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Database: UniProt
Entry: A1RX15_THEPD
LinkDB: A1RX15_THEPD
Original site: A1RX15_THEPD 
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
//
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