ID I1JAD1_SOYBN Unreviewed; 671 AA.
AC I1JAD1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=GLYMA_01G225200 {ECO:0000313|EMBL:KRH77642.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH77642.1};
RN [1] {ECO:0000313|EMBL:KRH77642.1, ECO:0000313|EnsemblPlants:KRH77642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH77642};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH77642.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH77642}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH77642};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH77642.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH77642.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {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; CM000834; KRH77642.1; -; Genomic_DNA.
DR AlphaFoldDB; I1JAD1; -.
DR SMR; I1JAD1; -.
DR STRING; 3847.I1JAD1; -.
DR PaxDb; 3847-GLYMA01G43470-1; -.
DR EnsemblPlants; KRH77642; KRH77642; GLYMA_01G225200.
DR Gramene; KRH77642; KRH77642; GLYMA_01G225200.
DR eggNOG; KOG1256; Eukaryota.
DR InParanoid; I1JAD1; -.
DR OMA; RRINHAG; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000008827; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
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:SF105; LONG CHAIN ACYL-COA SYNTHETASE 4; 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:UP000008827}.
FT DOMAIN 65..482
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 671 AA; 75366 MW; C50486820CE7511B CRC64;
MAQKRFIIEV EKAKEASEGR PSRGPVYRSL FAKDGFPAPI QGLNSCWDVF RLSVEKYPSN
PMLGRREIVD GKPGKYKWLT YKEVYDQVMK VGNSIRSCGY GEGVKCGIYG ANSAEWIMSM
QACNAHGLYC VPLYDTLGAG AIEFIICHAE VSIAFAEEKK IPELLKTFPN ATKYLKTIVS
FGKVTPEQKQ EVENSGLEIY SWDEFLQVGQ NQSFDLPIKK RSDICTIMYT SGTTGDPKGV
LISNESIITL LAGVKRLLES VNEQLTEKDV YISYLPLAHI FDRVIEETFI WHGASIGFWR
GDVKLLIEDV GELKPTIFCA VPRVLDRVYS GLTQKISSGG FLKKTLFNFA YSYKLNNMKK
GLRHGEASPL LDKIVFDKVK QGLGGRVRLI LSGAAPLSAH VEGYLRVVTC AHVLQGYGLT
ETCAGTFVSL PNEIEMLGTV GPPVPNVDVC LESVPEMGYD ALASTPRGEI CVKGKTLFAG
YYKREDLTKE VLIDEWFHTG DIGEWQPNGS MKIIDRKKNI FKLSQGEYVA VENLENIYGQ
VSSIESIWVY GNSFEAFLVA VVNPSKQALE HWAQENGISM DFNSLCEDAR AKSYIIEELS
KIAKEKKLKG FEFIKAVHLD SIPFDMERDL ITPTYKKKRP QLLKYYQHFY FVHRMPLTTC
IRVEVNPVPE T
//
