ID   A0A2I1GGS7_9GLOM        Unreviewed;       941 AA.
AC   A0A2I1GGS7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha-aminoadipic semialdehyde synthase {ECO:0000313|EMBL:PKY45837.1};
GN   ORFNames=RhiirA4_518036 {ECO:0000313|EMBL:PKY45837.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY45837.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY45837.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY45837.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:PKY45837.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LLXI01000412; PKY45837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1GGS7; -.
DR   VEuPathDB; FungiDB:FUN_004618; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1595626; -.
DR   VEuPathDB; FungiDB:RhiirA1_513207; -.
DR   OrthoDB; 2184985at2759; -.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000234323; 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; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323}.
FT   DOMAIN          27..158
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          198..393
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   941 AA;  104976 MW;  3494F8F040CAD18B CRC64;
     MNRIPALYHS NSRYLNQTVI RRLNTLALRR EDKSRWERRV ALTPDDVSKL IKETGVKVYV
     QPCNKRVFSN EKYEQAGAVV QEDISIADVI MGIKEVPTKS LIPNKTHIFF SHTHKGQSYN
     MKMLQDILDK KIRLIDYELM TNEEKKRLVL FGTHAGYAGM IDGLHGLGLR LLGLGYNTSF
     MHIAMSHSYK SLDSALSSVK SVGESIATEG LPKDLGPMTF VFTGTGNVSN GAQEIFKHLP
     HEYIDAKDLK ECTSTPHNYN NKKIYGCQVK LQDYLVHKNL GYFISKSDYY ANPNEYECEF
     HTKIAPYTTM LIHGSYWDTR YPRLLTNEHL RAIQADPSNK NRLLAISDIS CDINGALECL
     SHSTTIDDPF YYVDAVNNKE HKNDEGRGTQ IMAVDILPTE IPLESSKHFS KSLYPFMNDL
     INGKIDQNSV LSKATIAKDG KLTDSHRNLY NLLPKSNNSI SSLESRKDNK KILLLGSGFV
     AKPLVDYLSK QEDLSLIIAS NMRAEAIALT RGNQNIQTVD LDVNKKEELS KLVQGADVVV
     SLLPAPLHPI VAEMCITHRK NMVTASYISS EMKALDERAK QAGITILNEI GVDPGIDHLS
     AMKIIDEVKA EGGEVTSFIS WCGGLPAPED SDVPLGYKFS WSPRGTLTAT LNDASFWMNG
     KHQEIPGGAL LKSHFPTVTI YPGLVFEGFA NRDSLSYINT YGLAPLETKS AMFRGTLRYK
     GYSDLMYSFY KLGFLDTNTE ESDFLDHKLF GSYNNEPTEA SRISAIAEKL NLSKNHQMVE
     KVVDALKWLS LIPDSNTSLS SSLIPSTANT STSLDTFCSL LQQKLQYKPG ERDLLVLHHD
     FGIKLKNGEE RTKTSTLVSL GSLDTYTAMA QLVGLPAAIA TEMIVRGEIR DTGILAPTLP
     HIYNPILQNL DRNGVKIVEN TVNNNRGMKG KLNWSGSGIW E
//