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Database: UniProt/TrEMBL
Entry: Q0B2V8_BURCM
LinkDB: Q0B2V8_BURCM
Original site: Q0B2V8_BURCM 
ID   Q0B2V8_BURCM            Unreviewed;       557 AA.
AC   Q0B2V8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ABI91515.1};
GN   OrderedLocusNames=Bamb_5971 {ECO:0000313|EMBL:ABI91515.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI91515.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP000442; ABI91515.1; -; Genomic_DNA.
DR   RefSeq; WP_011660857.1; NZ_CP009800.1.
DR   AlphaFoldDB; Q0B2V8; -.
DR   GeneID; 69548922; -.
DR   KEGG; bam:Bamb_5971; -.
DR   PATRIC; fig|339670.21.peg.6931; -.
DR   eggNOG; COG0365; Bacteria.
DR   OMA; TTFYDGP; -.
DR   Proteomes; UP000000662; Chromosome 3.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd05973; MACS_like_2; 1.
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; 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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABI91515.1}.
FT   DOMAIN          45..402
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          463..540
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   557 AA;  59944 MW;  9FA99208E9263C9B CRC64;
     MRDGATAREV PAYADAVAGF RIETATAYLH GDLEQGLNAC VECCDRHAAA DPNAIALDWI
     DAGGRHRSFT FAQMQALSAR VANLLVEQGV KPGDVVAGLL PRTPELVATI LGTWRAGAVY
     QPLFTAFGPK AIEHRLRMSD ARLIVTNIAN RAKLDEIVDC PPVATVREPG DTLPARDIDF
     RTALDAQSGR FEPVLRKGTD LFMMMSTSGT TGLPKGVPVP LRALLAFGAY MRDAVDLRDS
     DRFWNIADPG WAYGLYYAIT GPLLLGHATT LYEGSFTVDS TCDVIERLGI TSLAGSPTAY
     RMLMAAGTEV AARLKGQLRV VSSAGEPLNP EVVRWFHAAL GAPIHDHYGQ TELGMVVNNH
     HGLTHVVHVG SAGLAMPGYR VAVLDEAGRE LGPGEPGNLA IDIARSPLLW FTGYWQQDTP
     AIAGGYYRTG DNVELEPDGT VSFIGRADDV ITSSGYRIGP FDVESALIEH PAVSEAAVIG
     VPDPERTEIV KAFVVLSKGF EGTPALADEL SQHVKRRLSA HAYPRAIDFV DALPKTPSGK
     IQRFVLRKME AEKTAQS
//
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