ID A0A0P9FZ14_9ARCH Unreviewed; 350 AA.
AC A0A0P9FZ14;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase {ECO:0000256|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000256|HAMAP-Rule:MF_02083};
DE EC=1.2.1.106 {ECO:0000256|HAMAP-Rule:MF_02083};
GN Name=lysY {ECO:0000256|HAMAP-Rule:MF_02083};
GN ORFNames=AOA66_0020 {ECO:0000313|EMBL:KPV64718.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV64718.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV64718.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV64718.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {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 -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-glutamyl-5-
CC semialdehyde)-L-glutamate + NADP(+) + phosphate = [amino-group
CC carrier protein]-C-terminal-gamma-(5-phospho-L-glutamyl)-L-glutamate
CC + H(+) + NADPH; Xref=Rhea:RHEA:52668, Rhea:RHEA-COMP:13313,
CC Rhea:RHEA-COMP:13327, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136717,
CC ChEBI:CHEBI:136761; EC=1.2.1.106; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02083};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-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:KPV64718.1}.
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DR EMBL; LIHK01000001; KPV64718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9FZ14; -.
DR STRING; 1700836.AOA66_0020; -.
DR KEGG; barb:AOA66_0020; -.
DR PATRIC; fig|1700836.3.peg.962; -.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000050284; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
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 InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
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 Pfam; PF02774; Semialdhyde_dhC; 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}; Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02083};
KW 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}.
FT DOMAIN 2..141
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
SQ SEQUENCE 350 AA; 38622 MW; BBC95A59C82BAB58 CRC64;
MRVGIIGGSG YVGGELLRLL LFHPHVEVTM VTSRKYAGEF VFGVHPNLRG ATRLKFLPLN
LSDIAKNCDL VFTAMPHGSS VNLVPKLLEI GLRVIDMSAD FRLKNPDDYV KWYGWKHVHP
ELLKEAVYGS TELHRQEMKN ARLIACPGCM AVATILGLAP IVKAGVIEKD RIVADAKIGS
SGAGSAPTIG SHHPERFGGV RPYKSVGHRH TAEIEQELNL LTNEPVTVSF SAHAVNMVRG
ILSTIHVFLT KSLTDKDVWK IYRSFYQGEP FVRLVRYKKG LYRLPDPKVV MGTNFCDVGF
EFDPHTNRLV ILSAIDNILK GASGQGIQCL NVVLGIDEKT ALESMGFHPM
//
