ID B8BS40_THAPS Unreviewed; 1000 AA.
AC B8BS40;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme {ECO:0000313|EMBL:EED96060.1};
DE Flags: Fragment;
GN ORFNames=THAPSDRAFT_261124 {ECO:0000313|EMBL:EED96060.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED96060.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED96060.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED96060.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED96060.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED96060.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
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DR EMBL; CM000638; EED96060.1; -; Genomic_DNA.
DR RefSeq; XP_002286419.1; XM_002286383.1.
DR AlphaFoldDB; B8BS40; -.
DR STRING; 35128.B8BS40; -.
DR PaxDb; 35128-Thaps261124; -.
DR EnsemblProtists; EED96060; EED96060; THAPSDRAFT_261124.
DR GeneID; 7449095; -.
DR KEGG; tps:THAPSDRAFT_261124; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_005231_1_0_1; -.
DR InParanoid; B8BS40; -.
DR OMA; TPHVHDI; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000001449; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR CDD; cd12189; LKR_SDH_like; 1.
DR CDD; cd12144; SDH_N_domain; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.30.70.2690; LOR/SDH bifunctional enzyme, conserved domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR007545; LOR/SDH_bifunc_enz_cons_dom.
DR InterPro; IPR043009; LOR/SDH_bifunc_enz_cons_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF04455; Saccharop_dh_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449}.
FT DOMAIN 2..146
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 192..377
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED96060.1"
FT NON_TER 1000
FT /evidence="ECO:0000313|EMBL:EED96060.1"
SQ SEQUENCE 1000 AA; 110543 MW; F432CE8D6FFA5F83 CRC64;
VGILAEHYDK WERRRSPITP DHVKQLITSF KHGELTNVYV QPSQRIFPET QYEAVGAKIS
ADLCDADILL GVKQPNIDDL LPDKTYFFFS HVIKGQPENM ALLQAILDKN IQLFDYEAIA
SDETDPSTGK IRKRRLVAFG KYAGIAGMID TFQCLGRRLL ASGYSTPFLN CSPAYVYYDL
DEAKRSVKEL GRHIEEDGLP MSLEPLVFAF TGNGNVTTGA LEMFQLLPHK MVTLDEAIAL
KNTTGPHKCI YGLMVQQQDL VKRTGSEEVF DVKHYRENPS EYESTFASKV APICNVIVNG
IYWDERYPRL LTKAEMSELY RNGSKGLFVV GDISCDVNGS IEFLEKTTTI EKPFFSWNPT
TNEADDEISK DGIAVMGVDI LPTELSVESS KHFGESLLPL LKQLITNGHD KDDDVYGNLS
PELANACITQ NGSLTPNFAY IKALMERPRA STTKTIHSLS QPHILLRIEG HLFDSGLINN
VLDVIENQDC PFDIEECTVK RTVNGVATKS ILMMRVFSDD DEKLGNVLKK ITLLLDLIDS
ADASMQHFDN RLQSKPSSSQ NRVTVLGERE QNILLLGAGK VASSFAEYLG RSKTNTITVA
SQYEADAMKT ARYATRGKAV TCDLSQPGDQ LKYLIQEADI VVSLLPAQMH PTIAEECISM
KTDLVTASYE SEEMRALCSS AEEAGIAILN EMGLDPGVDH MSAMKIIDDV HERGGEITSF
SSVCGGLPSP EVANHNPLLY KFSWSPMGVM KASQNAAVYR KDNQLVVIDG ADLLASAEPF
DAWKSLNLEC IPNRDSLVYG EKYGIESAAT IFRGTLRYQG FSSLLHVLKN MGLLDNKGTG
AVSWYDALDD LRKQGGHADL RKFVLACAGG DRDLGLRAYN CLSWLGLKEH TPVSEPSSIA
KSFCDVLQQH LQFEEGERDM VLMHHDIRAV FGDGSNETLS CSMELYGDDR MTAMCKTVGF
TAAIGTKLIL EGGITNKGLL LPTSKDVYTP SLELLREEGI
//
