ID A0A194PV33_PAPXU Unreviewed; 886 AA.
AC A0A194PV33;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000256|ARBA:ARBA00039638};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
GN ORFNames=RR46_04973 {ECO:0000313|EMBL:KPI96848.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI96848.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI96848.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI96848.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI96848.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; KQ459592; KPI96848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PV33; -.
DR STRING; 66420.A0A194PV33; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
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 InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
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 Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 50..436
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 487..562
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT DOMAIN 607..870
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
SQ SEQUENCE 886 AA; 96619 MW; D6952454CFDB3112 CRC64;
MAKSELGQNI RRTFMLTNQT RLLQSDPNAS YLHNPGSEPL TIATLGEVLA ESANKYPNRI
AIRSIHEDIT LTYEELLTQA DSLGCTLRAN GFNKGDRLGI WSHNMAGWIL TVLAAARVGL
ISVFINPVYE KSELSFCLKK TGMKGLIIGN SLSNRDYYNS LKHLIPELDG CKPGSLISEQ
FPDLTTIISL EKEKLDGVFT FDSLLGNKTN QVSKYGSEIK PEDGSIIHFT SGTTGDPKAA
LDSHLGVVNN TYFIGRRNGY DEDNQKICVQ VPLFHALGSV VTMLGALRHG ATLVLAAPMY
NIPANINALL AEKCTAVTGT PTMYVDMISQ IRERGDLPLR LRMALAAGAP CSPQLIRDMN
KYLKADSVLA LYGMTETTAS VFQSKPGDDI DVVADTVGYI QDHVEVKVVD EDGQTVPFGG
SGELLVRGYN TMICYWDEPE KTKNTFTEDG WLSTGDKFTV SPDGYGRVVG RLKDIIVRGG
ENIAPKEIED LLNTHPDVIE SQVVGISDER LGEELCAVLR TRDGVTVTLD DVRKFCSGHI
AKFKIPRVLK ITEDFPKTAS GKIQKYKLRD LIESGCTQYV DAASLRCYNG SLDNPMIVPL
DFPRPLINNS CINTSRVTKF FISGFNRNVT SEESITILSA YIERGDVNVV YLDWAEEASK
ESIGTVLGYL KAASNTQNIG ARFAAALLNL LDGGLEFTKV HLVGHSLGAQ IAGITGNTLV
AQGYILQRAS CLDPAGPLYS GLISFKNGVS PECAKQVDVI HTDPGGYGIA DRAGTADFWP
NYEGGKTVQP GCLRGNFPLL SEEGLCSHIA SWRYFAETIN DCNCFPAASA PDYATWSSTN
GTTNSTIYMG EYLSPEARGN YYLVTNDRSL YGIGEEGTDP NNRIDN
//
