ID R0H195_9BRAS Unreviewed; 666 AA.
AC R0H195;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
GN ORFNames=CARUB_v10003715mg {ECO:0000313|EMBL:EOA22974.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA22974.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC active form acyl-CoAs for both synthesis of cellular lipids, and
CC degradation via beta-oxidation. {ECO:0000256|RuleBase:RU369030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU369030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872, ECO:0000256|RuleBase:RU369030}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}.
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DR EMBL; KB870810; EOA22974.1; -; Genomic_DNA.
DR RefSeq; XP_006290076.1; XM_006290014.1.
DR AlphaFoldDB; R0H195; -.
DR STRING; 81985.R0H195; -.
DR GeneID; 17881053; -.
DR KEGG; crb:17881053; -.
DR eggNOG; KOG1256; Eukaryota.
DR OrthoDB; 22305at2759; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045311; LC-FACS_euk.
DR PANTHER; PTHR43272:SF55; LONG CHAIN ACYL-COA SYNTHETASE 5; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369030};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU369030};
KW Ligase {ECO:0000256|RuleBase:RU369030};
KW Lipid metabolism {ECO:0000256|RuleBase:RU369030};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 52..483
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 666 AA; 74045 MW; 0FD1BDB0F6D0085E CRC64;
MTTQKRFIFE VEAAKEATDG NPSVGPVYRS TFANNGFPNP IDGIHSCWDI FRTAVEKYPN
NRMLGRREIV NGKAGKYVWK TYKEVYDIVI KLGNSLRSCG IQEGEKCGIY GINCCEWIIS
MEACNANGLY CVPLYDTLGA GAVEFIISHA EVSVAFVEEK KIPEIFKTCP NSTKYLKTVV
SFGCVKPEQK EEAEKLGLII HSWDEFLKLG EGKQYDLPIK KESDICTIMY TSGTTGDPKG
VMISNESIVT ITTGVMHFLE SVNATISEKD VYISYLPLAH VFDRAVEECV IQVGGSIGFW
RGDVKLLIED LGELKPSIFC AVPRVLDRVY TGLQQKLSGG GFFKKKVFDV AFSYKFGNMK
KGQSHVAAAP FCDKLVFNKV KQGLGGNVRI ILSGAAPLAS HIESFLRVVA CCHVLQGYGL
TESCAGTFAT FPDELDMLGT VGPPVPNVDI RLESIPEMNY DALGSTPRGE ICIRGKTLFS
GYYKREDLTK EVLIDGWLHT GDVGEWQPNG SMKIIDRKKN IFKLAQGEYV AVENIENIYS
QVEAIDSVWV YGNSFESFLV AITNPAQQTL ERWAAENGVN GDFNSICQNA KAKAFILGEL
VKIAKEKKLK GFEIIKAVHL EPLAFDMERD LLTPTYKKKR PQLLKYYQNV IDEMYKTTKE
GQASGQ
//
