ID M7NAB6_9BACT Unreviewed; 304 AA.
AC M7NAB6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Alpha-aminoadipate--lysW ligase lysX {ECO:0000313|EMBL:EMR04197.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:EMR04197.1};
GN Name=lysX_2 {ECO:0000313|EMBL:EMR04197.1};
GN ORFNames=ADICEAN_00605 {ECO:0000313|EMBL:EMR04197.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR04197.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR04197.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR04197.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(2013).
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:EMR04197.1}.
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DR EMBL; AODQ01000009; EMR04197.1; -; Genomic_DNA.
DR RefSeq; WP_009194012.1; NZ_AODQ01000009.1.
DR AlphaFoldDB; M7NAB6; -.
DR STRING; 1279009.ADICEAN_00605; -.
DR PATRIC; fig|1279009.4.peg.621; -.
DR eggNOG; COG0189; Bacteria.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000011910; Unassembled WGS sequence.
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:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 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:EMR04197.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT DOMAIN 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 304 AA; 33323 MW; 0AF8E604E68DCAC3 CRC64;
MNIAVLSRNS NLYSTRRLVE AARQRGHECR VLDHLRCDII IEQNNPAIHY KGDLVRGVDA
IIPRIGASVT FYGSAVVRQF EMMNVFTTTK SQAIVRSRDK LRSMQILARS GVGLPKTAFT
NYSREDKYLI EAVGGTPCVI KLLEGTQGLG VVLAETRKAA QSVIEAFHNL KARVIVQEFI
KEAKAADIRA FVIGNEVVGA MRRQGKEGEF RSNLHRGGSA TVYKLNRAEK AAALTAAKAM
GLTIAGVDML QSNRGPLILE VNSSPGLEGI EQATGIDIAS KVIRYIEQEL SAQQPKRKKP
HTDA
//
