ID G3RBM8_GORGO Unreviewed; 518 AA.
AC G3RBM8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=medium-chain acyl-CoA ligase {ECO:0000256|ARBA:ARBA00039009};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000012889.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000012889.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000012889.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000012889.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00036212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000256|ARBA:ARBA00036212};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CABD030099610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030099611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030099612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3RBM8; -.
DR STRING; 9593.ENSGGOP00000012889; -.
DR Ensembl; ENSGGOT00000013260.3; ENSGGOP00000012889.3; ENSGGOG00000013214.3.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000164294; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; G3RBM8; -.
DR OMA; GPVGCRY; -.
DR TreeFam; TF354287; -.
DR Proteomes; UP000001519; Chromosome 16.
DR Bgee; ENSGGOG00000013214; Expressed in liver and 1 other cell type or tissue.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR43605:SF3; ACYL-COENZYME A SYNTHETASE ACSM2B, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 4..367
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 418..498
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 518 AA; 57182 MW; EFDF5B0F97D6C91E CRC64;
AGKRPPSPAL WWVNGKGKEL MWNFRELSEN SQQAANVLSG ACGLQRGDRV AVVLPRVPEW
WLVILGCIRA GLIFMPGTIQ MKSTDILYRL QMSQAKAIVA GDEVIQEVDT VASECPSLRI
KLLVSEKSCD GWLNFKKLLN EASTTHHCVE TGSQEASAIY FTSGTSGLPK MAEHSHSSLG
LKAKMDAGWT GLQASDIMWT ISDTGWILNI LGSLLETWAS GACTFVHLLP KFDPLVILKT
LSSYPIKHMM GAPIVYRMLL QQDLSSYKFP HLQNCLSGGE SLLPETLENW RAQTGLDIRE
FYGQTETGFT CIVSKTMKIK PGYMGTAASC YDVQVIDDKG NILPPGTEGD IGIRVKPIRP
IGIFSGYVDN PDKTAANIRG DFWLLGDRGI KDEDGYFQFM GRADDIINSS GYRIGPSEVE
NALMKHPAVV ETAVISSPDP VRGEVVKAFV VLASQFLSHD PEQLTKELQQ HVKSVTAPYK
YPRKIEFVLN LPKTVTGKIQ RTKLRDKEWK MSGKASAQ
//
