LYSW_SULTO
ID LYSW_SULTO Reviewed; 56 AA.
AC Q976J8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-aminoadipate/glutamate carrier protein LysW;
DE AltName: Full=AAA carrier protein LysW;
GN Name=lysW; OrderedLocusNames=STK_01925; ORFNames=STS023;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ZINC AND ARGX,
RP FUNCTION, GLUTAMYLATION AT GLU-56, AND SUBUNIT.
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: Carrier protein that bears the covalently bound substrates
CC for arginine and lysine biosynthesis; bound L-glutamate is sequentially
CC converted to L-ornithine, while bound alpha-aminoadipate (AAA) is
CC sequentially converted to L-lysine. {ECO:0000269|PubMed:23434852}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23434852}.
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. Formation of an isopeptide
CC bond between the gamma-carboxyl group of the C-terminal glutamate and
CC the amino group of L-glutamate is catalyzed by ArgX. The bound
CC substrate is then sequentially converted to ornithine which is
CC eventually converted to L-arginine (PubMed:23434852).
CC {ECO:0000269|PubMed:23434852}.
CC -!- MISCELLANEOUS: Binds zinc ions via its zinc finger domain, as shown by
CC X-ray crystallography (PubMed:23434852). In contrast, the absorption
CC spectrum of the ortholog from Thermophilus suggests that it may bind
CC iron ions, possibly via the predicted zinc finger domain.
CC {ECO:0000305|PubMed:23434852}.
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DR EMBL; BA000023; BAB65149.1; -; Genomic_DNA.
DR RefSeq; WP_010978131.1; NC_003106.2.
DR PDB; 3VPB; X-ray; 1.80 A; E/F=1-56.
DR PDBsum; 3VPB; -.
DR AlphaFoldDB; Q976J8; -.
DR SMR; Q976J8; -.
DR DIP; DIP-61748N; -.
DR IntAct; Q976J8; 1.
DR STRING; 273063.STK_01925; -.
DR EnsemblBacteria; BAB65149; BAB65149; STK_01925.
DR GeneID; 54121838; -.
DR KEGG; sto:STK_01925; -.
DR PATRIC; fig|273063.9.peg.236; -.
DR eggNOG; arCOG01588; Archaea.
DR OMA; EIVEHEC; -.
DR OrthoDB; 123863at2157; -.
DR UniPathway; UPA00033; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd13946; LysW; 1.
DR InterPro; IPR005906; LysW.
DR PANTHER; PTHR40393; PTHR40393; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis;
KW Isopeptide bond; Lysine biosynthesis; Metal-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..56
FT /note="Alpha-aminoadipate/glutamate carrier protein LysW"
FT /id="PRO_0000084538"
FT ZN_FING 1..34
FT /note="TFIIB-type"
FT MOTIF 50
FT /note="EDWGE"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 56
FT /note="5-glutamyl 2-aminoadipic acid; alternate"
FT /evidence="ECO:0000269|PubMed:23434852"
FT MOD_RES 56
FT /note="5-glutamyl glutamate; alternate"
FT /evidence="ECO:0000269|PubMed:23434852"
FT MOD_RES 56
FT /note="5-glutamyl N2-lysine; alternate"
FT /evidence="ECO:0000305"
FT MOD_RES 56
FT /note="5-glutamyl N2-ornithine; alternate"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3VPB"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3VPB"
SQ SEQUENCE 56 AA; 6104 MW; C72792074AD8585A CRC64;
MVVLKCPVCN GDVNVPDDAL PGEIVEHECG AQLEVYNDHG RLALRLAEQV GEDWGE
