ID I2H7T5_TETBL Unreviewed; 1383 AA.
AC I2H7T5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Alpha-aminoadipate reductase {ECO:0000256|ARBA:ARBA00032195};
DE EC=1.2.1.31 {ECO:0000256|ARBA:ARBA00013073};
DE EC=1.2.1.95 {ECO:0000256|ARBA:ARBA00012913};
DE AltName: Full=L-aminoadipate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00031335};
GN Name=TBLA0H01500 {ECO:0000313|EMBL:CCH62437.1};
GN ORFNames=TBLA_0H01500 {ECO:0000313|EMBL:CCH62437.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62437.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH62437.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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:0000256|ARBA:ARBA00003499}.
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:0000256|ARBA:ARBA00001581};
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:0000256|ARBA:ARBA00001477};
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:0000256|ARBA:ARBA00000512};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3.
CC {ECO:0000256|ARBA:ARBA00004827}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; HE806323; CCH62437.1; -; Genomic_DNA.
DR RefSeq; XP_004181956.1; XM_004181908.1.
DR STRING; 1071380.I2H7T5; -.
DR GeneID; 14497594; -.
DR KEGG; tbl:TBLA_0H01500; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_0_1; -.
DR InParanoid; I2H7T5; -.
DR OMA; ENDKFTM; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000002866; Chromosome 8.
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 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_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; 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 843..920
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1383 AA; 154981 MW; 7FBA2E922D8E3BDB CRC64;
MSQSIWVDRL SNPTLSTLPQ DYKNPQEVPF ICQETTSIEV PQLDTLPDSL NDPYIVVLCV
WSSLLFRLTG DNDIIIYISN SKILRFEIIS TWSFQEMYDT VCTELNKLQA LPSIESLDTL
SLEIQKQNGS ELIPKLFTQM VLLEGDTSLD QFKYNPLDIS LLLHLSSTES ANSILTINYN
SRIYSKERIL NLFDQLLQFI SAVIIDPKRI IAKINLITPD SLTNLPNPKA ALGWCDFVGC
IHDIFQDNAE RFPERTCVVE TPSFDSNLPL RKFTYGDINR SSNLVAHYLI SKGIEVGDVV
MIYSSRGVDL MICVMGVLKA GATFSVIDPS YPPERQTVYL SVAKPRGLIV IRKAGQLDPL
VKDYIAKELD IKAFIPSIEI QDNATLQGAL TNDPLEKVRS LENVRTDIIL GPDSNPTLSF
TSGSEGLPKG VLGRHFSLAY YFNWMSKTFK LSSSDRFTML SGIAHDPIQR DMFTPLYLGA
QLYVPTQTDI GTPGKLAEWI SKYQCTVTHL TPAMGQLLAA QATAQISALH HAFFVGDILT
KRDCTRLQSL APNCNIVNMY GTTETQRAVS YYEVISKNQD PTFLESLKDT IPAGKGMYNV
QLLVVNRYDR TQICGVGEVG EIYMRAGGLA EGYRGLPDLN KEKFVNNWFV DENHWNYLDD
KKDKPWNKYW LGPRDRLYRT GDLGRYLPDG NCECCGRADD QVKIRGFRIE LGEIDTHISQ
YPLVRENITL VRKNQNGEPT LITFMVPRFD MEDQLHKYYE PLSNNVSTDP IVKGLLEYGQ
LTKQIKDFLK KRLASYSIPT LIVVMNKLPL NPNGKVDKPK LQYPTEKQLQ LVQQNTNIEN
ETVNFTPTEK RVLELWLKVL PSPPASVTVE DSFFDLGGHS LLATKMIFML KKQYNINIPL
NTIYKFPTIK EFANKIDNRE VSETETDTSS ITSSNNYFAD AKKLVKSLPE LYPSNSANNI
SNKKAINFFV TGVTGFLGSY ILSNILNREG DVNYKVFAHV RSSSKEEGLQ RIRKAGIIYG
TWNESFVENI EVVLGDLSVK QFGLSDADWN SLASLIDVII HNGALVHWVY PYSKLRASNV
IATINVMSLA TIGKPKNFDF VSSTSVLDTT FYFDLSEKLI KDGKDGILET DDLMGSSNGL
SGGYGQSKWV AEYLVREAGK RGLRGCIVRP GYVTGASKNG SCNTDDFLLR FMKGCLQLGY
VPDIDNSVNM VPVDHVAQVV VATSLYSPSS TELPVAHVTA HPRISLRDYV SVLNDYGYFV
KQTSYADWRD RLENATINEG QENALYPLLH MVLNNLEENT KAPELDDRNA QFSLDKDNAN
VTKSISMGAT PRQIAIYISF LIQVGFLSNV AINSTKKLPV LELTKSQIEL VSSGAGSRTS
SAK
//
