ID Q1LB49_CUPMC Unreviewed; 544 AA.
AC Q1LB49;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=AMP-dependent synthetase and ligase putative o-succinylbenzoate-CoA ligase {ECO:0000313|EMBL:ABF12627.1};
DE EC=6.2.1.26 {ECO:0000313|EMBL:ABF12627.1};
GN OrderedLocusNames=Rmet_5768 {ECO:0000313|EMBL:ABF12627.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF12627.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP000353; ABF12627.1; -; Genomic_DNA.
DR RefSeq; WP_011520167.1; NC_007974.2.
DR AlphaFoldDB; Q1LB49; -.
DR KEGG; rme:Rmet_5768; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_5_4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd12118; ttLC_FACS_AEE21_like; 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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR43859:SF4; BUTANOATE--COA LIGASE AAE1; 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:0000313|EMBL:ABF12627.1};
KW Plasmid {ECO:0000313|EMBL:ABF12627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT DOMAIN 26..402
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 452..526
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 544 AA; 59337 MW; 1829998B1191C82D CRC64;
MPTDYDTGLA RNPANYVPIT PLDFIARAAE VYGDRLAIVH GTVRQNWRDT YARCRRLASA
LTRAGVGKGD TVAALLPNTP AMVEAHFGVP MAGAVLNALN IRLDAANLVF MLRHGEAKVL
LADTEFADAA RQMAREVRGL KVIAVEDVLG PDAERFGDTD YESFLASGDP EFDWKMPGDE
WDAIALNYTS GTTGDPKGVV YHHRGAAMNA ISNILEWDMA KHPVYLWTLP MFHCNGWCFP
WTVAARAGVN VCLRKFEPKL VFDLMRDEGV THYCAAPIVH TALVNAPPSW REGLRGPVRG
MVAGAPPPAA VLAQMEAMGF DLSHVYGLTE VYGPAAVCAE QDAWHTVSQE ERAVLKARQG
VRYHLQSGVT VLDPDTMQPV PRDGETIGEI MFRGNICMKG YLKNDKATRE AFAGGWFHTG
DLGVCMPDGY IKIKDRSKDI IISGGENISS VEVEDALYRH PAVLAAAVVA QPDAKWGETP
CAFVELKDGA SVTAEELIAH CRTLLAGFKV PKAVYFGPLP KTSTGKIQKF ELRKKMQSNA
AIDV
//
