ID A0A1R1MNI9_9BACT Unreviewed; 655 AA.
AC A0A1R1MNI9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=BLW93_00210 {ECO:0000313|EMBL:OMH41346.1};
OS Desulfurobacterium indicum.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=1914305 {ECO:0000313|EMBL:OMH41346.1, ECO:0000313|Proteomes:UP000187408};
RN [1] {ECO:0000313|EMBL:OMH41346.1, ECO:0000313|Proteomes:UP000187408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K6013 {ECO:0000313|EMBL:OMH41346.1,
RC ECO:0000313|Proteomes:UP000187408};
RA Cao J., Shao Z., Alain K., Jebbar M.;
RT "Genome sequence of a sulfur-reducing bacterium Desulfurobacterium indicum
RT K6013.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMH41346.1}.
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DR EMBL; MOEN01000001; OMH41346.1; -; Genomic_DNA.
DR RefSeq; WP_076712095.1; NZ_MOEN01000001.1.
DR AlphaFoldDB; A0A1R1MNI9; -.
DR STRING; 1914305.BLW93_00210; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000187408; 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:UP000187408}.
FT DOMAIN 220..313
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 655 AA; 73194 MW; 2079B15E34C54320 CRC64;
MRFLSEDKVY EMLDAAGLPV LKHKVFHSYD KIDWDLFPAV VKPLFEKPVH KTEMNAVFEC
LDKKELLKTI SVITKRFPDI DNFIVEEKLH GIEVFLTLKR DSSFGFVAGF GTGGFWVEFL
KDVVFVPNSA TKSQIIQALH KTKLFKLLTG YRNVKGNIEL FVDFVLKFLK IPEKYPELME
VEINPLFVSE NFVLPADGKG FTGDILFRNR KKTSYIDPGL FFPERIAVIG ASKKRDSVGY
AVLKNLSSFT GKIFPVNPKY DEIHGKRCFP SISSIPGKVD CAVIAIPACL VPEVLKECGE
KGVKLAVIIS AGFGERGEEG KTLEKRIRKI SEKFDIRILG PNTLGFIIPS IRLNASFSKI
MPEKGDVAFI SQSGAIITAV LDKAVEKDFG FSSVFSLGNQ LDISVTSLLS SLSTRRENKI
FIVYVEEVKD GYLLFPILKR NPVIFIKAGK SSEGKKATYS HTGALAGDYR VFKDIVTIEG
GIVVDSIDEA LECSRVLSCY GRLKGNRAVV ITNAGGFGAL LADYLSNYGF SLVDIASIKD
KLDSFLPEGW SHINPVDILG DATSLRYEKT FEVMENLDWD VVFVVVTPQY MTDIHSIARE
IVEFHKRVKK PVFPCFIGGY SIKNGIEYVE RNNIPAFDEP LFMVKIASFL KVEPC
//
