LYSW_THET8
ID LYSW_THET8 Reviewed; 54 AA.
AC Q5SH22;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Alpha-aminoadipate carrier protein LysW;
DE AltName: Full=AAA carrier protein LysW;
GN Name=lysW; OrderedLocusNames=TTHA1908;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, MUTAGENESIS OF GLU-54, IDENTIFICATION BY MASS SPECTROMETRY,
RP IRON-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19620981; DOI=10.1038/nchembio.198;
RA Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T.,
RA Nishiyama C., Kuzuyama T., Nishiyama M.;
RT "Discovery of proteinaceous N-modification in lysine biosynthesis of
RT Thermus thermophilus.";
RL Nat. Chem. Biol. 5:673-679(2009).
CC -!- FUNCTION: Carrier protein that bears the covalently bound substrates
CC for lysine biosynthesis; the bound alpha-aminoadipate (AAA) is
CC sequentially converted to L-lysine. {ECO:0000269|PubMed:19620981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78 uM for alpha-aminodipate {ECO:0000269|PubMed:19620981};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway.
CC -!- PTM: Formation of an isopeptide bond between the gamma-carboxyl group
CC of the C-terminal glutamate and the amino group of alpha-aminoadipate
CC (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine
CC in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of
CC the product L-lysine is catalyzed by LysK (PubMed:19620981).
CC {ECO:0000269|PubMed:19620981}.
CC -!- MISCELLANEOUS: The purified protein is red, and its absorption spectrum
CC suggests that it binds iron ions, possibly via the predicted zinc
CC finger domain (PubMed:19620981). In contrast, the ortholog from
CC Sulfolobus clearly binds zinc ions via its zinc finger domain, as shown
CC by X-ray crystallography. {ECO:0000305|PubMed:19620981}.
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DR EMBL; AP008226; BAD71731.1; -; Genomic_DNA.
DR RefSeq; WP_011229005.1; NC_006461.1.
DR RefSeq; YP_145174.1; NC_006461.1.
DR PDB; 3WWL; X-ray; 1.20 A; A=1-54.
DR PDBsum; 3WWL; -.
DR AlphaFoldDB; Q5SH22; -.
DR SMR; Q5SH22; -.
DR STRING; 300852.55773290; -.
DR EnsemblBacteria; BAD71731; BAD71731; BAD71731.
DR GeneID; 3167976; -.
DR KEGG; ttj:TTHA1908; -.
DR PATRIC; fig|300852.9.peg.1876; -.
DR eggNOG; ENOG503361X; Bacteria.
DR HOGENOM; CLU_195720_0_0_0; -.
DR OMA; HQIVECP; -.
DR PhylomeDB; Q5SH22; -.
DR UniPathway; UPA00033; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005906; LysW.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR40393; PTHR40393; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR TIGRFAMs; TIGR01206; lysW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Iron; Isopeptide bond;
KW Lysine biosynthesis; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..54
FT /note="Alpha-aminoadipate carrier protein LysW"
FT /id="PRO_0000391002"
FT ZN_FING 1..33
FT /note="TFIIB-type"
FT MOTIF 50
FT /note="EDWGE"
FT BINDING 5
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 8
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT MOD_RES 54
FT /note="5-glutamyl 2-aminoadipic acid; alternate"
FT MOD_RES 54
FT /note="5-glutamyl N2-lysine; alternate"
FT MUTAGEN 54
FT /note="E->A: Disrupts lysine biosynthesis. Lysine-
FT auxotrophic phenotype."
FT /evidence="ECO:0000269|PubMed:19620981"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3WWL"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:3WWL"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3WWL"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3WWL"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3WWL"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3WWL"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:3WWL"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3WWL"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3WWL"
SQ SEQUENCE 54 AA; 5812 MW; 835CEB60AF8C52DE CRC64;
MVGTCPECGA ELRLENPELG ELVVCEDCGA ELEVVGLDPL RLEPAPEEAE DWGE
