ID G4E3Z7_9GAMM Unreviewed; 324 AA.
AC G4E3Z7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Alpha-L-glutamate ligase-like protein {ECO:0000313|EMBL:EGZ47991.1};
GN ORFNames=ThisiDRAFT_1026 {ECO:0000313|EMBL:EGZ47991.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ47991.1};
RN [1] {ECO:0000313|EMBL:EGZ47991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ47991.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EGZ47991.1}.
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DR EMBL; AGFD01000015; EGZ47991.1; -; Genomic_DNA.
DR AlphaFoldDB; G4E3Z7; -.
DR STRING; 765914.ThisiDRAFT_1026; -.
DR PATRIC; fig|765914.3.peg.1028; -.
DR eggNOG; COG0189; Bacteria.
DR OrthoDB; 336227at2; -.
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 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011758; RimK-rel_E_lig.
DR InterPro; IPR039523; RimK-rel_E_lig_ATP-grasp.
DR NCBIfam; TIGR02291; rimK_rel_E_lig; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF14397; ATPgrasp_ST; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:EGZ47991.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 52..303
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 324 AA; 35717 MW; 7495066B203EDFCC CRC64;
MNWLRHLRWP LISPKRLAEI GILGMNGRNI DFISRYNPRH CYPLVDDKLK TKLLAQQHGL
STPQLRLIIQ SQHQVNHLAQ ALADLSAFVI KPARGSGGKG ITVITQRDGE QFLKASGQAL
SLGDLQRHLS NILAGIYSLA GAPDIAIIED LIQPDPYFRD YSYEGVPDIR VIVFKGYPVM
SMLRLSTHAS DGKANLHQGA VGVGLDIASG RAIYAVQFGR RVEQHPDTQR PLVEICPPHW
STILTLAVRC QQMTGLGYLG ADIVLDAQHG PTMLELNARP GLAIQVANGC GLLPRLRHIE
GLSQAHNTPH DCVNYAMQQF ATFK
//