ID A1RX15_THEPD Unreviewed; 508 AA.
AC A1RX15;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 28-JUN-2023, entry version 74.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:ABL77745.1};
GN OrderedLocusNames=Tpen_0336 {ECO:0000313|EMBL:ABL77745.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77745.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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DR EMBL; CP000505; ABL77745.1; -; Genomic_DNA.
DR RefSeq; WP_011752010.1; NC_008698.1.
DR AlphaFoldDB; A1RX15; -.
DR STRING; 368408.Tpen_0336; -.
DR EnsemblBacteria; ABL77745; ABL77745; Tpen_0336.
DR GeneID; 4601703; -.
DR KEGG; tpe:Tpen_0336; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_3_2; -.
DR OMA; ASHTGKL; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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; 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; 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; 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:UP000000641}.
FT DOMAIN 9..108
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 508 AA; 55161 MW; 498581F86E2118DF CRC64;
MTSESLKPFF DPRGVVVVGA SREEEKPGHV IFRVLLENRK KGLLKAPVYG VNPKADYILG
EKVFPSVKDI PGEVDLAVIV IPAEHVKRAI EDLGVKGIKA AIIISAGFSE IGRSDLEREV
AETAKKHGIR IIGPNCIGVY SPWSGVDTIF LPYTKVLEDG REVLNAPRPS KGFVALISQS
GAVGTAALDY MYGEGIGLSH FVSIGNKADV DEVELVEYLG GDDRTRVILL YLENIKRGRE
FIEVAGKVTL KKPVVVLKAG RTSAGRRAAA SHTAALAGVD EVYDAAFRRS GVIRANDIEE
LFDYAKALAM QPPARGERIG IITDGGGAGV MATDIAEMLG LKVPELQGNA RRELEELRER
GIFPRYAQLS NPVDLTGSAT SEMFVEATRI LLESDEVDAV VVLALHQVPG IPDPVKLARE
ISRLAAGYAK PVVAVDTGWS EAAILERKEF DSMGVPSYPT PERAVKSLSA LVRYGKYLSS
RGALGRYLQE YLDFKRKNIL QMHKNNST
//