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Database: UniProt
Entry: H2R189_PANTR
LinkDB: H2R189_PANTR
Original site: H2R189_PANTR 
ID   H2R189_PANTR            Unreviewed;       622 AA.
AC   H2R189;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|RuleBase:RU369030};
DE            EC=6.2.1.15 {ECO:0000256|RuleBase:RU369030};
DE            EC=6.2.1.3 {ECO:0000256|RuleBase:RU369030};
DE   AltName: Full=Acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030};
DE   AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030};
GN   Name=ACSL6 {ECO:0000313|Ensembl:ENSPTRP00000041973.5,
GN   ECO:0000313|VGNC:VGNC:11725};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000041973.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000041973.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000041973.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC         ChEBI:CHEBI:456215; EC=6.2.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00024548,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000256|ARBA:ARBA00024548,
CC         ECO:0000256|RuleBase:RU369030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC         ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00024565,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000256|ARBA:ARBA00024565,
CC         ECO:0000256|RuleBase:RU369030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-
CC         hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024495,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC         Evidence={ECO:0000256|ARBA:ARBA00024495,
CC         ECO:0000256|RuleBase:RU369030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-
CC         hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024532,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC         Evidence={ECO:0000256|ARBA:ARBA00024532,
CC         ECO:0000256|RuleBase:RU369030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-
CC         hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024469,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC         Evidence={ECO:0000256|ARBA:ARBA00024469,
CC         ECO:0000256|RuleBase:RU369030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024497,
CC         ECO:0000256|RuleBase:RU369030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000256|ARBA:ARBA00024497,
CC         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|ARBA:ARBA00024484};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000256|ARBA:ARBA00024484};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369030}. Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein
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; AC159021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2R189; -.
DR   Ensembl; ENSPTRT00000045193.5; ENSPTRP00000041973.5; ENSPTRG00000017210.7.
DR   VGNC; VGNC:11725; ACSL6.
DR   eggNOG; KOG1256; Eukaryota.
DR   GeneTree; ENSGT00940000162308; -.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   OMA; IAKCPIV; -.
DR   TreeFam; TF313877; -.
DR   Proteomes; UP000002277; Chromosome 5.
DR   Bgee; ENSPTRG00000017210; Expressed in bone marrow and 16 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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; 2.
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:SF54; LONG-CHAIN-FATTY-ACID--COA LIGASE 6; 1.
DR   Pfam; PF00501; AMP-binding; 2.
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|ARBA:ARBA00022832,
KW   ECO:0000256|RuleBase:RU369030}; Ligase {ECO:0000256|RuleBase:RU369030};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU369030};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU369030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT   DOMAIN          82..265
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          273..445
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   622 AA;  69194 MW;  37F72981A0010CAA CRC64;
     MQTQEILRIL RLPELGDLGQ FFRSLSATTL DSGGARRSVI GSGPQLLTHY YDDARTMYQV
     FRRGLSISGN GPCLGFRKPK QPYQWLSYQE VADRAEFLGS GLLQHNCKAC TDQFIGVFAQ
     NRPEWIIAEL ACYTYSMVVV PLYDTLGPGA IRYIINTADI STVIVDKPQK AVLLLEHVER
     KETPGLKLII LMDPFEEALK ERGQKCGVVI KSMQAVEDCG QENHQAPVPP QPDDLSIVCF
     TSGTTGNPKG AMLTHGNVVA DFSGFLKVTE GDIRLLSDDM KALCPTIFPV VPRLLNRMYD
     KIFSQANTPL KRWLLEFAAK RKQAEVRSGI IRNDSIWDEL FFNKIQASLG GCVRMIVTGA
     APASPTVLGF LRAALGCQVY EGYGQTECTA GCTFTTPGDW TSGHVGAPLP CNHIKLVDVE
     ELNYWACKGE GEICVRGPNV FKGYLKDPDR TKEALDSDGW LHTGDIGKWL PAGTLKIIDR
     KKHIFKLAQG EYVAPEKIEN IYIRSQPVAQ IYVHGDSLKA FLVGIVVPDP EVMPSWAQKR
     GIEGTYADLC TNKDLKKAIL EDMVRLGKES GLHSFEQVKA IHIHSDMFSV QNGLLTPTLK
     AKRPELREYF KKQIEELYSI SM
//
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