ID D8Q6Z3_SCHCM Unreviewed; 983 AA.
AC D8Q6Z3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Alanine dehydrogenase/pyridine nucleotide transhydrogenase N-terminal domain-containing protein {ECO:0000259|SMART:SM01003};
GN ORFNames=SCHCODRAFT_68324 {ECO:0000313|EMBL:EFI95940.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI95940.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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DR EMBL; GL377307; EFI95940.1; -; Genomic_DNA.
DR RefSeq; XP_003030843.1; XM_003030797.1.
DR AlphaFoldDB; D8Q6Z3; -.
DR STRING; 578458.D8Q6Z3; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02629850; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_005231_0_0_1; -.
DR InParanoid; D8Q6Z3; -.
DR OMA; TPHVHDI; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000007431; Unassembled WGS sequence.
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:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
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; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
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; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT DOMAIN 15..168
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
SQ SEQUENCE 983 AA; 107439 MW; 0958A3385F576B13 CRC64;
MSSLVAGLKR PLVLGIRRED PARIWERRSP LVPAHVRQLL EKHKDLKVQV QRCTRRFFTE
EQYTEAGAQV VDDLSQAHII LGVKEPPLEE VFTDGVASPK DDSTASRVSL MFSHTTKGQA
YNMPLLRKFL RGQNEDKHVK PATLIDYELL VNEEGKRTVG FGHFAGVAGA FEAFHSLGLS
LLEKGYATPF LYSPRPQSQP TLETLKTAFH HTSTMIAENG IPQQLGPIIV GLTGSGLVSK
GALSVLKDLP HDMVTVEQLP LLLQGFDAVN HKKVYIYHAH PQDYLTRQDG GPYDRSSYYE
SPRLYSSKFA EKASSLPSNS LWYELIFVAP YLTMLINGVG WQPGFPRLMT KEDLDKALSL
ARVYPGFRLQ NIADISCDIG GGLEFMTQST TLSHPTYIEH PADPTLPPVT IMSVDILPAS
LPFDASMHFS TVLYPYLEDI IVRYANGEAR FSDAIERAVV AKDGRLTEPH AWLEEAAFAS
TEFSTAQSPS TTTQDHGVLR RKRVLMLGSG MVAGPAVETI ASRSDVQLVV ASNSAQEAQK
LAAENPSVEY RIIDMADESA VAPLVAEADV VISLLPATLH PVVAEACIAN KKHLVTASYI
SDSMRALDQR AQDVGVLLLN EIGLDPGIDH CSAMRLLDEI KSKSEQTTSF ISFCGGLPAP
EASNNPFKYK FSWSPRAALT AISQNPALFR LDGEVSSGAG QEVLDNHFPA FPVKNGEETL
EFEGLPNRDS LQYISQYGLP EQIGTMLRGT LRYPGFFDLM KTCYKLGLLN TTETIRLEKW
ADLVPAAYTS IHGGAPEAVD SALAKAVTTQ QAAQFLNAMK WLGIVPGAPA GTNVPLPPLP
AEALSPLDAF AHLLIAKLRF LPGERDLVAL THEIRTVDAS SAARTYRSTL IAYGNDRHSA
MARTVGIPVA LAALGVLDGR IGVRGVQGAT DGSVYRPVLE GLEERGIGMK ETVERVPEGG
DRYAILDVFT ERQGHKEKKG RRI
//
