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Database: UniProt
Entry: A0A151TG56_CAJCA
LinkDB: A0A151TG56_CAJCA
Original site: A0A151TG56_CAJCA 
ID   A0A151TG56_CAJCA        Unreviewed;       659 AA.
AC   A0A151TG56;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=KK1_012312 {ECO:0000313|EMBL:KYP66032.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP66032.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP66032.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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; CM003608; KYP66032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151TG56; -.
DR   STRING; 3821.A0A151TG56; -.
DR   OMA; VICHTSG; -.
DR   OrthoDB; 22305at2759; -.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000075243; Chromosome 6.
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; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF94; 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:UP000075243}.
FT   DOMAIN          72..479
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   659 AA;  73925 MW;  95A0D8D8BE7C3D8E CRC64;
     MAGVYTVKVE EARPATPEKP SAGPAYRCIF AKDALTNLPS LFESPWDFFR DTKTRCPSNP
     MLGRRKKTGS KVDPYEWITY QEAYDAAIQI GSAMKSRGVN PGDRCGIYGS NCPEWIIAME
     ACNGYAVTYV PLYDTLGPNA VEFIINHAEV SIAFVQDNKI PSVLSCLDRC SNLKTIVSFG
     NVSSSQKKEA EELGASCFTW GEFLQLGNTD FDVPLKKKTN ICTIMYTSGT TGEPKGVIIK
     NEAFMTQVLS IDQILYITDV VGTEDDVYFS FLPLAHIYDQ IMETYCIYKG SSIGFWQGDV
     RFLMEDIQAL KPTLFCGVPR VYDRVYAGIS SQISSGGALR STLFQYAYNY KLGYLEKGLP
     QDKAAPLFDR LVFDKIRQAL GGRVRLLLSG AAPLPRQVEE FLRVTFGANM SQGYGLTESC
     GGCFTAISNV FSMMGTIGVP MTTIEARLES VPEMGYDALS SEARGEICLR GNTLFSGYHK
     RQDLTEEVLV DGWFHTGDIG EWQPNGSMKI IDRKKNIFKL SQGEYVAVEN IENKYLQCPL
     VTSIWVYGNS FEPFLVAVVV PERNALEDWA MKHNSNVDFK SLCGNLKARK YILDELNRTG
     QKHQLRGFEM LKAVHLEPIP FDMERDLVTP TFKLKRSQLL KHYKDYIDQL YKEAKAQKV
//
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