ID LYSJ_SULAC Reviewed; 387 AA.
AC Q4JAP8;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=[LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305};
DE EC=2.6.1.118 {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|PubMed:23434852};
DE EC=2.6.1.124 {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|PubMed:23434852};
GN Name=lysJ {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000303|PubMed:23434852};
GN Synonyms=argD {ECO:0000312|EMBL:AAY80131.1};
GN OrderedLocusNames=Saci_0755 {ECO:0000312|EMBL:AAY80131.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Thermoproteota; 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_02084,
CC ECO:0000305|PubMed:23434852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [amino-group carrier protein]-C-terminal-
CC gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-
CC terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate;
CC Xref=Rhea:RHEA:41952, Rhea:RHEA-COMP:9714, Rhea:RHEA-COMP:9715,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:78501,
CC ChEBI:CHEBI:78526; EC=2.6.1.118; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02084, ECO:0000305|PubMed:23434852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [amino-group carrier protein]-C-terminal-
CC gamma-(L-ornithyl)-L-glutamate = [amino-group carrier protein]-C-
CC terminal-gamma-(L-glutamyl-5-semialdehyde)-L-glutamate + L-glutamate;
CC Xref=Rhea:RHEA:52672, Rhea:RHEA-COMP:13327, Rhea:RHEA-COMP:13328,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:136761,
CC ChEBI:CHEBI:136763; EC=2.6.1.124; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02084, ECO:0000305|PubMed:23434852};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02084};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_02084};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
CC {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|PubMed:23434852}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|PubMed:23434852}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02084}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. LysJ subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02084}.
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DR EMBL; CP000077; AAY80131.1; -; Genomic_DNA.
DR RefSeq; WP_011277633.1; NZ_CP046615.1.
DR AlphaFoldDB; Q4JAP8; -.
DR SMR; Q4JAP8; -.
DR STRING; 330779.Saci_0755; -.
DR GeneID; 78441102; -.
DR KEGG; sai:Saci_0755; -.
DR PATRIC; fig|330779.12.peg.724; -.
DR eggNOG; arCOG00914; Archaea.
DR HOGENOM; CLU_016922_10_1_2; -.
DR BioCyc; MetaCyc:MONOMER-18314; -.
DR UniPathway; UPA00033; UER00038.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-UniRule.
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 CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_02084; LysJ_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR037537; LysJ.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..387
FT /note="[LysW]-aminoadipate semialdehyde/glutamate
FT semialdehyde transaminase"
FT /id="PRO_0000439028"
FT BINDING 96..97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 123
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 207..210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
SQ SEQUENCE 387 AA; 42743 MW; 2CE56671BCBEA5A4 CRC64;
MKLIQLYGDR GLTIVKGEAQ YVWDIEGRRY LDFHTGIGVA FLGHRNPIIL EYLKNQLENI
SILSTSFSTP IKDEMLQALD KVKPDKMDNA MLLNSGTEAV EAALKTARKI TGRKKIIAFK
NAFHGRTAGS LSVTWNKKYR EPFEPLVGPV EFLTFNNIED LSKIDNETAA VIVEPIQGES
GVIPANIEFM KALKEKTENT GSLLIFDEIQ TGFGRTGKLW AYKHYNIVPD ILTAGKAIGG
GFPVSVVFLP DHIANKLEEG DHGSTYGGNP MAMAAVTAAC KVIEKENVVE QANQKGQQFS
NILVKNLADL KVVREVRGKG LMIGIDIRFQ PGQVLKYLQE KGILAVKAGS TVIRFLPSYL
ITYENMEEAS NVLREGLLKI ENKAVSS
//
