LYSJ_PYRAE
ID LYSJ_PYRAE Reviewed; 383 AA.
AC Q8ZV07;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Putative [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=PAE2515;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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}.
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DR EMBL; AE009441; AAL64249.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZV07; -.
DR SMR; Q8ZV07; -.
DR STRING; 178306.PAE2515; -.
DR EnsemblBacteria; AAL64249; AAL64249; PAE2515.
DR KEGG; pai:PAE2515; -.
DR PATRIC; fig|178306.9.peg.1874; -.
DR eggNOG; arCOG00914; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR InParanoid; Q8ZV07; -.
DR OMA; PFMVPTY; -.
DR UniPathway; UPA00033; UER00038.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000002439; 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; 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 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..383
FT /note="Putative [LysW]-aminoadipate semialdehyde/glutamate
FT semialdehyde transaminase"
FT /id="PRO_0000112826"
FT BINDING 97..98
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
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 209..212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
SQ SEQUENCE 383 AA; 42146 MW; A69E88520F3F74A6 CRC64;
MGRIAKYYRE YGIRIVKGFM QYVWDDKGQR YIDCNTNHGV VFLGHANPKI VEAVKKQVEE
IWAVPLNFAT PARERFIEEF SKLLPPKFGV VFLQNTGTEA VEVAIKIAKK VTRKPTIVAF
TNSFHGRTMG SLSITWNEKY KKAFEPLYPH VRFGKFNVPH EVDKLIGEDT CCVVVEPIQG
EGGVNPATPE FLKALREEAQ RKGALLIFDE VQTGFGRTGA VWAFQKYGVE PDIFTAGKPV
AGGLPIGLAV AREDFGDVFE PGEHGSTFAG NAVVMAAAAA ASRLLREEDV PGRAERIGAE
LAKALGDTGS RLAVRVKGMG LMLGLELRVK ADQFIQPLLE RGVMALTAGV NTLRFLPPYM
ISKEDVEVVH AAVTEVLKKA EQQ
