ID A0A157SGQ4_9BORD Unreviewed; 730 AA.
AC A0A157SGQ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:SAI69617.1};
GN ORFNames=SAMEA3906486_02606 {ECO:0000313|EMBL:SAI69617.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI69617.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI69617.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI69617.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FKIF01000006; SAI69617.1; -; Genomic_DNA.
DR RefSeq; WP_066128818.1; NZ_FKIF01000006.1.
DR AlphaFoldDB; A0A157SGQ4; -.
DR STRING; 288768.SAMEA3906486_02606; -.
DR OrthoDB; 8664175at2; -.
DR Proteomes; UP000076848; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076848}.
FT DOMAIN 9..104
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 730 AA; 75663 MW; 883CF73BEC500BD6 CRC64;
MPLPDLDSFL SPRSIAIVGA SSNPAKIGAV PVRYLVEHGY DGAIYPINAR ADQIEGRRAY
PSLRAVEAPI DLAVFAIPAS SVDAALDDAI AARVKNIVMF SAGFAEMGKE GEQAQAEFAA
RAKAAGIRVL GPNCLGFMNV ARAVYATFSP VVGTGANEPG SVGIVSQSGA FGAYAYAMSR
ERGLGLSAWI TTGNESDIGV ADCIAWMARD PATRVIMAYL EGCKDGRKLR DALDLARAAG
KPVVVVKVGR TELGALTAAS HTAALAGDDA VFDALFRQHG AYRARNIEEF FDVAHGLAVA
GLPPNKQVGL LTVSGGVGVM MADEAADAAL EVTALPAAAQ AMIHARVPLA ATHNPVDITG
QVTAEPDLLE ATARIMLGEA GHGSLLIFLA AFGATPAMRI LQQQMAQALR NDFPGRLIIF
STLADTAQQR ALEAAGCLSF TDPARAVRVM AAMQFFIRHA DRVSRSDAET SWPGAIAAMP
APQDASAAPG PLRRVAHNEA DALGTLRAYG IPTVPFHRAN SPDEVIAGAR SLGFPVAMKV
LSADITHKSD VGGVVLDIRD ADEAVAAHAR ILDAARSSAP NARIDGVLVA RMVRGGVECI
LGARRDPALG VVVMLGSGGV TVELLGDVTF RLAPVDIGQA RAMVGELRTA RLLQGFRGKP
PCDVEALAEA IVRLSRFALA AGDSLESVEL NPFVVLPAGQ GALALDAVLL TAPPATANAS
SPAFAPSVSF
//
