ID A0A0F7VT13_9ACTN Unreviewed; 709 AA.
AC A0A0F7VT13;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Uncharacterized protein MJ0590 {ECO:0000313|EMBL:CQR60642.1};
GN Name=sle_11800 {ECO:0000313|EMBL:CQR60642.1};
OS Streptomyces leeuwenhoekii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1437453 {ECO:0000313|EMBL:CQR60642.1, ECO:0000313|Proteomes:UP000035016};
RN [1] {ECO:0000313|EMBL:CQR60642.1, ECO:0000313|Proteomes:UP000035016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C34 (DSM 42122 / NRRL B-24963)
RC {ECO:0000313|Proteomes:UP000035016};
RA Gomez-Escribano P.J.;
RL Submitted (FEB-2015) 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; LN831790; CQR60642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7VT13; -.
DR KEGG; sle:sle_11800; -.
DR Proteomes; UP000035016; Chromosome Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP 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; 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.
PE 4: Predicted;
FT DOMAIN 253..348
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 709 AA; 74771 MW; F125B14DEC47FB32 CRC64;
MLRVRALLDS VRAEGRTALT APEGKVVAKA YGIAVPGEEL ARDVEEAVAC AARFGGPVVL
KIVSPDILHK SDAGGVVVGV EGAARVRAAF RRIVDNARAY APEARIHGVQ VQELLPRGQE
VIVGAVTDPT FGKVVAFGLG GVLVEVLKDV TFRLAPVDAD EALSMLDSIR AAQVLDGVRG
QPAVDRRAVA EQIRRVSELV ADFPEIAEVD LNPVIATARG AVAADVRVIL AESLPPVRRS
YTREEILTSM RRLMRPSSVA VIGASGEPGK IGNSVMRNLV DGGFPGEIHP VNPKADDILG
RKAYKSVTDV PGEVDVAVFA IPARFVAAAL EEVGRRKIPN AVLIPSGFAE IGEHALQAEI
VAIAERHGVR LLGPNIYGYY STWQDLCATF CTPYDVKGGV ALTSQSGGIG MAVLGFARST
KTGVSAIVGL GNKSDVDEDD LLTWFCEDPH TECIAMHLED LKDGRAFVEA ARATVPRKPV
VVLKAGRTAA GARAAGSHTG ALAGDDAVYD DILRQAGVIR APGLKEMLEY ARALPVLPTP
KGDNVVVITG AGGSGVLLSD AVTDNGLSLM EIPSDLDTAF RAFIPPFGAA GNPVDITGGE
PPSTYEATIR LGMEDPRIHA LVLGYWHTIV TPPMVFAELT ARVVEEFRAR GVEKPVVASL
AGDVEVEEAG RYLFERGVVA YPYTTEMPVA VLGAKYRWAR AAGLLGGGS
//
