ID A0A101FYM7_9CHLR Unreviewed; 697 AA.
AC A0A101FYM7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE SubName: Full=Putative acetyl-CoA synthetase {ECO:0000313|EMBL:KUK46769.1};
GN ORFNames=XD73_0341 {ECO:0000313|EMBL:KUK46769.1};
OS Anaerolinea thermophila.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46769.1, ECO:0000313|Proteomes:UP000064249};
RN [1] {ECO:0000313|EMBL:KUK46769.1, ECO:0000313|Proteomes:UP000064249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46_16 {ECO:0000313|EMBL:KUK46769.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK46769.1}.
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DR EMBL; LGFU01000008; KUK46769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FYM7; -.
DR PATRIC; fig|167964.4.peg.597; -.
DR Proteomes; UP000064249; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion 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; IPR011761; ATP-grasp.
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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 490..526
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 697 AA; 75270 MW; D7E5FB074212B3FE CRC64;
MQDNLSSFFE PQSVALIGAS SNPSKLSYGI LKNISQYGYR GGIYPINPKS NEILGFPCYS
SILDVPEEVD LTVIILPAEI IPQVIDDCGK KGVKACIVIS GGFKELGEDG KQREKELEIS
TRKYGIRIIG PNCVGNINVY SGLNTTFIKG MPVKGGIGFV SQSGAVCGGV VDHVVQEGIG
FSHLISLGNE MDVNETDMIS YLADDENTHV IACYVESIRD GARFMEVAKH VSKKKPIVLL
KAGKSELGAK AVSSHTGSLA GSHTAYSTAF KQAGVIEVSS LRALLQTSMA LDMQPLPQNK
QAVIFTNAGG PAALLSDSLD EHGLKLANLN EKTQQMLKAK LNPAAQTMNP VDMLGGATQG
EYAQAMRVVK ENNDAGILLP VLVPQALVDP VAVARAIISE TQNSQRTTIA CMVGKQSTQE
AKLLLHQQHI PLLDYPEDVG EVLGGMLRYK AYHDAPAETL EISRIAQKEE ARSYFHGLAD
QKQFGEAETR PLLELYGVKN VEGKRADSLA EAQQAAKELG YPVVIKVISD EILHKSDAGG
IRLDIKDERS LADAYQDMLT DVRSHAPEAV IKGVLVEKMQ KQGEEVIVGM KWDANFGALL
MFGMGGIYVE AFKDVSFRIA PVSEVDVRNM IAETAAGKIL NGLRGIRYDI DAVVQTILAL
SQVCLDFPEI QELEINPLKV FSKGDGAAAL DSRMIIK
//
