ID M0CM21_9EURY Unreviewed; 296 AA.
AC M0CM21;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Lysine biosynthesis protein LysX {ECO:0000313|EMBL:ELZ23422.1};
GN ORFNames=C477_02714 {ECO:0000313|EMBL:ELZ23422.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ23422.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ23422.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ23422.1,
RC ECO:0000313|Proteomes:UP000011657};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily.
CC {ECO:0000256|ARBA:ARBA00006239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ23422.1}.
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DR EMBL; AOIS01000011; ELZ23422.1; -; Genomic_DNA.
DR RefSeq; WP_008892883.1; NZ_AOIS01000011.1.
DR AlphaFoldDB; M0CM21; -.
DR STRING; 1227488.C477_02714; -.
DR PATRIC; fig|1227488.3.peg.539; -.
DR eggNOG; arCOG01589; Archaea.
DR OrthoDB; 33241at2157; -.
DR Proteomes; UP000011657; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011870; LysX_arch.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR02144; LysX_arch; 1.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF2; COENZYME GAMMA-F420-2:ALPHA-L-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000011657}.
FT DOMAIN 96..279
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 296 AA; 32674 MW; 2ADF9C22EE86B499 CRC64;
MTLQVGILYS RIRKDEKLLL NELRERDHEI EKIDVRKQTF DISEAPEEFA DLDIVVDRCL
ATSRSLYATQ FFEAYGIPVI NSHETADICA DKVKNSLALE KAGVPTPATK VAFTKETAME
AIEEFGYPCV LKPVVGSWGR LMAKIDSKDA AEAILEHKAT LGHYEHKVFY VQEFVEKPGR
DIRVLATDGE PIAGMVRSSD HWITNAAKGA ETDVFEPDEE AKELVQKASD AVGGGLLGID
LMETEDGYTV HEVNHTVEFK ALDGAVETDV AGTVVDWLES KAEAATEDKD ELEVSA
//
