Reviewed, UniProtKB/Swiss-Prot Q9BEA2 (ACSM1_BOVIN)

Names and origin

Protein names

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

Gene names

Name:	ACSM1
Synonyms:	BUCS1, LAE, MACS1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 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. Ref.1 Ref.2
Catalytic activity	ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA. GTP + lipoate = diphosphate + lipoyl-GMP.
Cofactor	Magnesium. Ref.2
Subunit structure	Monomer. Ref.1
Subcellular location	Mitochondrion matrix. Ref.1 Ref.2
Tissue specificity	Detected in liver. Ref.1
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW butyrate-CoA ligase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 31	31	Mitochondrion Ref.2
	Chain	32 – 577	546	Acyl-coenzyme A synthetase ACSM1, mitochondrial		PRO_5000049630
Regions
	Nucleotide binding	226 – 234	9	ATP By similarity
Sites
	Binding site	452	1	ATP By similarity
	Binding site	467	1	ATP By similarity
	Binding site	563	1	ATP By similarity
Natural variations
	Natural variant	372	1	T → A
Experimental info
	Sequence conflict	186	1	L → H in AAI09603. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9BEA2-1 [UniParc]. Last modified October 2, 2007. Version 2. Checksum: 33C3DA651E461BE4	FASTA	577	64,923
	10 20 30 40 50 60 MQRLMKFRVL WGIHMSCPGF HHAPQHLRCR SLSGAGTLRW NDYDRPEEFN FASDVLDHWT 70 80 90 100 110 120 QMEKEGKRSP NPALWWVNDQ GDEVKWSFRE MTDLTCRTAN VLTQTCGLQT GDRLALILPR 130 140 150 160 170 180 VPEWWLVCVG CIRTGIIFMP GTTQMKAKDI LYRLQVSGAK AIVTTDTLAP EVESVAPECP 190 200 210 220 230 240 SLKTKLLVSD HSREGWLDFR SLVKSASPDH ICIKSKTLDP MAIFFTSGTT GFPKMAKHSH 250 260 270 280 290 300 GFALRSYFPA CRKLLQLKMS DVFWCLSDTG WILAALGSLL EPWTAGSTVF AHHLPQFDPK 310 320 330 340 350 360 VIIETFFKYP ITQCLAAPSV YRMILQQNYT SLRFPTLEHC CTGGEALLPE EQEQWKRQTG 370 380 390 400 410 420 VLLYQAYGQS ETGISCGTLR GMKIKPGSMG KAIPPFDIQI IDDKGNIQPP NTEGNIGIRI 430 440 450 460 470 480 KPTRPIGLFM YYENNPEKTA EVECGDFYNT GDRATIDEEG YFWFLGRSDD VINASGYRVG 490 500 510 520 530 540 PAEVENALAE HPAVAESAVV SSPDPVRGEV VKAFIVLNPE FSSRDPGELT KELQQHVKSV 550 560 570 TAPYKYPRKV EFVSELPKTI TGKIKRSELR KKEFGQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequencing of cDNAs for the XL-I and XL-III forms of bovine liver xenobiotic-metabolizing medium-chain fatty acid:CoA ligase." Vessey D.A., Lau E., Kelley M. J. Biochem. Mol. Toxicol. 14:11-19(2000) [PubMed: 10561077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-53 AND 324-333, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver." Fujiwara K., Takeuchi S., Okamura-Ikeda K., Motokawa Y. J. Biol. Chem. 276:28819-28823(2001) [PubMed: 11382754] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-35, VARIANT ALA-372, FUNCTION, COFACTOR, SUBCELLULAR LOCATION. Tissue: Liver.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-372. Strain: Crossbred X Angus. Tissue: Liver.
[4]	"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." Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K. Protein Expr. Purif. 47:405-414(2006) [PubMed: 16378734] [Abstract] Cited for: MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF126145 mRNA. Translation: AAD39140.1. AJ132751 mRNA. Translation: CAB44431.1. AB048289 mRNA. Translation: BAB40420.1. BC109602 mRNA. Translation: AAI09603.1.
IPI	IPI00703179.
RefSeq	NP_777107.1.
UniGene	Bt.64940
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000001859; ENSBTAP00000001859; ENSBTAG00000001417; Bos taurus. [Genome view]
GeneID	282576.
KEGG	bta:282576.
Organism-specific databases
CTD	282576.
Phylogenomic databases
HOVERGEN	Q9BEA2.
Enzyme and pathway databases
BRENDA	6.2.1.2. 251.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSM1_BOVIN

Accession

Primary (citable) accession number: Q9BEA2
Secondary accession number(s): Q32LF8, Q9TVB5, Q9XT43

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 2, 2007
Last modified:	September 1, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)