ID A0A1H3EAV6_9ACTN Unreviewed; 727 AA.
AC A0A1H3EAV6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SDX75029.1};
GN ORFNames=SAMN05661080_01046 {ECO:0000313|EMBL:SDX75029.1};
OS Modestobacter sp. DSM 44400.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1550230 {ECO:0000313|EMBL:SDX75029.1, ECO:0000313|Proteomes:UP000199500};
RN [1] {ECO:0000313|EMBL:SDX75029.1, ECO:0000313|Proteomes:UP000199500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44400 {ECO:0000313|EMBL:SDX75029.1,
RC ECO:0000313|Proteomes:UP000199500};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNOZ01000005; SDX75029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3EAV6; -.
DR STRING; 1550230.SAMN05661080_01046; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000199500; Unassembled WGS sequence.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000199500}.
FT DOMAIN 28..123
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 73811 MW; A24EE3E278E0CFA1 CRC64;
MPVPQPPPQL ETSGDRSSAP RSEELQALLR PRGIALLGIS GRSDNLMARP LRYLVEHGYS
GAIYPINPKY DELVGQKCYP TLAHVPGPVD LVLVLVAAEA VEDAIRQAAA AGATAAVVYA
SGFAEVGPEG VALQQRLAAV ARETGVRVLG PNCQGFLYAP TGVVATFTAA ADRPLASDSG
VAYVGQSGAV GGSVLDLATD MGLGLAAWAS TGNQADLGLV EVSRALLEDP AVRVLMLYVE
AAGDGKAYAA LARQARTAGK HLVVLRSGRS SAGRRAVASH TGSMLGDDVA FVLTSREHGV
VLVDDIDELL SVAAVLATGK RSEGRRVVVV TTSGGAGSLA ADLCEDLGLE LPELSAETQD
RLRPLIPAFG ALTNPVDVTA QLFNRGAHAF GDVCRIVADD PSVDAVAVFV TMVVGEAGAR
LAEDLVVTAG KLATPLLVGW IAGQELTTAG RAAFREAAIP VFGSVGDLVR CAARLAPPPY
RGAAPVLSPA PGLPAEAVRA QLAAPVVDGP ALLRAIGVAQ PASTLVTTPE AARAAVAALP
GPGVLKLSAG ELAHKSDVGG VRVGVATDEA AQVFTELLDA ATRHRVPDVA GVLVQELIPP
GIELIIGATA GQDGFPPVVT VGLGGVTTEL YRDIASGLAP VSPEQAWTML RSLRAWPLLA
GFRGAPPADV PAAVDAVVRL SEAVVAAGNR LTELEVNPLI VAARGGGATA VDVLVGVGTG
PSAPLGE
//