ID C3YZI2_BRAFL Unreviewed; 551 AA.
AC C3YZI2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000256|ARBA:ARBA00039638};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_164673 {ECO:0000313|EMBL:EEN54253.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN54253.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54253.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN54253.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty
CC acid metabolism, by forming a thioester with CoA. Has some preference
CC toward medium-chain substrates. Plays a role in adipocyte
CC differentiation. {ECO:0000256|ARBA:ARBA00037247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00035758};
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:0000256|ARBA:ARBA00036216};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; GG666566; EEN54253.1; -; Genomic_DNA.
DR RefSeq; XP_002598241.1; XM_002598195.1.
DR AlphaFoldDB; C3YZI2; -.
DR STRING; 7739.C3YZI2; -.
DR eggNOG; KOG1177; Eukaryota.
DR InParanoid; C3YZI2; -.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd05917; FACL_like_2; 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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT DOMAIN 20..421
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 472..547
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN54253.1"
FT NON_TER 551
FT /evidence="ECO:0000313|EMBL:EEN54253.1"
SQ SEQUENCE 551 AA; 62163 MW; 82D4C6A51AED9D6C CRC64;
SYYHNLTTTP LQGITIGQKL QQTVQKFPDR EMLVFKRGNI RRTYEQFFEE CDRLAAGFVA
LGLKKGDRVG MWGPNTLEWV LTQFATARAG LILVNINPAY QVHELEYALR KVGCRAIVSA
TAFKTQDYYK MLHQICPELE SCNPGELKTR NLPMLETVIK LGEEKFPGTY SFPEVLDMGD
HAHMRTVLEM QDKLQFDDPI NIQFTSGTTG NPKGATLTHH NILNNQWFIG HRLGFHEKVR
SICMPVPLYH CFGMVGGALA AGVFGTTVVT PAPSFEPEPC LQAIQEERQL FQLFCTYFCT
AIYGTPTMFI DILHHSNFDN YDLTSLNTGI MAGSPCPIEI MKQVVSKMHC PEVCIAYGTT
ENSPVTFMGY MADSLERKVG TIGQPFPHVE VKIVDTDGRV TPVNTPGELC TRGPGTMLGY
WDDPEKTAEV IGPDRWYMTG DIAVLDEEGY GQIVGRIKDM IIRGGENIYP REIEEFLYTH
PKIEDVQVIG VPDERMGEEV CAWIKLREGE NMEEDEIRAF CKGEISHFKI PRYIRFVSEF
PLTVTGKVNG F
//
