ID Q63MN2_BURPS Unreviewed; 567 AA.
AC Q63MN2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:CAH38075.1};
GN OrderedLocusNames=BPSS0618 {ECO:0000313|EMBL:CAH38075.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38075.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38075.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38075.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; BX571966; CAH38075.1; -; Genomic_DNA.
DR RefSeq; WP_011205437.1; NZ_CP009537.1.
DR RefSeq; YP_110639.1; NC_006351.1.
DR AlphaFoldDB; Q63MN2; -.
DR STRING; 272560.BPSS0618; -.
DR KEGG; bps:BPSS0618; -.
DR PATRIC; fig|272560.51.peg.6801; -.
DR eggNOG; COG0365; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
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:UP000000605}.
FT DOMAIN 45..404
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 455..532
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 544..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 63495 MW; 80DE08957B36FE63 CRC64;
MTAQAFLDAR DFLLRHRTDY DTAYRDFRWP ALDEFNWALD YFDAIARGND KPALWIVDAA
SGDGARYSFA QMSERSARIA NWLREIGVAR GERILLMLPN RVELWDTMLA AMKLGAVVLP
ATTQLSADDV RERVQIGGAR YAIVDEHEAE KFEQPGLDVT KIVAGAPRAG WLALADGYRA
PAEFAPDART RASDPMLLYF TSGTTSKPKL VEHTHRTYPV GSLSTMYWVG LQPGDIHWNI
SSPGWAKHAW SCFYAPWNAQ ACVFAFNYAR FEPKVVLDAL VKYQVTTMCA PPTVWRMLVQ
QPLSTFAVKL REIVGAGEPL NPEIIERVRK AWGVTIRDGY GQTETTYLIG NSPGQPVVPG
SMGRPLPGYA IALLDPDGAH ASEGEIALPV GPDVERPVGL MKGYASNPEA TAHAMRDGHY
RTSDIALRRD DGYFVYVGRA DDVFKSSDYR LSPFELESVL IEHEAIAEAA VVPSPDPVRL
SVPKTFVMLR AGYEPSETLA REIFRFSREK LAPYKRIRRL QFAELPKTIS GKIRRVELRR
RELERGDDAS SRMPGEYWEE DFAADGK
//
