LYSJ_SACS2
ID LYSJ_SACS2 Reviewed; 388 AA.
AC Q7SI94; Q980W6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=[LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase {ECO:0000255|HAMAP-Rule:MF_02084};
DE EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_02084};
DE EC=2.6.1.118 {ECO:0000255|HAMAP-Rule:MF_02084};
GN Name=lysJ {ECO:0000255|HAMAP-Rule:MF_02084}; OrderedLocusNames=SSO0160;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12042311; DOI=10.1074/jbc.m203528200;
RA Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W.M., van der Oost J.;
RT "The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine
RT biosynthesis in response to lysine availability.";
RL J. Biol. Chem. 277:29537-29549(2002).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000255|HAMAP-Rule:MF_02084}.
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};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_02084};
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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02084}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=DAA00054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40506.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK000545; DAA00054.1; ALT_INIT; Genomic_DNA.
DR PIR; C90156; C90156.
DR RefSeq; WP_009990385.1; NC_002754.1.
DR AlphaFoldDB; Q7SI94; -.
DR SMR; Q7SI94; -.
DR STRING; 273057.SSO0160; -.
DR EnsemblBacteria; AAK40506; AAK40506; SSO0160.
DR GeneID; 44129122; -.
DR KEGG; sso:SSO0160; -.
DR PATRIC; fig|273057.12.peg.157; -.
DR eggNOG; arCOG00914; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR InParanoid; Q7SI94; -.
DR OMA; PFMVPTY; -.
DR UniPathway; UPA00033; UER00038.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_02084; LysJ_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
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 Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00707; argD; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..388
FT /note="[LysW]-aminoadipate semialdehyde/glutamate
FT semialdehyde transaminase"
FT /id="PRO_0000112830"
FT BINDING 124
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 208..211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
SQ SEQUENCE 388 AA; 43323 MW; E0A2368FDB6E80F2 CRC64;
MIKLLKFYQD RGIKIIKGEG QYVWDEKNNK YLDMHAGHGV AFLGHRNKVI IDHLKKQMEE
ISTLSLAFDT PIREEMIKEL DELKPEDLDN LFLLNSGSEA VELALKIARK ITKRRKIVAF
KNSFHGRSMG ALSVTWNKKY REPFEPLIGP VEFLEYNNVD SLKSITEDTA AVIVEPVQGE
GGVIPAKKEF VKSLREVTEK VNALLIIDEV QTGFGRTGKI WAYQHFDIKP DILTAGKAIG
GGFPVSAVFL PNWISEKIEE GDHGSTYGGN PLAAAAVTAA CKVAKSEKIA EQAQKKGELF
MRILKEKLED FKIVREIRGL GLMIGIDLKV NPSIAIKVLQ DEKVLSLKAG LTTIRFLPPY
LITQSDMEWA SDATRKGISE TESKRVAS
