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Database: UniProt
Entry: A0A1H3EAV6_9ACTN
LinkDB: A0A1H3EAV6_9ACTN
Original site: A0A1H3EAV6_9ACTN 
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
//
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