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Protein

Glutaconate CoA-transferase subunit B

Gene

gctB

Organism
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathway: L-glutamate degradation via hydroxyglutarate pathway

This protein is involved in step 3 of the subpathway that synthesizes crotonoyl-CoA from L-glutamate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Glutaconate CoA-transferase subunit A (gctA), Glutaconate CoA-transferase subunit B (gctB)
  4. (R)-2-hydroxyglutaryl-CoA dehydratase subunit beta (hgdB), (R)-2-hydroxyglutaryl-CoA dehydratase subunit alpha (hgdA)
  5. Glutaconyl-CoA decarboxylase subunit gamma (gcdC), Glutaconyl-CoA decarboxylase subunit beta (gcdB), Glutaconyl-CoA decarboxylase subunit delta (gcdD), Glutaconyl-CoA decarboxylase subunit alpha (gcdA)
This subpathway is part of the pathway L-glutamate degradation via hydroxyglutarate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes crotonoyl-CoA from L-glutamate, the pathway L-glutamate degradation via hydroxyglutarate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciAFER591001:GHUL-1891-MONOMER.
MetaCyc:MONOMER-1029.
BRENDAi2.8.3.12. 85.
SABIO-RKQ59112.
UniPathwayiUPA00533; UER00686.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaconate CoA-transferase subunit B (EC:2.8.3.12)
Alternative name(s):
GCT small subunit
Gene namesi
Name:gctB
Ordered Locus Names:Acfer_1818
OrganismiAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Taxonomic identifieri591001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus
ProteomesiUP000001902 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 266265Glutaconate CoA-transferase subunit BPRO_0000157930Add
BLAST

Interactioni

Subunit structurei

Heterooctamer of four A and four B subunits.

Protein-protein interaction databases

DIPiDIP-6201N.
IntActiQ59112. 1 interaction.
STRINGi591001.Acfer_1818.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Beta strandi26 – 283Combined sources
Helixi33 – 4311Combined sources
Beta strandi50 – 534Combined sources
Turni54 – 563Combined sources
Beta strandi57 – 604Combined sources
Helixi72 – 754Combined sources
Beta strandi77 – 815Combined sources
Helixi84 – 9714Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi125 – 1317Combined sources
Helixi138 – 1447Combined sources
Beta strandi147 – 1504Combined sources
Turni155 – 1573Combined sources
Helixi176 – 1794Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi196 – 2005Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2126Combined sources
Helixi218 – 2236Combined sources
Helixi242 – 2509Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POIX-ray2.50B/D3-262[»]
ProteinModelPortaliQ59112.
SMRiQ59112. Positions 3-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59112.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221246.
KOiK01040.
OMAiREEIDPG.

Family and domain databases

InterProiIPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 1 hit.
[Graphical view]
SMARTiSM00882. CoA_trans. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q59112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADYTNYTNK EMQAVTIAKQ IKNGQVVTVG TGLPLIGASV AKRVYAPDCH
60 70 80 90 100
IIVESGLMDC SPVEVPRSVG DLRFMAHCGC IWPNVRFVGF EINEYLHKAN
110 120 130 140 150
RLIAFIGGAQ IDPYGNVNST SIGDYHHPKT RFTGSGGANG IATYSNTIIM
160 170 180 190 200
MQHEKRRFMN KIDYVTSPGW IDGPGGRERL GLPGDVGPQL VVTDKGILKF
210 220 230 240 250
DEKTKRMYLA AYYPTSSPED VLENTGFDLD VSKAVELEAP DPAVIKLIRE
260
EIDPGQAFIQ VPTEAK
Length:266
Mass (Da):29,166
Last modified:January 23, 2007 - v3
Checksum:i1E691B864237A784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81440 Genomic DNA. Translation: CAA57200.1.
CP001859 Genomic DNA. Translation: ADB48172.1.
PIRiS51052.
RefSeqiWP_012939155.1. NC_013740.1.
YP_003399487.1. NC_013740.1.

Genome annotation databases

EnsemblBacteriaiADB48172; ADB48172; Acfer_1818.
KEGGiafn:Acfer_1818.
PATRICi31910227. VBIAciFer109666_1809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81440 Genomic DNA. Translation: CAA57200.1.
CP001859 Genomic DNA. Translation: ADB48172.1.
PIRiS51052.
RefSeqiWP_012939155.1. NC_013740.1.
YP_003399487.1. NC_013740.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POIX-ray2.50B/D3-262[»]
ProteinModelPortaliQ59112.
SMRiQ59112. Positions 3-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6201N.
IntActiQ59112. 1 interaction.
STRINGi591001.Acfer_1818.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADB48172; ADB48172; Acfer_1818.
KEGGiafn:Acfer_1818.
PATRICi31910227. VBIAciFer109666_1809.

Phylogenomic databases

HOGENOMiHOG000221246.
KOiK01040.
OMAiREEIDPG.

Enzyme and pathway databases

UniPathwayiUPA00533; UER00686.
BioCyciAFER591001:GHUL-1891-MONOMER.
MetaCyc:MONOMER-1029.
BRENDAi2.8.3.12. 85.
SABIO-RKQ59112.

Miscellaneous databases

EvolutionaryTraceiQ59112.

Family and domain databases

InterProiIPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 1 hit.
[Graphical view]
SMARTiSM00882. CoA_trans. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiGCTB_ACIFV
AccessioniPrimary (citable) accession number: Q59112
Secondary accession number(s): D2RM70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.