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Q5REV5 (ACSM3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acyl-coenzyme A synthetase ACSM3, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 3
Butyrate--CoA ligase 3
Butyryl-coenzyme A synthetase 3
Middle-chain acyl-CoA synthetase 3
Protein SA homolog
Gene names
Name:ACSM3
Synonyms:SAH
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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) By similarity.

Catalytic activity

ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium or manganese By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
Gene Ontology (GO)
   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

butyrate-CoA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 586559Acyl-coenzyme A synthetase ACSM3, mitochondrial
PRO_0000306099

Regions

Nucleotide binding235 – 2439ATP By similarity
Nucleotide binding374 – 3796ATP By similarity

Sites

Binding site4611ATP By similarity
Binding site4761ATP By similarity
Binding site5721ATP By similarity

Amino acid modifications

Modified residue431Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5REV5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A923438898F18582

FASTA58666,060
        10         20         30         40         50         60 
MLACVTMKML RHAKCFQRLA IFGSVRALHK DNRTATPQNF SNYESMKQDF KLGIPEYFNF 

        70         80         90        100        110        120 
AKDVLDQWTD KEKAGKKPSN PAFWWINRNG EEVRWSFEEL GSLSRKFANI LSEACSLQRG 

       130        140        150        160        170        180 
DRVILILPRV PEWWLANVAC LRTGTVLIPG TTQLTQKDIL YRLQSSKANC IITNDVLAPA 

       190        200        210        220        230        240 
VDAVAPKCEN LHSKLIVSEN SREGWGNLKE MMKHASDSHT CVKTKHNEIM AIFFTSGTSG 

       250        260        270        280        290        300 
YPKMTAHTHS SFGLGLSVNG RFWLDLTPSD VMWNTSDTGW AKSAWSSVFS PWIQGACVFT 

       310        320        330        340        350        360 
HHLPRFEPTS ILQTLSKYPI TVFCSAPTVY RMLVQNDMAS YKFKSLKHCV SAGEPITPDV 

       370        380        390        400        410        420 
TEKWRNKTGL DIYEGYGQTE TVLICGNFKG MKIKPGSMGK PSPAFDVKIV DVNGNVLPPG 

       430        440        450        460        470        480 
QEGDIGIQVL PNRPFGLFTH YVDNPSKTAS TLRGNFYITG DRGYMDEDGY FWFVARADDV 

       490        500        510        520        530        540 
ILSSGYRIGP FEVENALNEH PSVAESAVVS SPDPIRGEVV KAFVVLNPDY KSHDQEQLIK 

       550        560        570        580 
EIQEHVKKTT APYKYPRKVE FIQELPKTIS GKTKRNELRK KEWKTI 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857411 mRNA. Translation: CAH89702.1.
RefSeqNP_001124772.1. NM_001131300.1.
UniGenePab.12217.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ5REV5.
SMRQ5REV5. Positions 53-584.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000008431; ENSPPYP00000008096; ENSPPYG00000007161.
GeneID100171624.
KEGGpon:100171624.

Organism-specific databases

CTD6296.

Phylogenomic databases

HOVERGENHBG053031.
InParanoidQ5REV5.
OMAKFPITVF.
OrthoDBEOG4ZPDTX.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01896.
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSM3_PONAB
AccessionPrimary (citable) accession number: Q5REV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families