ID A0A0N8GQ30_9CHLR Unreviewed; 344 AA.
AC A0A0N8GQ30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Putative [LysW]-L-2-aminoadipate 6-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000256|HAMAP-Rule:MF_02083};
GN Name=lysY {ECO:0000256|HAMAP-Rule:MF_02083};
GN ORFNames=SE15_10535 {ECO:0000313|EMBL:KPL82554.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL82554.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL82554.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL82554.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of [LysW]-
CC aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-semialdehyde.
CC {ECO:0000256|HAMAP-Rule:MF_02083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-N-(1-carboxy-5-
CC oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group
CC carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-
CC yl)-L-glutamine + H(+) + NADPH; Xref=Rhea:RHEA:41948, Rhea:RHEA-
CC COMP:9712, Rhea:RHEA-COMP:9714, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78499,
CC ChEBI:CHEBI:78501; EC=1.2.1.103; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02083};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5.
CC {ECO:0000256|HAMAP-Rule:MF_02083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02083}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. LysY sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_02083}.
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:KPL82554.1}.
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DR EMBL; LGKO01000005; KPL82554.1; -; Genomic_DNA.
DR RefSeq; WP_054522064.1; NZ_LGKO01000005.1.
DR AlphaFoldDB; A0A0N8GQ30; -.
DR STRING; 869279.SE15_10535; -.
DR PATRIC; fig|869279.4.peg.1727; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00033; UER00037.
DR Proteomes; UP000050544; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043870; F:N-acetyl-gamma-aminoadipyl-phosphate reductase activity; IEA:RHEA.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR HAMAP; MF_02083; LysY; 1.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR037535; LysY.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR32338:SF11; [LYSW]-L-2-AMINOADIPATE_[LYSW]-L-GLUTAMATE PHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 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:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_02083}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02083};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02083};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02083};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02083}; Reference proteome {ECO:0000313|Proteomes:UP000050544}.
FT DOMAIN 3..139
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 147
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
SQ SEQUENCE 344 AA; 37658 MW; B53B0764061160CC CRC64;
MIRAAIVGAS GYAGGEVLRL LLDHPEVEVV QVTSRRHLGE YVYQVHPNLR KRTSLKFSDP
AGLEAVDVLF LALPHGEAQH QIDRLAGLAT YIIDLSADFR LKRAEDYEHW YGAPHAAPHW
LGRFVYGLPE LHREDLRGAH YASGVGCNAT AANLALWPLV RADLLDTSQP VVVEIKVGSS
ESGAEGNVGT HHPERSGVIR TFSPFGHRHT AEVIQEMGLE HVVLTMTAVD LVRGALATAH
ARVKAGVSQR DLWRAYRAVV NENPFLRLVK EQRGIYRVPE PKILAGSNYA DLGFELDERT
GHVVSMCALD NLMKGAAGSA VQCMNLMLGL DETLGLTFPG LHPI
//
