LYSW_SACS2
ID LYSW_SACS2 Reviewed; 56 AA.
AC Q980W8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-aminoadipate/glutamate carrier protein LysW;
DE AltName: Full=AAA carrier protein LysW;
GN Name=lysW; OrderedLocusNames=SSO5317;
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 FUNCTION IN LYSINE BIOSYNTHESIS, AND INDUCTION.
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: 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:0000250,
CC ECO:0000269|PubMed:12042311}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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DR EMBL; AE006641; AAK40504.1; -; Genomic_DNA.
DR EMBL; BK000545; DAA00052.1; -; Genomic_DNA.
DR PIR; A90156; A90156.
DR RefSeq; WP_009990383.1; NC_002754.1.
DR AlphaFoldDB; Q980W8; -.
DR SMR; Q980W8; -.
DR STRING; 273057.SSO5317; -.
DR EnsemblBacteria; AAK40504; AAK40504; SSO5317.
DR GeneID; 44129120; -.
DR KEGG; sso:SSO5317; -.
DR PATRIC; fig|273057.12.peg.155; -.
DR eggNOG; arCOG01588; Archaea.
DR HOGENOM; CLU_195720_1_0_2; -.
DR InParanoid; Q980W8; -.
DR OMA; EIVEHEC; -.
DR PhylomeDB; Q980W8; -.
DR UniPathway; UPA00033; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001974; 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 Amino-acid biosynthesis; Arginine biosynthesis; Isopeptide bond;
KW Lysine biosynthesis; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..56
FT /note="Alpha-aminoadipate/glutamate carrier protein LysW"
FT /id="PRO_0000084537"
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 /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="5-glutamyl 2-aminoadipic acid; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q976J8"
FT MOD_RES 56
FT /note="5-glutamyl glutamate; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q976J8"
FT MOD_RES 56
FT /note="5-glutamyl N2-lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q976J8"
FT MOD_RES 56
FT /note="5-glutamyl N2-ornithine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q976J8"
SQ SEQUENCE 56 AA; 6065 MW; 59C8A2C54D96C676 CRC64;
MVNLKCPICG GEITVEDDAL PGELVEHECG AQLEVVKQNG KLSLRLAEQI GEDWGE
