ID A0A1D8G205_9ACTN Unreviewed; 656 AA.
AC A0A1D8G205;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A4G23_02324 {ECO:0000313|EMBL:AOT59482.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT59482.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT59482.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT59482.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017316; AOT59482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8G205; -.
DR STRING; 285473.A4G23_02324; -.
DR KEGG; srn:A4G23_02324; -.
DR PATRIC; fig|285473.5.peg.2431; -.
DR Proteomes; UP000095349; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349}.
FT DOMAIN 444..482
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 66686 MW; FB11AFD216AA4463 CRC64;
MTGTGAGAAT AGPGAGAGAG GAATGAGAGA VPGLEALFRP RAVALLGSGD GRDAVVAWAL
GRGARVYAVR GEAAAGVLPA GSVAELPEDV DLAVVLGGDP LPVLRQLADA KVPLAVALGP
SASTDRLRGG ATRVLGPTDA AQFQPLRDDP AGPGLAVVVP SGPAGRHLYA LQELGVRVSH
WAVTGGEADL TAADLLAYCA EQPGVGAVAL HLDALRDAPA LLRAADHAAL HGVPVVALPA
PADPATAPVL QAALRQHGVV PVGSPDQLRD TAVLLARARP PRAEGIAVYD DGSSAAAPFA
ALARAAGLPA EARPGAPLEA LLADPDTGLV VCPVPAAHPP HTDLLARALA DAAETTDKPV
CVVWGSPDGT EPAYRKTLLG SSRLVVFRTT ANCVAALAAY TAHHRRAAAH RSPYEEAPEA
PSPSARKARP LLRPGHRLSE HAAKQLLRAY GVRVPREQLV TSAAAAVRAA AQIGYPVVLK
ASAPQLSRRA ELGLVRVGVT SASQVRDTYR DLAEIARYDR VDLDGVLVCQ MVERGAELSI
RVGHDPLFGP TVTLGTGGAL AEVVADTAVR VPPFGEREAR SMLDELRLRR LLDGTGGGPP
LDADALVEAV LRVRRIAQEL GGELAELAVD PLVVRERGQG AVALGAHALC RPATPA
//
