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Q59112 (GCTB_ACIFV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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 B

EC=2.8.3.12
Alternative name(s):
GCT small subunit
Gene names
Name:gctB
Ordered Locus Names:Acfer_1818
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP]
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus

Protein attributes

Sequence length266 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 B 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 – 266265Glutaconate CoA-transferase subunit B
PRO_0000157930

Sites

Active site541

Secondary structure

............................................. 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59112 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1E691B864237A784

FASTA26629,166
        10         20         30         40         50         60 
MADYTNYTNK EMQAVTIAKQ IKNGQVVTVG TGLPLIGASV AKRVYAPDCH IIVESGLMDC 

        70         80         90        100        110        120 
SPVEVPRSVG DLRFMAHCGC IWPNVRFVGF EINEYLHKAN RLIAFIGGAQ IDPYGNVNST 

       130        140        150        160        170        180 
SIGDYHHPKT RFTGSGGANG IATYSNTIIM MQHEKRRFMN KIDYVTSPGW IDGPGGRERL 

       190        200        210        220        230        240 
GLPGDVGPQL VVTDKGILKF DEKTKRMYLA AYYPTSSPED VLENTGFDLD VSKAVELEAP 

       250        260 
DPAVIKLIRE EIDPGQAFIQ VPTEAK 

« 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 2-19 AND 44-66.
[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: CAA57200.1.
CP001859 Genomic DNA. Translation: ADB48172.1.
PIRS51052.
RefSeqYP_003399487.1. NC_013740.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1POIX-ray2.50B/D3-262[»]
ProteinModelPortalQ59112.
SMRQ59112. Positions 3-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6201N.
IntActQ59112. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB48172; ADB48172; Acfer_1818.
GeneID8738321.
KEGGafn:Acfer_1818.
PATRIC31910227. VBIAciFer109666_1809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221246.
KOK01040.
OMAHSKRTFV.

Enzyme and pathway databases

BioCycAFER591001:GHUL-1891-MONOMER.
MetaCyc:MONOMER-1029.
SABIO-RKQ59112.
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

EvolutionaryTraceQ59112.

Entry information

Entry nameGCTB_ACIFV
AccessionPrimary (citable) accession number: Q59112
Secondary accession number(s): D2RM70
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 85 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