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Q59111 (GCTA_ACIFV) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaconate CoA-transferase subunit A

EC=2.8.3.12
Alternative name(s):
GCT large subunit
Gene names
Name:gctA
Ordered Locus Names:Acfer_1819
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP]
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the CoA moiety from acetyl-CoA to (R)-2-hydroxyglutarate and related compounds like glutaconate.

Catalytic activity

Acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA.

Pathway

Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 3/5.

Subunit structure

Heterooctamer of four A and four B subunits.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the 3-oxoacid CoA-transferase subunit A family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglutamate catabolic process via 2-hydroxyglutarate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutaconate CoA-transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 320319Glutaconate CoA-transferase subunit A
PRO_0000157927

Secondary structure

................................................................ 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59111 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C51B214FE17FEB46

FASTA32035,722
        10         20         30         40         50         60 
MSKVMTLKDA IAKYVHSGDH IALGGFTTDR KPYAAVFEIL RQGITDLTGL GGAAGGDWDM 

        70         80         90        100        110        120 
LIGNGRVKAY INCYTANSGV TNVSRRFRKW FEAGKLTMED YSQDVIYMMW HAAALGLPFL 

       130        140        150        160        170        180 
PVTLMQGSGL TDEWGISKEV RKTLDKVPDD KFKYIDNPFK PGEKVVAVPV PQVDVAIIHA 

       190        200        210        220        230        240 
QQASPDGTVR IWGGKFQDVD IAEAAKYTIV TCEEIISDEE IRRDPTKNDI PGMCVDAVVL 

       250        260        270        280        290        300 
APYGAHPSQC YGLYDYDNPF LKVYDKVSKT QEDFDAFCKE WVFDLKDHDE YLNKLGATRL 

       310        320 
INLKVVPGLG YHIDMTKEDK 

« Hide

References

« Hide 'large scale' references
[1]"Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans."
Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W.
Eur. J. Biochem. 226:41-51(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
[2]"Complete genome sequence of Acidaminococcus fermentans type strain (VR4)."
Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K. expand/collapse author list , Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.
Stand. Genomic Sci. 3:1-14(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25085 / DSM 20731 / VR4.
[3]"Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases."
Jacob U., Mack M., Clausen T., Huber R., Buckel W., Messerschmidt A.
Structure 5:415-426(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81440 Genomic DNA. Translation: CAA57199.1.
CP001859 Genomic DNA. Translation: ADB48173.1.
PIRS51051.
RefSeqYP_003399488.1. NC_013740.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1POIX-ray2.50A/C2-318[»]
ProteinModelPortalQ59111.
SMRQ59111. Positions 2-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6200N.
IntActQ59111. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB48173; ADB48173; Acfer_1819.
GeneID8738322.
KEGGafn:Acfer_1819.
PATRIC31910229. VBIAciFer109666_1810.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000011749.
KOK01039.
OMAIFSWGGN.
ProtClustDBCLSK2461731.

Enzyme and pathway databases

BioCycAFER591001:GHUL-1892-MONOMER.
MetaCyc:MONOMER-1028.
SABIO-RKQ59111.
UniPathwayUPA00533; UER00686.

Family and domain databases

InterProIPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERPTHR13707. PTHR13707. 1 hit.
PfamPF01144. CoA_trans. 1 hit.
[Graphical view]
SMARTSM00882. CoA_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ59111.

Entry information

Entry nameGCTA_ACIFV
AccessionPrimary (citable) accession number: Q59111
Secondary accession number(s): D2RM71
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways