ID G5C2G3_HETGA Unreviewed; 579 AA.
AC G5C2G3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=medium-chain acyl-CoA ligase {ECO:0000256|ARBA:ARBA00039009};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
GN Name=ACSM5 {ECO:0000313|EMBL:JAO02455.1};
GN ORFNames=GW7_15576 {ECO:0000313|EMBL:EHB15724.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15724.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15724.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAO02455.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:JAO02455.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; JH173077; EHB15724.1; -; Genomic_DNA.
DR EMBL; GEBF01001178; JAO02455.1; -; Transcribed_RNA.
DR AlphaFoldDB; G5C2G3; -.
DR STRING; 10181.G5C2G3; -.
DR Ensembl; ENSHGLT00000074044; ENSHGLP00000051209; ENSHGLG00000010732.
DR Ensembl; ENSHGLT00100015055; ENSHGLP00100014892; ENSHGLG00100011024.
DR eggNOG; KOG1175; Eukaryota.
DR InParanoid; G5C2G3; -.
DR OMA; PFNWALD; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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:SF6; ACYL-COENZYME A SYNTHETASE ACSM5, 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:UP000006813}.
FT DOMAIN 69..422
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 486..566
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 579 AA; 64837 MW; CACFAFA3CDCD12A5 CRC64;
MRLWLRGLGL QALRNFREFC RVHTQLPPLP VPEKILAVWE AISLGRQPVP EYFNFAHDVL
DMWAQLEKAG HRPSCPAFWW LDGRGAEVKW SFAELGTQSR KAANVLGDAC GLQPRDRMIL
VLPRLPEWWL ISVACMRTGV VMIPGVSQLT EKDLKYRLQM SRAKSIVASD SLAPHVDAIS
AECPSLQTKL LVSDSSRPGW VNFRELLQEA SAEHSCVRTK SGDPLVIYFT SGTTGAPKMV
EHSQCSYGLG FVASGSRWLG LTGSDVFWNT SDTGWVKAGW SFFPTWAMGS CVFVHEMPRV
DTKVILNTLS TYPITNFCCV PTIFRLLVQE DLTRYQFQSL QHCLAGGEAL NPDVRDKWKR
HTGLELHEGY GQSETVAICA NARGTKIKSG SMGQASPPYD VQIVDDEGNV LPPGEEGNIA
VRVRPTRPFC LFNYYLDNPE KTAASEQGDF YITGDRGRMD TDGYFWFMGR NDDVINSSSY
RIGPVEVESV LAEHPAVLEC AVVSSPDPIR GEVVKAFIVL SPAYYSHDPE ALTRELQEHV
KRVTAPYKYP RKVAFVSELP KTVSGKIQRS KLRNQEWAR
//
