ID   ACSM1_HUMAN             Reviewed;         577 AA.
AC   Q08AH1; Q08AH2; Q96A20;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   07-JUL-2009, entry version 27.
DE   RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
DE            EC=6.2.1.2;
DE   AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
DE   AltName: Full=Middle-chain acyl-CoA synthetase 1;
DE   AltName: Full=Butyryl coenzyme A synthetase 1;
DE   AltName: Full=Butyrate--CoA ligase 1;
DE   AltName: Full=Lipoate-activating enzyme;
DE   Flags: Precursor;
GN   Name=ACSM1; Synonyms=BUCS1, LAE, MACS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   MEDLINE=21443789; PubMed=11470804; DOI=10.1074/jbc.M106651200;
RA   Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K.,
RA   Takahashi S., Sakai J., Yamamoto T.T.;
RT   "Molecular identification and characterization of two medium-chain
RT   acyl-CoA synthetases, MACS1 and the Sa gene product.";
RL   J. Biol. Chem. 276:35961-35966(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Has medium-chain fatty acid:CoA ligase activity with
CC       broad substrate specificity (in vitro). Acts on acids from C(4) to
CC       C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-
CC       unsaturated acids (in vitro). Functions as GTP-dependent lipoate-
CC       activating enzyme that generates the substrate for
CC       lipoyltransferase (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + an acid + CoA = AMP + diphosphate + an
CC       acyl-CoA.
CC   -!- CATALYTIC ACTIVITY: GTP + lipoate = diphosphate + lipoyl-GMP.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08AH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08AH1-2; Sequence=VSP_028391;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; AB059429; BAB64535.1; -; mRNA.
DR   EMBL; AB062503; BAB68363.1; -; Genomic_DNA.
DR   EMBL; BC125177; AAI25178.1; -; mRNA.
DR   EMBL; BC125178; AAI25179.1; -; mRNA.
DR   IPI; IPI00059184; -.
DR   IPI; IPI00867642; -.
DR   RefSeq; NP_443188.2; -.
DR   UniGene; Hs.306812; -.
DR   PRIDE; Q08AH1; -.
DR   Ensembl; ENSG00000166743; Homo sapiens.
DR   GeneID; 116285; -.
DR   KEGG; hsa:116285; -.
DR   NMPDR; fig|9606.3.peg.11827; -.
DR   UCSC; uc002dhm.1; human.
DR   GeneCards; GC16M020543; -.
DR   HGNC; HGNC:18049; ACSM1.
DR   PharmGKB; PA25468; -.
DR   HOVERGEN; Q08AH1; -.
DR   OMA; Q08AH1; FTSIRFP.
DR   BRENDA; 6.2.1.2; 247.
DR   Reactome; REACT_13433; Biological oxidations.
DR   NextBio; 79860; -.
DR   ArrayExpress; Q08AH1; -.
DR   Bgee; Q08AH1; -.
DR   CleanEx; HS_ACSM1; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Complete proteome;
KW   Fatty acid metabolism; GTP-binding; Ligase; Lipid metabolism;
KW   Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Polymorphism; Transit peptide.
FT   TRANSIT       1     31       Mitochondrion (By similarity).
FT   CHAIN        32    577       Acyl-coenzyme A synthetase ACSM1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000306091.
FT   NP_BIND     226    234       ATP (By similarity).
FT   BINDING     452    452       ATP (By similarity).
FT   BINDING     467    467       ATP (By similarity).
FT   BINDING     563    563       ATP (By similarity).
FT   VAR_SEQ     205    577       Missing (in isoform 2).
FT                                /FTId=VSP_028391.
FT   VARIANT     272    272       I -> M (in dbSNP:rs16970511).
FT                                /FTId=VAR_048238.
FT   VARIANT     479    479       I -> V (in dbSNP:rs8056709).
FT                                /FTId=VAR_035245.
FT   VARIANT     515    515       I -> T (in dbSNP:rs16970453).
FT                                /FTId=VAR_035246.
FT   CONFLICT    549    549       K -> N (in Ref. 1; BAB64535/BAB68363).
SQ   SEQUENCE   577 AA;  65273 MW;  380BF4B8944B0E34 CRC64;
     MQWLMRFRTL WGIHKSFHNI HPAPSQLRCR SLSEFGAPRW NDYEVPEEFN FASYVLDYWA
     QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR
     VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP
     SLKTKLLVSD HSREGWLDFR SLVKSASPEH TCVKSKTLDP MVIFFTSGTT GFPKMAKHSH
     GLALQPSFPG SRKLRSLKTS DVSWCLSDSG WIVATIWTLV EPWTAGCTVF IHHLPQFDTK
     VIIQTLLKYP INHFWGVSSI YRMILQQDFT SIRFPALEHC YTGGEVVLPK DQEEWKRRTG
     LLLYENYGQS ETGLICATYW GMKIKPGFMG KATPPYDVQV IDDKGSILPP NTEGNIGIRI
     KPVRPVSLFM CYEGDPEKTA KVECGDFYNT GDRGKMDEEG YICFLGRSDD IINASGYRIG
     PAEVESALVE HPAVAESAVV GSPDPIRGEV VKAFIVLTPQ FLSHDKDQLT KELQQHVKSV
     TAPYKYPRKV EFVSELPKTI TGKIERKELR KKETGQM
//