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Database: UniProt
Entry: A0A067EMB7_CITSI
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ID   A0A067EMB7_CITSI        Unreviewed;       698 AA.
AC   A0A067EMB7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=CISIN_1g005406mg {ECO:0000313|EMBL:KDO56314.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO56314.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO56314.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) 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|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; KK784975; KDO56314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067EMB7; -.
DR   STRING; 2711.A0A067EMB7; -.
DR   PaxDb; 2711-XP_006472021-1; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
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:SF90; LONG CHAIN ACYL-COA SYNTHETASE 7, PEROXISOMAL; 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:UP000027120}.
FT   DOMAIN          103..508
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   698 AA;  77457 MW;  C8B4354864FD2062 CRC64;
     MEDSSAQRRF KAVQRHLTST NTDRCSQLDY NHTTGCFVQS QGYSVRLPEK LQTGKWNVYR
     SARSPLTLVD RFPDHPEIGT LHDNFIYAVE NYPDYKYLGT RVRVDGTVGG YKWMTYGEVS
     AARKEIGSGL LFHGLQKGVR IGLYLINRPE WLIVDHACSA YSYISVPLYD TLGPDAVKYV
     VNHAEIEAIF CIPQTLNTLL SFISEIPSVH LIVVVGGKDE HLPSLPSTSG VKLISYLQLQ
     SQGCSSPQPF CPPKPEDIAT ICYTSGTTGT PKGAVLTHGN LISNVAGFSL MVQFYPSDIY
     MSYLPLAHIY ERANQIVSVY YGVAVGFYQG DNLKLMDDLA VLKPTIFPSV PRLYNRIYAG
     ITNAVKASGT LREKLFTAAY NSKKQAIVSG QTPSKMWDRL VFNKIRERLG GRVRFMGSGA
     SPLSPDVMDF LKVCFGCQVM EGYGMTETSC IISAIDKGDN LSGHVGSPNP ACEIKLVDVP
     EMNYTSEDQP HPRGEICVRG PIVFQGYYKN EVQTREVIDG DGWLHTGDIG LWLPGGRLKI
     IDRKKNIFKL AQGEYVAPEK IENVYAKCKF VLQCFIYGDS FNSCLVAIVA VDPDVLKDWA
     ASQGIKFEDL EQLCNDPRAR AAVLAEMNAV GKEGQLRGFE YAKAVTLMPE PFSVENGLLT
     PTFKIKRPQA KERFAKAISN MYAELATSDQ IPQKTSNL
//
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