ID F1A3U9_DICPU Unreviewed; 912 AA.
AC F1A3U9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGC29130.1};
GN ORFNames=DICPUDRAFT_51448 {ECO:0000313|EMBL:EGC29130.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29130.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871479; EGC29130.1; -; Genomic_DNA.
DR RefSeq; XP_003294346.1; XM_003294298.1.
DR AlphaFoldDB; F1A3U9; -.
DR STRING; 5786.F1A3U9; -.
DR EnsemblProtists; EGC29130; EGC29130; DICPUDRAFT_51448.
DR GeneID; 10506500; -.
DR KEGG; dpp:DICPUDRAFT_51448; -.
DR eggNOG; KOG0172; Eukaryota.
DR InParanoid; F1A3U9; -.
DR OMA; TPHVHDI; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000001064; Unassembled WGS sequence.
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 Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
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:SF26; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF05222; AlaDh_PNT_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:UP000001064}.
FT DOMAIN 8..138
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 178..376
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 912 AA; 103052 MW; 3F3EB47527B3318D CRC64;
MTKVYSLGIR REDKNRWERR APLAPSHVED LVKKGIKVIV QPSTLRNYPN VLYERAGAII
QEDLKECDVI AAVKEVPSEY LYEDKTYIFF SHTIKAQPYN MPMLDEINRK RIRLIDYERI
TDENNRRLVR FGSFAGYAGM IDMLHALGDR LLAKGFSTPF LHVGYSYVYS KLESAMEAVK
AIGEEISQVG LPDDLLPFTF AFTSDGAVAQ GALKIFKLLP HKMVTPDEMV DLVKNKKGER
GILYGTIITA EHMVAPIDPT KKFDKKDYYS QPHTYKPIFV EKYAPYISCI INCMYWDAKY
PRLITIRQME EMVENNNTRL IGVADISADI NGSLEFLMTT TSIDSPLYIY DPKTQEVHDP
TTDQQYMYRD GILFLAVDNL PTEFPKEATQ WFGDHLSKFI EAVVKSDPTL PYDKMTDIAP
EIKRAVITAH GSLTKPFEYI TELRKKREEL ISRILVLGAG SVSYSTISYL TRNPSHKITI
GDISLDQAKK AASVEPDADI QTVVIDVHNK EALDELVSKF KVIASLLPDE LSILVAESCL
RNKKHMVCPS YLSKEMEALH EQAKEAGVTL LNEMGLDPGI DHLEASRVIN DVKSKGGKIR
SFVSWCGGLP APESSDNPLG YKFTWSPKEI ISGVTNDSKF RRDGQDIFIS GQEVYKRLQP
VDIFPALSLE GVPNRDCLFL AKAYDIENVS TLFRGTIRYR GFCSVMEAAV EIGLLDTTSK
THLQPSSSPL SWNHAMRTLL PSPLADGIPT QELLRRKLRT RRGYPSKGYD DDKITHILSV
FDWLGVFSEE INVKLEGNFF DAFTELLKTK LSLLPSEKDL IILHNIIGIE WEGGKHETKT
STLVYYGSKD QSAVGTVVGL PIAIATELLL EGQVKERGAI RPVSKEYYKP MIKALHNEGI
TFIHRNEFDK QY
//
