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Database: UniProt
Entry: A0A2G8SFW1_9APHY
LinkDB: A0A2G8SFW1_9APHY
Original site: A0A2G8SFW1_9APHY 
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
//
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