LYSY_SULAC
ID LYSY_SULAC Reviewed; 350 AA.
AC Q4JAQ3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305};
DE EC=1.2.1.103 {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305|PubMed:23434852};
DE EC=1.2.1.106 {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305|PubMed:23434852};
GN Name=lysY {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000303|PubMed:23434852};
GN Synonyms=argC {ECO:0000312|EMBL:AAY80126.1}; OrderedLocusNames=Saci_0750;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23434852; DOI=10.1038/nchembio.1200;
RA Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H.,
RA Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C.,
RA Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.;
RT "Lysine and arginine biosyntheses mediated by a common carrier protein in
RT Sulfolobus.";
RL Nat. Chem. Biol. 9:277-283(2013).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000255|HAMAP-Rule:MF_02083,
CC ECO:0000305|PubMed:23434852}.
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, ECO:0000305|PubMed:23434852};
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, ECO:0000305|PubMed:23434852};
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, ECO:0000305|PubMed:23434852}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305|PubMed:23434852}.
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,
CC ECO:0000305}.
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DR EMBL; CP000077; AAY80126.1; -; Genomic_DNA.
DR RefSeq; WP_011277628.1; NC_007181.1.
DR AlphaFoldDB; Q4JAQ3; -.
DR SMR; Q4JAQ3; -.
DR STRING; 330779.Saci_0750; -.
DR EnsemblBacteria; AAY80126; AAY80126; Saci_0750.
DR GeneID; 3473281; -.
DR KEGG; sai:Saci_0750; -.
DR PATRIC; fig|330779.12.peg.719; -.
DR eggNOG; arCOG00495; Archaea.
DR HOGENOM; CLU_006384_0_1_2; -.
DR OMA; PHLTPMI; -.
DR BioCyc; MetaCyc:MON-18313; -.
DR BRENDA; 1.2.1.106; 6160.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001018; 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; IPR023013; AGPR_AS.
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.
DR PROSITE; PS01224; ARGC; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lysine biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..350
FT /note="[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate
FT reductase"
FT /id="PRO_0000112497"
FT ACT_SITE 150
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 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
SQ SEQUENCE 350 AA; 39174 MW; F1A570AA45451FB8 CRC64;
MIRVAVIGGS GYTGGELLRL LAMHNKVEVT YITSREYAGK PISIIHPNLR GFYNINFSQF
SWDKIGEKAE AVFLALPHKV SVDYVPKLLE MGLQVVDLSA DFRLKNPELY KLWYEFDHPY
PDLLKKAVYG IPEIHYEELK GAKLIASPGC NSTATILAAA PLVYSNILDN YRLISDVKVG
SSEGGAKPSE GSHHPERQNA IRPYEAEGHR HAAEVEQELQ YISKKEVKIS LVPHAVSTIR
GALASVHGWL ISDDLNEIEF WKKIIEFYRG RKFVRVIRGN IHPYPDPKYV IGSNFVDIGF
AVEKRVGRIT MFSAIDNLMK GAAGQAVQAF NVSRGFEEDE GLRIPPLRPA
