ID G0EDE0_PYRF1 Unreviewed; 282 AA.
AC G0EDE0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Lysine biosynthesis enzyme LysX {ECO:0000313|EMBL:AEM38625.1};
GN OrderedLocusNames=Pyrfu_0756 {ECO:0000313|EMBL:AEM38625.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38625.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM38625.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
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}.
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DR EMBL; CP002838; AEM38625.1; -; Genomic_DNA.
DR RefSeq; WP_014026302.1; NC_015931.1.
DR AlphaFoldDB; G0EDE0; -.
DR STRING; 694429.Pyrfu_0756; -.
DR GeneID; 11139224; -.
DR KEGG; pfm:Pyrfu_0756; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR InParanoid; G0EDE0; -.
DR OrthoDB; 33241at2157; -.
DR Proteomes; UP000001037; Chromosome.
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:UP000001037}.
FT DOMAIN 91..277
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 282 AA; 31380 MW; DB977DB434CA43AC CRC64;
MTRVALAYDY LRQEEKLVIE ALREVGLEVK MLPVTEKPFH IGGEPDIDLV VVRTTSMFNG
LYTAAAYESM GIRSINQSRT ILYSGDKALT YSLLARAKIP TPDTYIALGS RAVFEAAKLL
GYPLVDKPPI GSWGRLVSLI YDDFNLVTVV EHREALCNRQ MRIHVMQEYV ETGNKDIRCL
VLGGELLGCI YRIAREGEWR SNVALGGHTE VVDVTPDLEN LVLRAAAVVE GDFVSIDVFE
HPEKGYVVNE VNGIPEFKGF MRATGVNVAR KLAEYVKSLV KA
//
