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Database: UniProt
Entry: A0A1Q7HY86_9CHLR
LinkDB: A0A1Q7HY86_9CHLR
Original site: A0A1Q7HY86_9CHLR 
ID   A0A1Q7HY86_9CHLR        Unreviewed;       214 AA.
AC   A0A1Q7HY86;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN   ORFNames=AUH85_06630 {ECO:0000313|EMBL:OLC56392.1};
OS   Chloroflexi bacterium 13_1_40CM_4_68_4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC56392.1, ECO:0000313|Proteomes:UP000185706};
RN   [1] {ECO:0000313|EMBL:OLC56392.1, ECO:0000313|Proteomes:UP000185706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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:OLC56392.1}.
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DR   EMBL; MNFM01000068; OLC56392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7HY86; -.
DR   Proteomes; UP000185706; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic 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; 1.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
PE   4: Predicted;
FT   DOMAIN          4..99
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   214 AA;  22393 MW;  113FA8351AEB7171 CRC64;
     MSVLVTERTR VIVQGVGREG RFHAAQMRKY GTKVVAGVKP GAGGTSIDEL PMYDTVHAAV
     EATEANASII FVPAAAAADA ILEALNEELE LVVAITEWIP VHDMLRIASV LARASTTLVG
     PNCPGVISPG KGKVGILPIE SFSAGSIGFV SRSGTLTYEI ADLLSREGFG QSTCIGIGGD
     PVIGLPMPKA VQLLNEDPAT RPSEIPHLLR EQLS
//
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