ID Q64YZ9_BACFR Unreviewed; 551 AA.
AC Q64YZ9;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Acetyl-coenzyme A synthetase {ECO:0000313|EMBL:BAD47277.1};
GN OrderedLocusNames=BF0528 {ECO:0000313|EMBL:BAD47277.1};
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD47277.1, ECO:0000313|Proteomes:UP000002197};
RN [1] {ECO:0000313|EMBL:BAD47277.1, ECO:0000313|Proteomes:UP000002197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD47277.1,
RC ECO:0000313|Proteomes:UP000002197};
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; AP006841; BAD47277.1; -; Genomic_DNA.
DR RefSeq; WP_005784390.1; NC_006347.1.
DR RefSeq; YP_097811.1; NC_006347.1.
DR AlphaFoldDB; Q64YZ9; -.
DR STRING; 295405.BF0528; -.
DR GeneID; 66330435; -.
DR KEGG; bfr:BF0528; -.
DR PATRIC; fig|295405.11.peg.544; -.
DR HOGENOM; CLU_000022_59_10_10; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 37..409
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 459..539
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 551 AA; 62361 MW; D57EF5D75CC3357F CRC64;
MIDRFLSQTS FSSQEDFVKN LKIHVPDNFN FGYDIVDAWA AEQPDKPALL WTNDKGEHHQ
FSFADMKQYT DRTASYFQSL GIGHGDMVML ILKRRYEFWF SIIALHKLGA VVIPATHLLT
KKDIVYRCNA ADIKMIVAAG EEVVTKHIID AMPDSPTVKH LVSVGPEIPE GFDDFHQGIE
HAAPFVKPEH PNTNDDISLM YFTSGTTGEP KMVAHDFTYP LGHIVTGSFW HNLKENSLHL
TIADTGWGKA VWGKLYGQWI AGANVFVYDH EKFTPADILE KIQNYHVTSL CAPPTIFRFL
IHEDLTKYDL SSLEYCTIAG EALNPAVFDT FKKLTGIKLM EGFGQTETTL TVATFPWMEP
KPGSMGVPNP QYNVDLIDYE GRSVEAGEQG QIVIRTDKGK PLGLFKEYYR DASRTHEAWH
DGIYYTGDVA WKDEDGYLWF VGRADDVIKS SGYRIGPFEV ESALMTHPAV VECAITGVPD
EIRGQVVKAT IVLAKEYRER KGEDLVKELQ NHVKKVTAPY KYPRVIEFVD ELPKTISGKI
RRVEIRKNDE K
//
