ID A0A1H3EIP4_9EURY Unreviewed; 355 AA.
AC A0A1H3EIP4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN04487946_102270 {ECO:0000313|EMBL:SDX77794.1};
OS Halobellus clavatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=660517 {ECO:0000313|EMBL:SDX77794.1, ECO:0000313|Proteomes:UP000199170};
RN [1] {ECO:0000313|Proteomes:UP000199170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10118 {ECO:0000313|Proteomes:UP000199170};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02083}.
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DR EMBL; FNPB01000002; SDX77794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3EIP4; -.
DR STRING; 660517.SAMN04487946_102270; -.
DR OrthoDB; 372053at2157; -.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000199170; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199170}.
FT DOMAIN 14..148
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 21..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 319
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
SQ SEQUENCE 355 AA; 37488 MW; B4668E8EC2453ED0 CRC64;
MSSESGAGTD ADYTAAVVGG SGFTGGELLR LLYQHPEFDV VQATSRSKAR KTVGHAHPNL
REMDLRFTSP EELESVDVLF AATPHGVSME HIDRFREAAG TVVDLSADFR LSSEAQYDEW
YDGHVCPEYL EDAEYALPEL NRDNLPGADL IASGGCNATA TILGLKPLFD AGILDGDEQA
VVDVKVGSSE GGAGGGDASS HPERSGIVRP YAPTGHRHEA EIEEFLGLSV SFTVHAVDMT
RGASATCHLF PGAPVSNGDL WSAYRDAYAE EPFMRTVAGG GGVYRYPEPK AVAGTNYGEV
GFEVDPGNRR LVVFSAIDNM MKGSAGQAVH AANIALGIEE TAGLEFTGLH PVGAP
//
