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Database: UniProt
Entry: A0A0D7K8X2_9BURK
LinkDB: A0A0D7K8X2_9BURK
Original site: A0A0D7K8X2_9BURK 
ID   A0A0D7K8X2_9BURK        Unreviewed;       547 AA.
AC   A0A0D7K8X2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Long-chain fatty acid--CoA ligase {ECO:0000313|EMBL:KJA10407.1};
GN   ORFNames=RP29_11225 {ECO:0000313|EMBL:KJA10407.1};
OS   Acidovorax temperans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA10407.1, ECO:0000313|Proteomes:UP000032566};
RN   [1] {ECO:0000313|EMBL:KJA10407.1, ECO:0000313|Proteomes:UP000032566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY4 {ECO:0000313|EMBL:KJA10407.1,
RC   ECO:0000313|Proteomes:UP000032566};
RA   Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT   "Isolation of bacteria from lake water.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJA10407.1}.
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DR   EMBL; JXYQ01000033; KJA10407.1; -; Genomic_DNA.
DR   RefSeq; WP_044398429.1; NZ_JXYQ01000033.1.
DR   AlphaFoldDB; A0A0D7K8X2; -.
DR   STRING; 80878.RP29_11225; -.
DR   PATRIC; fig|80878.5.peg.1919; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000032566; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd12119; ttLC_FACS_AlkK_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:SF67; MEDIUM-CHAIN-FATTY-ACID--COA LIGASE (ALKK-3); 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:KJA10407.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032566}.
FT   DOMAIN          18..401
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          455..529
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   547 AA;  60073 MW;  1F7D74C7F65BCF38 CRC64;
     MLGLMQSQPL LISSLIEFAE RHHGDAEIVS RRVEGDIHRY TYRDLAARAR RLANALDAHQ
     LQFSDRVATL AWNGYRHMEM YFGVSGSGRV LHTINPRLHP DQIAWIVNHA EDQVLCFDMT
     FLPLVQAVHA KCPTVKQWVA LCDADKLPAD SGIPGLLSYE AWIGAQSADY SWPEFDENSA
     SSMCYTSGTT GNPKAALYSH RSTTLHAYAA ALPDVMCLSA RDSVLPVVPM FHVNAWGIPY
     SAALTGCKLV FPGPALDGKS VYELIEAEQV TYAAGVPTVW QMLLGHMKPA GLTFSSLKRT
     VIGGSACPPA MITAFQEGYG VTVLHAWGMT EMSPLGTLCT LKNKHLSLPK DEQMKIVQKQ
     GRAIYGVDMK IVDGDGEELP WDGKTYGDLL VKGPWIVGSY FKGEGGDPLI KDSRGRGWFP
     TGDVATIDAD GFMQITDRSK DVIKSGGEWI SSIDIENIAM AHPSIQMAAC VGMPHPKWDE
     RPIVAVVKRP GTEVTREELL AFYEGKTAKW QIPDDVVFVD AIPIGATGKM LKTKLRELLK
     DYRLPGL
//
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