ID C0QAY6_DESAH Unreviewed; 708 AA.
AC C0QAY6;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=SucD3 {ECO:0000313|EMBL:ACN14785.1};
DE EC=6.2.1.13 {ECO:0000313|EMBL:ACN14785.1};
GN Name=sucD3 {ECO:0000313|EMBL:ACN14785.1};
GN OrderedLocusNames=HRM2_16770 {ECO:0000313|EMBL:ACN14785.1};
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:ACN14785.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14785.1, 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; ACN14785.1; -; Genomic_DNA.
DR RefSeq; WP_015903572.1; NC_012108.1.
DR AlphaFoldDB; C0QAY6; -.
DR STRING; 177437.HRM2_16770; -.
DR KEGG; dat:HRM2_16770; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_7; -.
DR OrthoDB; 9791027at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:ACN14785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT DOMAIN 7..102
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 708 AA; 75679 MW; 85BB8FA5648EE327 CRC64;
MDKLDAIFAP ESIAVIGAST QKGKVGHDIF ANILFGGFKG TIYPVNPKAK SIIGVKCYTS
VTNIPDPIDL AMVILPPKLA LNAVKECIAK GVKGVVIVSA GFKEVRGEGA EIEEQIKAVC
RAANIRLVGP NCLGVINPSP DVSLNASFSS RMPTAGNVSF ISQSGALCTA VLDFAADKGF
GFSKFISIGN KADVDELDLL RYYHKDPNTD VVMIYMEELS RGAEEFISEV REMTSGVNPT
PVIAIKSGTS VAGAAAAASH TGALAGSDAI YDSIFFQSGI VRCHTVNELF DYAQALAAKK
IPNGDKIAIV TNAGGPGIIA TDMSENSGLS LARFSDETIS ELHKYLPPTA NFHNPVDVIG
DAARDRYENT LATVLSDPGV DGVLIILTPQ SMTDAMGTAE AIVNIARNAI KPIVCSFMGV
VDVSDGVKLL QRNHVPVYQF PESAARAMGV LYRSKQWLSR KILPEYAVVH DVERAGRIVQ
DCMDRGQTTM GELDGSELLA CYGFKTLDMA LAKTRAEAIQ IAGRIGYPVV MKIVSEQILH
KSDAKAVMVG IVTPDEAGEA FDKIMANAEA YNSMAKLDGV LVQESAKKGR EVILGVSRDD
VFGHAVMFGL GGIFVEVYKD VVFRMAPMGR NVARRMVKGI KGYPLLAGVR GEAPADIEAL
EKNLVSLRAM VTDYPVIKEL DINPLFVHEA GEGTTVADVI IKFEPLKK
//
