ALKK_PSEOL
ID ALKK_PSEOL Reviewed; 546 AA.
AC Q00594;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Medium-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.2 {ECO:0000269|PubMed:1453953};
DE AltName: Full=Medium-chain acyl-CoA synthetase;
GN Name=alkK {ECO:0000303|PubMed:1453953};
OS Pseudomonas oleovorans.
OG Plasmid OCT.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=GPo1;
RX PubMed=1453953; DOI=10.1111/j.1365-2958.1992.tb01769.x;
RA van Beilen J.B., Eggink G., Enequist H., Bos R., Witholt B.;
RT "DNA sequence determination and functional characterization of the OCT-
RT plasmid-encoded alkJKL genes of Pseudomonas oleovorans.";
RL Mol. Microbiol. 6:3121-3136(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:1453953};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:1453953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1453953}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AJ245436; CAB54055.1; -; Genomic_DNA.
DR PIR; S27995; S27995.
DR AlphaFoldDB; Q00594; -.
DR SMR; Q00594; -.
DR BioCyc; MetaCyc:MON-1083; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Plasmid.
FT CHAIN 1..546
FT /note="Medium-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000193142"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 59262 MW; DD7DA4A538010776 CRC64;
MLGQMMRNQL VIGSLVEHAA RYHGAREVVS VETSGEVTRS CWKEVELRAR KLASALGKMG
LTPSDRCATI AWNNIRHLEV YYAVSGAGMV CHTINPRLFI EQITYVINHA EDKVVLLDDT
FLPIIAEIHG SLPKVKAFVL MAHNNSNASA QMPGLIAYED LIGQGDDNYI WPDVDENEAS
SLCYTSGTTG NPKGVLYSHR STVLHSMTTA MPDTLNLSAR DTILPVVPMF HVNAWGTPYS
AAMVGAKLVL PGPALDGASL SKLIASEGVS IALGVPVVWQ GLLAAQAGNG SKSQSLTRVV
VGGSACPASM IREFNDIYGV EVIHAWGMTE LSPFGTANTP LAHHVDLSPD EKLSLRKSQG
RPPYGVELKI VNDEGIRLPE DGRSKGNLMA RGHWVIKDYF HSDPGSTLSD GWFSTGDVAT
IDSDGFMTIC DRAKDIIKSG GEWISTVELE SIAIAHPHIV DAAVIAARHE KWDERPLLIA
VKSPNSELTS GEVCNYFADK VARWQIPDAA IFVEELPRNG TGKILKNRLR EKYGDILLRS
SSSVCE