ID A0A1Q8BLY1_9CYAN Unreviewed; 223 AA.
AC A0A1Q8BLY1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=ATP-dependent carboxylate-amine ligase {ECO:0000313|EMBL:OLE97038.1};
DE Flags: Fragment;
GN ORFNames=AUG75_12990 {ECO:0000313|EMBL:OLE97038.1};
OS Cyanobacteria bacterium 13_1_20CM_4_61_6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1805100 {ECO:0000313|EMBL:OLE97038.1, ECO:0000313|Proteomes:UP000186597};
RN [1] {ECO:0000313|EMBL:OLE97038.1, ECO:0000313|Proteomes:UP000186597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE97038.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNIV01001754; OLE97038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8BLY1; -.
DR Proteomes; UP000186597; 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 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 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 PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:OLE97038.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 9..219
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OLE97038.1"
SQ SEQUENCE 223 AA; 24198 MW; 2518AC47C8398EC6 CRC64;
TETSKALQLS LLEQLGLPFP AARVINHAAQ VAEAARGLRF PVVLKPNIGG SGAGVRRFET
PEQLEQAAQA AALDLGIDHT ALVQEYIPAA EQRIVRVEVL GGRYLYAIRI YTSGESFNLC
PADVCQTVGG AELVRGACPV DAPRNNLRVE GYTPTPEIVA QVECIMQAAH IDVGGVEYMI
DARDGRLYFY DINALSNFVA DAPRVVGFDP FVRLVDYLER EAV
//
