ID A0A1F7TIF8_9BACT Unreviewed; 702 AA.
AC A0A1F7TIF8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=A3J27_04960 {ECO:0000313|EMBL:OGL65367.1};
OS Candidatus Tectomicrobia bacterium RIFCSPLOWO2_12_FULL_69_37.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia.
OX NCBI_TaxID=1802343 {ECO:0000313|EMBL:OGL65367.1, ECO:0000313|Proteomes:UP000176745};
RN [1] {ECO:0000313|EMBL:OGL65367.1, ECO:0000313|Proteomes:UP000176745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGL65367.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGDP01000088; OGL65367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7TIF8; -.
DR Proteomes; UP000176745; 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;
FT DOMAIN 10..105
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 702 AA; 72697 MW; 3AA0C1F582365F65 CRC64;
MSANRSLAAL FTPRSVAVVG ASADLRRLGG IPIRLMRDHA FPGALYPINP NREEIGGFRC
YPDVASLPET PDLALFATPR EGVLAALRQC AGRGVKCAAV FTSGFGETGA EGAALQEEMA
RIARGAGMRL LGPNCMGVIH TRSRLMATFT ISIREGELLS PGPVALVTHS GALAACMISD
LHDAGTGLSA MASLGNEADV DFAECVDHFV DDPDTRVICG YLESVRDGRR LRSAAGRALA
AGKPIVLLKS GATEAGARAA LSHTAALATP HGVFAAFARQ YGVALCRSYQ ELIETADFLA
RAPRTRGRRL GVLSFSGGAG SLVADAAVEE GFALPPLAEA TCARLRAALP PYAAVRNPVD
LVSVMVSKPG ESPIAEAGAA VRDDPEVDAV VLVMGVYHHV AAQVAKELKG LFADSAKPLA
CCWMAPQRAE LQALRKAGVP VFEDYNRAVR ALAAAVSFEE AAAGEAVPKP SSDPARRDRA
LRLIAGASKS PEGMLPPAAC RALLELYGIR QPAQAEASYA EEAVAVWRGM GGPVALKVIA
EGLVHKSDAG GVSLGLDGEG AVRAAAARLL GLAPGARLLV QGMVVGGEVE LLAGLSRDPA
FGLCVTGGIG GIFVEVFEEA ARRLPPFGEK EAGAMLRGLR GAKLLQGVRG RPAVNAAAAA
QVLSRLSEMA AELGEVLAEL DINPLIVTQD DALAVDARVR VV
//
