ID   A0A157SAI3_9BORD        Unreviewed;       705 AA.
AC   A0A157SAI3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:SAI66916.1};
GN   ORFNames=SAMEA3906486_01218 {ECO:0000313|EMBL:SAI66916.1};
OS   Bordetella ansorpii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI66916.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI66916.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI66916.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FKIF01000002; SAI66916.1; -; Genomic_DNA.
DR   RefSeq; WP_066124727.1; NZ_FKIF01000002.1.
DR   AlphaFoldDB; A0A157SAI3; -.
DR   STRING; 288768.SAMEA3906486_01218; -.
DR   OrthoDB; 8664175at2; -.
DR   Proteomes; UP000076848; 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   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:UP000076848}.
FT   DOMAIN          12..107
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   705 AA;  72744 MW;  6C5A7D858B0C7055 CRC64;
     MTTHLDASLS RLFDPRSIAI VGASATPGKI GAMPVTLLRQ YGYAGRIVPI NPRAGEIQGL
     PAFAGLSAVD DAIDLAILAV PAVHAAQALA QARPGQIAGA VIFTSGFSET GDAGRAQQAA
     LTQAARERGI RLLGPNCLGF MNVRKHVYAT FSPAPANGAV APGGIGMVSQ SGAFGAYAYS
     MARERGLGLS HWISTGNEAD IDVADCIAWL ADDADTRVIM AYMEGCRDGD KLRAAFASAR
     AAGKPVVVTK IGRTQAGAQA AASHTAALAG DDAVYDALFR QYGVLRARTI EEFFNLGYAL
     DTWKQPPRGN RLGIFTISGG VGALMADEAA DAGLVLPEPA ADAQARLLAQ VPFASGRNPV
     DVTGQAVSEP GVLLSTAQDM LSDGRYDALA VFLAAAGSSE KLWPTFENFA RQLQASRPDV
     PLAICALFPP ARRRELEQLG CLVFADPSAA VRTIASLAGL AHERTDDAGR PASEAPASQG
     QTLLPSYNEV QAMALLREAG LPATPCTLVG DADGAAAAAA ADIDAPVVLK IVSADIVHKS
     DVGGVKLKLS GEAAVRQAHA SILASVRQHA PQARVDGVLV APMAPAGVEC IAGIHDDPVF
     GPVVMFGLGG VFVEVLKDVS FRLAPFGHGE ALAMIREIKG YAVLRGARGA PPCDLDALAE
     ALVRLSRLAD AQRGRLKSLE INPLLALPHG ALALDAVVIP ASPAG
//