ID C5AMN7_BURGB Unreviewed; 719 AA.
AC C5AMN7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Feruloyl-CoA synthetase {ECO:0000313|EMBL:ACR31088.1};
GN OrderedLocusNames=bglu_2g06550 {ECO:0000313|EMBL:ACR31088.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31088.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR31088.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR31088.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
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DR EMBL; CP001504; ACR31088.1; -; Genomic_DNA.
DR RefSeq; WP_012733483.1; NC_012721.2.
DR AlphaFoldDB; C5AMN7; -.
DR STRING; 626418.bglu_2g06550; -.
DR KEGG; bgl:bglu_2g06550; -.
DR PATRIC; fig|626418.3.peg.894; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_4; -.
DR Proteomes; UP000002187; Chromosome 2.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion 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; IPR011761; ATP-grasp.
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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT DOMAIN 507..543
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 719 AA; 75652 MW; 088E5C2CF9E59937 CRC64;
MNLIQSGTWP AATGQAVARL LRPSSIAIVG ASPTPGALGA SVLANLERND YRGQIYLVNP
KRDEINGRPC VNSIAQLPDG VDVAVLAIPQ AAVLDAVRQL AARKVGAVVI FSAGFAEAGA
EGIAQQQEIA RIAAETGMLV EGPNCLGCIN YLERVPLTFI ETAVSAEQAS RNRSQPAIGI
LSQSGAMMAV LNTTLASRGL PLSYAVSTGN EAASHLEDYL QFLLDDAGTR VIAMIAEQFR
QPARLLEIAR HARRAGKLLV LLHPGRSAAA RASAATHTGA MAGDHSLMRT KVERAGVVIA
PTLEELGDIA EIGLRCAHLP SRGTAIVGES GAFKALCLDI CEGLGLELPA LSDDDAPALR
AAMPAFVAVS NPLDLTAQGL VDPELYYRTL SALFDDDRFS AIVVGLIQTD PVTCAIKMPP
VLRAVLELRP DKPVICAGLD EGAAVPAEYI EQMRELGIPY FPGTERALRA VARLVELGGR
DFSEVDHAPV EIGLPLQEGV IPEHRAKAML APLGIPFARG ALAADIDDAL AIAGRVGYPV
ALKVQSGDIS HKSDVGGVML GIDDAQALRA AWMQLGSNVK RHAPSAVIEG VLVEAMGDRG
LEMIVGARND PQWGPVILVG FGGVAAEVMH DVRLLPHDLP RDGVIREISL LKGAALLRGF
RGEPARDVGA LADIVMRLGA LLQYEPGIRE IDLNPVVLYP EGRGALALDA LMLVEPASN
//
