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Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (XL-III) (Xenobiotic/medium-chain fatty acid:CoA ligase XL-3) (XM-ligase 3)

 ACSM1_BOVIN             Reviewed;         577 AA.
Q9BEA2; Q32LF8; Q9TVB5; Q9XT43;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
15-MAR-2017, entry version 83.
RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
EC=6.2.1.2;
AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
AltName: Full=Butyrate--CoA ligase 1;
AltName: Full=Butyryl-coenzyme A synthetase 1;
AltName: Full=Lipoate-activating enzyme;
AltName: Full=Middle-chain acyl-CoA synthetase 1;
AltName: Full=XL-III;
AltName: Full=Xenobiotic/medium-chain fatty acid:CoA ligase XL-3;
Short=XM-ligase 3;
Flags: Precursor;
Name=ACSM1; Synonyms=BUCS1, LAE, MACS1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-53 AND 324-333,
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10561077;
DOI=10.1002/(SICI)1099-0461(2000)14:1<11::AID-JBT2>3.0.CO;2-E;
Vessey D.A., Lau E., Kelley M.;
"Isolation and sequencing of cDNAs for the XL-I and XL-III forms of
bovine liver xenobiotic-metabolizing medium-chain fatty acid:CoA
ligase.";
J. Biochem. Mol. Toxicol. 14:11-19(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-35, VARIANT
ALA-372, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=11382754; DOI=10.1074/jbc.M101748200;
Fujiwara K., Takeuchi S., Okamura-Ikeda K., Motokawa Y.;
"Purification, characterization, and cDNA cloning of lipoate-
activating enzyme from bovine liver.";
J. Biol. Chem. 276:28819-28823(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-372.
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16378734; DOI=10.1016/j.pep.2005.11.006;
Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K.;
"Purification, characterization, and mass spectrometric sequencing of
a medium chain acyl-CoA synthetase from mouse liver mitochondria and
comparisons with the homologues of rat and bovine.";
Protein Expr. Purif. 47:405-414(2006).
-!- FUNCTION: Has medium-chain fatty acid:CoA ligase activity with
broad substrate specificity (in vitro). Acts on acids from C(4) to
C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-
unsaturated acids (in vitro). Functions as GTP-dependent lipoate-
activating enzyme that generates the substrate for
lipoyltransferase. {ECO:0000269|PubMed:10561077,
ECO:0000269|PubMed:11382754}.
-!- CATALYTIC ACTIVITY: ATP + a carboxylate + CoA = AMP + diphosphate
+ an acyl-CoA.
-!- CATALYTIC ACTIVITY: GTP + lipoate = diphosphate + lipoyl-GMP.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11382754};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10561077}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:10561077, ECO:0000269|PubMed:11382754}.
-!- TISSUE SPECIFICITY: Detected in liver.
{ECO:0000269|PubMed:10561077}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF126145; AAD39140.1; -; mRNA.
EMBL; AJ132751; CAB44431.1; -; mRNA.
EMBL; AB048289; BAB40420.1; -; mRNA.
EMBL; BC109602; AAI09603.1; -; mRNA.
RefSeq; NP_777107.1; NM_174682.2.
UniGene; Bt.64940; -.
ProteinModelPortal; Q9BEA2; -.
SMR; Q9BEA2; -.
STRING; 9913.ENSBTAP00000001859; -.
PaxDb; Q9BEA2; -.
PeptideAtlas; Q9BEA2; -.
PRIDE; Q9BEA2; -.
GeneID; 282576; -.
KEGG; bta:282576; -.
CTD; 116285; -.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
HOGENOM; HOG000229982; -.
HOVERGEN; HBG053031; -.
InParanoid; Q9BEA2; -.
KO; K01896; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISS:AgBase.
GO; GO:0003996; F:acyl-CoA ligase activity; ISS:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047760; F:butyrate-CoA ligase activity; ISS:AgBase.
GO; GO:0015645; F:fatty acid ligase activity; ISS:AgBase.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; ISS:AgBase.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Fatty acid metabolism; GTP-binding; Ligase;
Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 31 Mitochondrion.
{ECO:0000269|PubMed:11382754}.
CHAIN 32 577 Acyl-coenzyme A synthetase ACSM1,
mitochondrial.
/FTId=PRO_5000049630.
NP_BIND 226 234 ATP. {ECO:0000250}.
BINDING 452 452 ATP. {ECO:0000250}.
BINDING 467 467 ATP. {ECO:0000250}.
BINDING 563 563 ATP. {ECO:0000250}.
MOD_RES 85 85 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 146 146 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 146 146 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 183 183 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 204 204 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 204 204 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 237 237 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 356 356 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 356 356 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 391 391 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 391 391 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 531 531 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 538 538 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 538 538 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VA0}.
MOD_RES 549 549 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VA0}.
VARIANT 372 372 T -> A. {ECO:0000269|PubMed:11382754,
ECO:0000269|Ref.3}.
CONFLICT 186 186 L -> H (in Ref. 3; AAI09603).
{ECO:0000305}.
SEQUENCE 577 AA; 64923 MW; 33C3DA651E461BE4 CRC64;
MQRLMKFRVL WGIHMSCPGF HHAPQHLRCR SLSGAGTLRW NDYDRPEEFN FASDVLDHWT
QMEKEGKRSP NPALWWVNDQ GDEVKWSFRE MTDLTCRTAN VLTQTCGLQT GDRLALILPR
VPEWWLVCVG CIRTGIIFMP GTTQMKAKDI LYRLQVSGAK AIVTTDTLAP EVESVAPECP
SLKTKLLVSD HSREGWLDFR SLVKSASPDH ICIKSKTLDP MAIFFTSGTT GFPKMAKHSH
GFALRSYFPA CRKLLQLKMS DVFWCLSDTG WILAALGSLL EPWTAGSTVF AHHLPQFDPK
VIIETFFKYP ITQCLAAPSV YRMILQQNYT SLRFPTLEHC CTGGEALLPE EQEQWKRQTG
VLLYQAYGQS ETGISCGTLR GMKIKPGSMG KAIPPFDIQI IDDKGNIQPP NTEGNIGIRI
KPTRPIGLFM YYENNPEKTA EVECGDFYNT GDRATIDEEG YFWFLGRSDD VINASGYRVG
PAEVENALAE HPAVAESAVV SSPDPVRGEV VKAFIVLNPE FSSRDPGELT KELQQHVKSV
TAPYKYPRKV EFVSELPKTI TGKIKRSELR KKEFGQK


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