ID A0A1I4RU76_9PSEU Unreviewed; 702 AA.
AC A0A1I4RU76;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetyl coenzyme A synthetase (ADP forming), alpha domain-containing protein {ECO:0000313|EMBL:SFM55560.1};
GN ORFNames=SAMN05421805_101688 {ECO:0000313|EMBL:SFM55560.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM55560.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM55560.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM55560.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-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; FOUP01000001; SFM55560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4RU76; -.
DR STRING; 455193.SAMN05421805_101688; -.
DR Proteomes; UP000199398; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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}.
FT DOMAIN 22..58
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 702 AA; 73679 MW; 31FE0494617AD88D CRC64;
MREVLDAVRA AGRTALTAPE AKQLCDAYGI PTAGEGLATS ADEAVALARE IGGPVALKIV
SPDILHKTDA GCVLVGVSGD EAVRSGYAEI LANAHAFTEN PAIAGVQVQQ MVSGLEVIVG
ATTDPTFGKV VAFGLGGILV EVLKDVTFRL APLSPEQARS MLDDIAAAEV LRGARGGEPV
DAAALADVLR RVSELVDDFP EISELDLNPV FATAAGAIAA DVRIVLATEP DEAPPQRSQE
EILQAMRRLM NPDSVAVIGA SNEDGKIGNS VMKNLINGGY AGEIHPVNPK ADEILGRTAY
RSITDVPGPV DVAVFTVPAK FVAAALEDCG RKGVAAAVLI PSGFAETGNQ ELQDEVVAVA
RKHGIRLLGP NIYGYYYTPQ NLCATFCTPY DVRGGVALTS QSGGIGMAIL GFSRTTKMGV
SAIVGLGNKS DVDEDDLLTF FEQDDNTHCV AMHLEDLKDG RAFVEAAQRV TKKKPVVVLK
AGRTDLGARA ASSHTGALAG NDKVYDDVLR QSGVVRAPGL NEMLEYARGI PVLPTPKGEN
VVIITGAGGS GVLLSDACVA NGLRLMDIPP DLDAEFRRYI PPFGAAGNPI DITGGEPPST
YEATIRLGLR DPRIHALILG YWHTIVTPPM VFAELAARVA EEARTDGVDK PIVVSLAGDT
EVEKAADYLY DHGIVAFPYT TEKPVAVLGA KYQWARAAGL LD
//
