ID C0QDM4_DESAH Unreviewed; 487 AA.
AC C0QDM4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN OrderedLocusNames=HRM2_21900 {ECO:0000313|EMBL:ACN15288.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15288.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN15288.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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DR EMBL; CP001087; ACN15288.1; -; Genomic_DNA.
DR RefSeq; WP_015904057.1; NC_012108.1.
DR AlphaFoldDB; C0QDM4; -.
DR STRING; 177437.HRM2_21900; -.
DR KEGG; dat:HRM2_21900; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_2_3_7; -.
DR OrthoDB; 9791027at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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:UP000000442}.
FT DOMAIN 14..109
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 487 AA; 51863 MW; BD6BF48C2568D1EE CRC64;
MIPSSIENSE IYPIANPGSI AFFGASNNLA AMGTTVLGCI CAMGYAGKIY PVHPKDREIK
GFQAFQRVSD LPEIPDLAYI VLPTPVVVET LEACGQLGIR HAVIVSAGFN EVGGQGKQLQ
SELTAVAEKY GIRFLGPNCI GVINTHLNLN ATFLPYEAGR GYIGMASQSG SFITQMSPHM
SRLGMGFSTG FSIGNEANVD IVDCMAYLGA CPNTRVIALY IESIRRGRAF IDTARAIVPK
KPIVAFYVGG SDEGRRAGFS HTGALAGPDP LYNGVFRQSG VIRASSIEEL FDFCYVLGAS
PPIQGNRVIV QTHSGGPGAA AADACGRNGL HLPALTAATL ERLKPHVPHT ASVANPVDLT
FTKTPLDFFQ TIPQILTADE NADALLIYFL ATSRMIQVVL EALGVSDDMS GDKAEEIIIQ
QADAIAALGE QIKKPIVGFS FLARKESSLI RALQDRGIPV LPSPERGARA LAALVKYKNL
REKLTQG
//
