ID A0A2G8SFW1_9APHY Unreviewed; 1011 AA.
AC A0A2G8SFW1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Alanine dehydrogenase/pyridine nucleotide transhydrogenase N-terminal domain-containing protein {ECO:0000259|SMART:SM01003};
GN ORFNames=GSI_05369 {ECO:0000313|EMBL:PIL32665.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL32665.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL32665.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL32665.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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:PIL32665.1}.
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DR EMBL; AYKW01000010; PIL32665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8SFW1; -.
DR STRING; 1077348.A0A2G8SFW1; -.
DR OrthoDB; 2184985at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; 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; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT DOMAIN 28..188
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
SQ SEQUENCE 1011 AA; 110488 MW; 4243F7936423866F CRC64;
MAVLQRSPHP LRLCRPYTAA SPKRLTVGIR REDPARIWER RCPLTPDAVH DLVHNNGIDV
LIQPCERRVF TANDFIKAGA KLHPTLQPAH VIVGIKETPL PEVSTDPLPA PASLLLDPSN
LIPRTHIMFS HTVKGQLYNM ELLGKFLASE SPDAVQAGTL LPRLIDYELL TGRDGKRTVG
FGWFAGVAGA LESLVAMSRA HLELGVASPF LWTPRPHTHP SLASIRKTLR DVVGAQIATD
GTPKSLGPLV IGITGTGNVA HGCLDLLEEL PVEHINADQL RKVVTDPNTD LHKIYVVHAH
PKDYFVRRDG RAFERLDYYA HPDQYVSEFH TKIAPYLSLL LHGAGWAPTY PRLMTNEQLT
TTLEIAQTLG KGRFACVGDI SCDVNGGLEF LSQYTTLCSP TFVARPPPLP AHLPSVTMMA
VDILPTALPL EASQHFSAKF IPYLRSILST YTGKDDASEE ARLIQEALKR ATVASGGELR
SEWEWLRKPL GVWKDNVSSP EGSKQKTDGM QAKKKVLMLG SGMVAPPAVQ ELCSRSDVRL
VVASNVLADA ERLTAPYDNA MPVLVDMGHI EAVESLVADS DVVISLLPVP FHPSVAELCI
RHRKHLVTAS YISPAMRELH DRAISADVLL MNEIGLDPGI DHCSALSLID SLRAQGKEVV
SFTSFCGGLP APEDAEVPLG YKFSWSPKGV LTAASNSALF KLYGKTCEID GDDLLRTYFP
DVPLSNTLRF EGLANRNSLP YADVYGLEPL DSIRTIFRGT LRYPGFADLM HSLKSIGLLE
VSTAVNPHDW HSLVRAALEQ KLGTLIMNDP RSLKSAIDDV ISPKQHDVVL EALHWLSIVP
PSLSEYALGT SADCSLPPLP SKPTAPIDLF AALLAHKLRY APHERDLVVL SHEIVTRPKG
SQVPLTAPSI GEEEIHTSSL VTYGTKDASA MSRTVGLPVA FAALQIVDGG VSARGVQGPT
SKEVYENVLR RLEEVGLGMR ENVRKVTAGN ALGISVEESL RRRWRVMQEM F
//