPLN PNGKIDKNKL QFPEPTELDR ASEHFASETL
GLSSFSPLEQ EIRKIWLDLL PTRPAITSSD ESFFDLGGTS ILATRMAIVL RNRLNISLAL
STIFRYPTVK ELAKEISRVR GTISDDKSSN SGTTEYYADA KHVSEAELAS KYESRLSLLP
SGATSAPVYV FLTGVTGFLG CHILADLLNR SRKPYDITVY AHVRASDESS ALQRIKSVCT
AYGLWKNAYA PRIKVVLGNL AEKQFGLPKK AWHDLQEGID VIIHNAALVH WVYPYSKLRE
ANVLSTVNVL NLAAAGKAKY FTFVSSTSAL DTKHYLELSN AAIESGGSGV PEDDDLMGGS
LGLKGGYGQS KWAAEFIIKR AGERGLRGCI LRPGYVTGSP STGASNADDF LLRFLRGCVQ
LGKIPDIEGT VNMVPVDYVA RLATAASFSS SGNTHMMVVN VNAKPRISFR DYLLALKEYG
YQVTSVPYDE WSKALESSSD EENPLYPLLY LVLDDLPKKL RSPELDTTNA KFVLEEDFAR
TNIEPIIITS VSLEVVGSYI SFLHKLGFLE EPAKGSRPLP NISLSDEQIS LIAAVATARS
STAKP
//
