ACSM5_RAT
ID ACSM5_RAT Reviewed; 578 AA.
AC Q6AYT9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM5, mitochondrial;
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q08AH1};
DE Flags: Precursor;
GN Name=Acsm5; Synonyms=Macs3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q08AH1}.
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:0000250|UniProtKB:Q08AH1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q91VA0}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; BC078915; AAH78915.1; -; mRNA.
DR RefSeq; NP_001014184.3; NM_001014162.4.
DR RefSeq; XP_006230185.1; XM_006230123.1.
DR RefSeq; XP_006230188.1; XM_006230126.2.
DR RefSeq; XP_017444881.1; XM_017589392.1.
DR AlphaFoldDB; Q6AYT9; -.
DR SMR; Q6AYT9; -.
DR STRING; 10116.ENSRNOP00000043828; -.
DR iPTMnet; Q6AYT9; -.
DR PhosphoSitePlus; Q6AYT9; -.
DR PRIDE; Q6AYT9; -.
DR Ensembl; ENSRNOT00000046025; ENSRNOP00000047613; ENSRNOG00000031211.
DR GeneID; 361637; -.
DR KEGG; rno:361637; -.
DR UCSC; RGD:1309578; rat.
DR CTD; 54988; -.
DR RGD; 1309578; Acsm5.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000161148; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q6AYT9; -.
DR OrthoDB; 683933at2759; -.
DR Reactome; R-RNO-177128; Conjugation of salicylate with glycine.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR PRO; PR:Q6AYT9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000031211; Expressed in liver and 11 other tissues.
DR ExpressionAtlas; Q6AYT9; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion 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; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Fatty acid metabolism; GTP-binding; Ligase;
KW Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..578
FT /note="Acyl-coenzyme A synthetase ACSM5, mitochondrial"
FT /id="PRO_0000306103"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 367..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGA8"
FT MOD_RES 96
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGA8"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGA8"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGA8"
SQ SEQUENCE 578 AA; 64623 MW; 0F2C8720E03E44CA CRC64;
MRLWLRGLVY QARRSSWGVF RIHTQPPPPP IPEVVATWEA ISLGKRPVPE YFNFAHDVLD
VWSQLEKTGH RPPNPAFWWV NGSGTEVKWT FEELGKQSRK AANILEGACG LKPGDRLMLV
LPRLPEWWLT IVACMRTGVV MIPGISQLTQ KDLKYRLQAA RVKSIITSDA LAPHVDAISA
DCPSLQSRLL VSDTSRPGWI NFRELLRVAS PEHNCLRTRS GDSMAIYFTS GTTGTPKMVE
HSQCSYGLGF VASGRRLMAL TESDIFWNTT DTGWVKAAWT LFSAWANGAC VFVHELPQVD
AQTILNTLCR FPITTICCVP TLFRLLVQED LTRYKFQCLR HCLAGGEALN SDVRDKWKNQ
TGLEIHEGYG QSETVLICGN FRGSTIKSGS MGKASPPYDV QIVDEEGNVL PPGKEGNIAI
RIKPTRPFCL FNCYLDNPEK TAASEQGDFY ITGDRAHMDE DGYFWFVGRN DDVINSSSYR
IGPVEVESAL AEHPAVLESA VVSSPDPIRG EVVKAFIVLS PAYVSHDPEA LTRELQEHVK
TVTAPYKYPR KVAFISELPK TVSGKILRSK LRNQEWGR
