ID Q2L081_BORA1 Unreviewed; 554 AA.
AC Q2L081;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:CAJ48779.1};
GN OrderedLocusNames=BAV1171 {ECO:0000313|EMBL:CAJ48779.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48779.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ48779.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ48779.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; AM167904; CAJ48779.1; -; Genomic_DNA.
DR RefSeq; WP_012416853.1; NC_010645.1.
DR AlphaFoldDB; Q2L081; -.
DR STRING; 360910.BAV1171; -.
DR GeneID; 41393074; -.
DR KEGG; bav:BAV1171; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_4; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000001977; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT DOMAIN 38..387
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 455..535
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 554 AA; 61351 MW; FF3CC36AD5C5B1EA CRC64;
MNDQYQSLYQ SFRWLVPTQF NIADVCCHRW ATSGADARRI AIFYEDEAGN REVWTYARLA
EAANQLAHGL TKMGVERGDR IGVVLGQRPE TVVAHMAIYS VGAVVLPLSP LFGPEALESR
LRDSEARIAI VDAASRANLL AASEHCPHLH QIIGIGFADE RVLPWRSLLA RQPGEFKAVL
TRASDPAILL YTSGTTGAPK GALLPHSVLI GNLPGFVASQ NWFPKQGDVF WSPADWAWTG
GLMDALLPTL YFGHPIVGAR GRFSAERAFE LMERYQVTNT FLFPTALKMM MKSVPEPRSR
HRLALRAIMS AGESVGETVF NWCQDALGVT PNEMFGQTEM NYIVGNSHKR WPARPGSMGR
PYPGHNVAVI DELGHAVAPG EIGEVALNRL DIHGHPDPVL FLGYWRKDAA TADKYTGDWC
RTGDLATVDA DGYLWYAGRA DDVFKSAGYR IGPGEIENCL IAHPAVANAA VVPKPDAERG
ALVKAYVVLT EDYAGEDRNA MTQKLQEHVR ERLAPYEYPK EIEYVEHLPM TTTGKIQRAV
LRRREQERAA NHDV
//
