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LYS2_ASHGO
ID   LYS2_ASHGO              Reviewed;        1385 AA.
AC   Q75BB3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 114.
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   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium 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 + 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   -!- 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; 33169.AAS51573; -.
DR   PRIDE; 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   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; 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; 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; 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   Pfam; PF00501; AMP-binding; 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.
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
 
 
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