ID A0A397UWB0_9GLOM Unreviewed; 499 AA.
AC A0A397UWB0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Monofunctional lysine-ketoglutarate reductase 2 {ECO:0000313|EMBL:RIB14092.1};
GN ORFNames=C2G38_1681569 {ECO:0000313|EMBL:RIB14092.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB14092.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB14092.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB14092.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIB14092.1}.
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DR EMBL; QKWP01000864; RIB14092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397UWB0; -.
DR STRING; 44941.A0A397UWB0; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12189; LKR_SDH_like; 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 PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11133:SF26; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 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.
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:UP000266673}.
FT DOMAIN 34..165
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 212..399
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 499 AA; 57169 MW; 14AFDA5BABC3CE35 CRC64;
MNVKAKPFFF LSRSQNYSRY TTNLYQTRCL QSIALRREDK SHWERRVALT PDTISRLMKE
TGVKVYVQPC NKRIFNNNKF INAGAIVQED ISNADVILGI KEVPTKYLIP NKTYMFFSHT
HKGQLYNMPM LQDILDKKIR LIDYELMTDA QKRRLVLFGT HAGYAGMIDG LHGLGRRLLG
LGYNTPFMHI AMSHTYKSLD SAKSAVKDIG VTIADEGLPN DFSPMTFVFT GTGNVSNGVQ
DIFKCLPHEY VQVNDLKECA MASHKFSSYK VYGCQVHLHD YLIRTDTGKF DTKRDYYENP
QYYKSLFHTK IAPYTSMLIH GSYWDSRFPR LITKEQLCEI QKNSNNRRLL CVADISCDIE
GALEFLSHST TIDDPYFYFD AVKNEEHKKD EGEGTQIMAV DILPTEIPLE SSEHFSRSLY
PFIKDLVNGT IDNNPVLSNA TIAKDGRLVG AHTKLYELLP RNSRHNLSKI REMEITSSFV
NKPVISNHES LIRNSNISI
//
