LYSY_PYRCJ
ID LYSY_PYRCJ Reviewed; 351 AA.
AC A3MT41;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000255|HAMAP-Rule:MF_02083};
DE EC=1.2.1.106 {ECO:0000255|HAMAP-Rule:MF_02083};
GN Name=lysY {ECO:0000255|HAMAP-Rule:MF_02083}; OrderedLocusNames=Pcal_0373;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02083}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. LysY sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_02083}.
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DR EMBL; CP000561; ABO07808.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MT41; -.
DR SMR; A3MT41; -.
DR STRING; 410359.Pcal_0373; -.
DR EnsemblBacteria; ABO07808; ABO07808; Pcal_0373.
DR KEGG; pcl:Pcal_0373; -.
DR eggNOG; arCOG00495; Archaea.
DR HOGENOM; CLU_006384_0_1_2; -.
DR OMA; PHLTPMI; -.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001431; Chromosome.
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: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 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 Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lysine biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..351
FT /note="Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate
FT phosphate reductase"
FT /id="PRO_1000076738"
FT ACT_SITE 151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
SQ SEQUENCE 351 AA; 38774 MW; FC45D3C3827C2E80 CRC64;
MKRVCIVGAS GFTGGELLRI LLQHSGVEVV CATSRKFKGE YVYRVHPNLR GFTQLKFVEP
TIDAALKADV VFLALPHGES VKWVPQLYES GVAVFDLSAD FRLKDPNAYV EWYKWPQPHP
YPDLLAKAVY GQPELHREEL VGARLVAVPG CMATASILML APLAKFGLIS APPVVDAKIG
SSGAGAEGSV VDLHSFRTYV VRPYEPVHHR HIAEIEQELS RLAGKEVKVA FTPHAVDIVR
GIFTTGHVFV EKMPTEADLW KYYRALFGDS KFIRIVKDRL GISRYPNVKY VLGSNLVDLG
FELDARMKRV VTFAAIDNLV RGAAGQAVQA FNIAMGFPED EGLRHIPVAP I
