Reviewed, UniProtKB/Swiss-Prot Q08AH1 (ACSM1_HUMAN)

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
    Lipoate-activating enzyme

Gene names

Name:	ACSM1
Synonyms:	BUCS1, LAE, MACS1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 transcript 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 By similarity.
Catalytic activity	ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA. GTP + lipoate = diphosphate + lipoyl-GMP.
Cofactor	Magnesium By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
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	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	ATP-binding GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08AH1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q08AH1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     205-577: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 31	31	Mitochondrion By similarity
	Chain	32 – 577	546	Acyl-coenzyme A synthetase ACSM1, mitochondrial		PRO_0000306091
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
	Alternative sequence	205 – 577	373	Missing in isoform 2.		VSP_028391
	Natural variant	272	1	I → M: dbSNP rs16970511.		VAR_048238
	Natural variant	479	1	I → V: dbSNP rs8056709.		VAR_035245
	Natural variant	515	1	I → T: dbSNP rs16970453.		VAR_035246
Experimental info
	Sequence conflict	549	1	K → N in BAB64535. Ref.1
	Sequence conflict	549	1	K → N in BAB68363. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 1. Checksum: 380BF4B8944B0E34	FASTA	577	65,273
	10 20 30 40 50 60 MQWLMRFRTL WGIHKSFHNI HPAPSQLRCR SLSEFGAPRW NDYEVPEEFN FASYVLDYWA 70 80 90 100 110 120 QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR 130 140 150 160 170 180 VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP 190 200 210 220 230 240 SLKTKLLVSD HSREGWLDFR SLVKSASPEH TCVKSKTLDP MVIFFTSGTT GFPKMAKHSH 250 260 270 280 290 300 GLALQPSFPG SRKLRSLKTS DVSWCLSDSG WIVATIWTLV EPWTAGCTVF IHHLPQFDTK 310 320 330 340 350 360 VIIQTLLKYP INHFWGVSSI YRMILQQDFT SIRFPALEHC YTGGEVVLPK DQEEWKRRTG 370 380 390 400 410 420 LLLYENYGQS ETGLICATYW GMKIKPGFMG KATPPYDVQV IDDKGSILPP NTEGNIGIRI 430 440 450 460 470 480 KPVRPVSLFM CYEGDPEKTA KVECGDFYNT GDRGKMDEEG YICFLGRSDD IINASGYRIG 490 500 510 520 530 540 PAEVESALVE HPAVAESAVV GSPDPIRGEV VKAFIVLTPQ FLSHDKDQLT KELQQHVKSV 550 560 570 TAPYKYPRKV EFVSELPKTI TGKIERKELR KKETGQM
	Isoform 2. Checksum: 6C7EAEA423A0D790	FASTA	204	23,538
	10 20 30 40 50 60 MQWLMRFRTL WGIHKSFHNI HPAPSQLRCR SLSEFGAPRW NDYEVPEEFN FASYVLDYWA 70 80 90 100 110 120 QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR 130 140 150 160 170 180 VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP 190 200 SLKTKLLVSD HSREGWLDFR SLVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product." Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K., Takahashi S., Sakai J., Yamamoto T.T. J. Biol. Chem. 276:35961-35966(2001) [PubMed: 11470804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB059429 mRNA. Translation: BAB64535.1. AB062503 Genomic DNA. Translation: BAB68363.1. BC125177 mRNA. Translation: AAI25178.1. BC125178 mRNA. Translation: AAI25179.1.
IPI	IPI00059184. IPI00867642.
RefSeq	NP_443188.2.
UniGene	Hs.306812
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q08AH1.
Genome annotation databases
Ensembl	ENSG00000166743. Homo sapiens. [Contig view]
GeneID	116285.
KEGG	hsa:116285.
NMPDR	fig|9606.3.peg.11827.
UCSC	uc002dhm.1. human.
Organism-specific databases
GeneCards	GC16M020543.
HGNC	HGNC:18049. ACSM1.
PharmGKB	PA25468.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q08AH1.
OMA	Q08AH1. FTSIRFP.
Enzyme and pathway databases
BRENDA	6.2.1.2. 247.
Reactome	REACT_13433. Biological oxidations.
Gene expression databases
ArrayExpress	Q08AH1.
Bgee	Q08AH1.
CleanEx	HS_ACSM1.
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...
Other Resources
NextBio	79860.

Entry information

Entry name

ACSM1_HUMAN

Accession

Primary (citable) accession number: Q08AH1
Secondary accession number(s): Q08AH2, Q96A20

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 31, 2006
Last modified:	July 7, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)