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Database: UniProt
Entry: A0A1F7JCB3_9BACT
LinkDB: A0A1F7JCB3_9BACT
Original site: A0A1F7JCB3_9BACT 
ID   A0A1F7JCB3_9BACT        Unreviewed;       281 AA.
AC   A0A1F7JCB3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Lysine biosynthesis enzyme LysX {ECO:0000313|EMBL:OGK53252.1};
GN   ORFNames=A3H78_03015 {ECO:0000313|EMBL:OGK53252.1};
OS   Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_02_FULL_36_11.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802071 {ECO:0000313|EMBL:OGK53252.1, ECO:0000313|Proteomes:UP000177418};
RN   [1] {ECO:0000313|EMBL:OGK53252.1, ECO:0000313|Proteomes:UP000177418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGK53252.1}.
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DR   EMBL; MGAV01000021; OGK53252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7JCB3; -.
DR   Proteomes; UP000177418; 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:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 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}.
FT   DOMAIN          90..274
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   281 AA;  31115 MW;  986F65E3EC2F5E2A CRC64;
     MVIGLLHTTI RTDEKLLIEA AKKRNVKMML IDVRESAFLP SILYNFDVVL ERCVSTTKGN
     YAISFFESLN IPVVNSSRVA AICEDKFLTS LALYKNKVKE PQFAMVFNID QAVITIEKMG
     GYPVVIKPTK GSWGRLLAKV NDSDALETIL EHKTVLGSPQ HKAFYIQQYI DKAGVDIRAF
     VIDGVVISAI SRRSDHWITN TARGGSVENY HVTQSLQDIC KSASYAVGGG VLAIDLMETD
     SGYLVNEINH TMEFKNSEIP TGVSISGAII DYCLKIINKK C
//
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