LYSJ_DEIRA
ID LYSJ_DEIRA Reviewed; 429 AA.
AC Q9RW75;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=[LysW]-aminoadipate semialdehyde transaminase {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=DR_0794;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Catalyzes the transfer of the amino group of L-glutamate to
CC [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine.
CC {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 -!- 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 -!- 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=AAF10373.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10373.1; ALT_INIT; Genomic_DNA.
DR PIR; E75474; E75474.
DR RefSeq; NP_294518.1; NC_001263.1.
DR RefSeq; WP_034350363.1; NC_001263.1.
DR AlphaFoldDB; Q9RW75; -.
DR SMR; Q9RW75; -.
DR STRING; 243230.DR_0794; -.
DR EnsemblBacteria; AAF10373; AAF10373; DR_0794.
DR KEGG; dra:DR_0794; -.
DR PATRIC; fig|243230.17.peg.974; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_0; -.
DR InParanoid; Q9RW75; -.
DR OMA; GMTTQIY; -.
DR OrthoDB; 572533at2; -.
DR UniPathway; UPA00033; UER00038.
DR Proteomes; UP000002524; Chromosome I.
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: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; Cytoplasm; Lysine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..429
FT /note="[LysW]-aminoadipate semialdehyde transaminase"
FT /id="PRO_0000112742"
FT REGION 408..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 139
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 226..229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT BINDING 284
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02084"
SQ SEQUENCE 429 AA; 46613 MW; BA614DEDBA7B1025 CRC64;
MTGNEQNPSK WLAAEKKYDS GVYNKHDVVM VRGQGATVWD ENGRSYIDCV VGYGVATLGH
SHPDVVKAVQ EQAGKLMVMP QTVPNDKRAE FLQELVGVLP QGLDRVFLCN SGTEAMEAAK
KFAITATGRS RFVSMKRGFS GRSLGALSFT WEPKYREPFG DAVDNKSVDF VTYGNLDELR
AAVTEQTAAV IMEPVQGEGG VRPASAEFIQ EARRITREKG ALLILDEIQT GFCRTGKMFA
CEHFGVIPDG MTLAKAIAGG TPTAAFAMMS EVADRMPAGG HGTTFGGNPL SMAAGVASLR
AMKREGLAEQ AREKGAYMMD KLRAIQSPKI REVRGLGLMI GVELKEKSAP YIHAMEHDEG
VLCLAATPLV VRFLPPAVIS KEQIDQVVAA FERVLNNVNP REERQAELRA QQSEMGQQQV
SQGESVQTE
