ID F7PP01_9EURY Unreviewed; 311 AA.
AC F7PP01;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:CCQ33666.1};
DE EC=2.3.1.1 {ECO:0000313|EMBL:CCQ33666.1};
DE SubName: Full=Alpha-aminoadipate--LysW ligase LysX protein {ECO:0000313|EMBL:ERJ06744.1};
GN Name=lysX {ECO:0000313|EMBL:ERJ06744.1};
GN ORFNames=HLRTI_001160 {ECO:0000313|EMBL:ERJ06744.1}, HTIA_1539
GN {ECO:0000313|EMBL:CCQ33666.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ33666.1, ECO:0000313|Proteomes:UP000015381};
RN [1] {ECO:0000313|EMBL:ERJ06744.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06744.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ06744.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06744.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ33666.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ33666.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
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DR EMBL; HF571520; CCQ33666.1; -; Genomic_DNA.
DR EMBL; AFNT02000010; ERJ06744.1; -; Genomic_DNA.
DR RefSeq; WP_008527723.1; NZ_AFNT02000010.1.
DR STRING; 1033806.HTIA_1539; -.
DR GeneID; 23799910; -.
DR KEGG; hti:HTIA_1539; -.
DR PATRIC; fig|1033806.12.peg.1527; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR OrthoDB; 33241at2157; -.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
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 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CCQ33666.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:CCQ33666.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Transferase {ECO:0000313|EMBL:CCQ33666.1}.
FT DOMAIN 94..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 237..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 34371 MW; CC6A50A80C4747F7 CRC64;
MNVAILYSRI RQDEKLLLEE LRERDHEVTK IDVRKQRFGL DEPPEDFEDV DLVLDRCLAT
SRSLYATEFL SAYDIPVINS HETAETCADK VTNSLALKQA GVPTPKTEVA FTKDTALEII
EDFGYPCVLK PVIGSWGRLM AKIDTKDAAE AILEHKATLG HYEHKVFYVQ EFVEKPGRDI
RVLATDGEPI AAMVRSSDHW LTNAAKGAET DAFELDDRAR ELVAEASEAV GGGLLGIDLM
ETGGSRSDPQ QSSGEHSDPR DGVDDETGEP TGYTVHEVNH TVEFKALNDA VETDVPGQVV
DWLETNAEVS E
//
