ID A0A1C7ICK4_9FIRM Unreviewed; 706 AA.
AC A0A1C7ICK4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:ANU76573.1};
GN ORFNames=A4V09_12810 {ECO:0000313|EMBL:ANU76573.1};
OS Blautia pseudococcoides.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1796616 {ECO:0000313|EMBL:ANU76573.1, ECO:0000313|Proteomes:UP000092574};
RN [1] {ECO:0000313|Proteomes:UP000092574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL58 {ECO:0000313|Proteomes:UP000092574};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP015405; ANU76573.1; -; Genomic_DNA.
DR RefSeq; WP_065542734.1; NZ_CP065312.1.
DR AlphaFoldDB; A0A1C7ICK4; -.
DR STRING; 1796616.A4V09_12810; -.
DR KEGG; byl:A4V09_12810; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000092574; Chromosome.
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 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; 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; 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:UP000092574}.
FT DOMAIN 6..101
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 706 AA; 76145 MW; F98018EDB782B4CC CRC64;
MDLTKLLKPK SVAVIGASEK EGFGGDVCRN ILSYMEDRSH VYFIHPKRDQ VFGVPCYKSV
TDVPESVDLM VICTSQKTVI PLLREGAAKG CGGAVVFASG YGEVGTDQGR ANEKELMETA
KELGIAVMGP NCAGFVNYVD NVQAFAFISD KRDRKGSVGV VSQSGQLCLS LMDCPGMRFS
YSISAGNGKI VQMEDYMDFL VEDENTKVVS IYIEGVKNAD KFAAVLKKAA DRRKPVVILK
AGRSAKGGAI AASHTGSLSG SDASFDAVLK KFGAIRVDDL EELMAMSLML STLKQMPKQA
TFASMNLSGG ETGICADVGS LNGIEYPDFT EETLASLKAQ LPSYASPNNP LDMTASLSYD
ADLYAGALRT VMDDPNIGMV LIGYTLLLEI ADPAIHYMYE GIEKVVKEKG ENCKPIAMIP
FAENTRNAEY QEKLFNMGVP VLPPTVYAFK ILRRLADFIS YTPENKSLSL AVGQKKSGET
YALSEHDSKK ELGAYGVPVP KEVIVTSAEE AAEFAKDTEE ALVMKVESAD ILHKSDVGGV
KLNIHGSCEA VRAYNDIMES VTSKRPDAKI NGILTVPMLK SGVEMIIGVN NDPQFGPMVM
VGMGGVFVEL FKDVALYPAP ISKAEALDML RSLKSFKLLN GYRGGKKCDI DALCDTIVSI
ADFASANRDT LKELDINPLF VYPEGEGVGV ADALVVKYGS REESRL
//
