ID A0A101WI10_9FIRM Unreviewed; 222 AA.
AC A0A101WI10;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acetyl-CoA synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=APF81_27370 {ECO:0000313|EMBL:KUO73397.1};
OS Desulfosporosinus sp. BRH_c37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO73397.1, ECO:0000313|Proteomes:UP000053148};
RN [1] {ECO:0000313|EMBL:KUO73397.1, ECO:0000313|Proteomes:UP000053148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO73397.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO73397.1}.
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DR EMBL; LOEW01000217; KUO73397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WI10; -.
DR Proteomes; UP000053148; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 4: Predicted;
SQ SEQUENCE 222 AA; 24465 MW; 232F89BA53E6385D CRC64;
MTENSSLLSW SEAQKLLGSY GISLSGEAVV EVDVCKVAGK YAFPLVLKGY ATFNSHKKEQ
GLVRLGINNE EELTRVYTEL DVQMKGWSGQ NEIVLQPTAS SGIELVIGAR RDPTFGAVLM
FGLGGTLVEV LNEVVFALAP LDLQAALAML ERWPRRQLLD GYRGWPTVDR QELATLLIKL
GHLISEHLEI LEIDLNPVIV GHKGLILVDV RVTVNQRIAE YA
//