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Q59111

- GCTA_ACIFV

UniProt

Q59111 - GCTA_ACIFV

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Protein

Glutaconate CoA-transferase subunit A

Gene

gctA

Organism
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. glutaconate CoA-transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glutamate catabolic process via 2-hydroxyglutarate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciAFER591001:GHUL-1892-MONOMER.
MetaCyc:MONOMER-1028.
SABIO-RKQ59111.
UniPathwayiUPA00533; UER00686.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaconate CoA-transferase subunit A (EC:2.8.3.12)
Alternative name(s):
GCT large subunit
Gene namesi
Name:gctA
Ordered Locus Names:Acfer_1819
OrganismiAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Taxonomic identifieri591001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus
ProteomesiUP000001902: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 320319Glutaconate CoA-transferase subunit APRO_0000157927Add
BLAST

Interactioni

Subunit structurei

Heterooctamer of four A and four B subunits.

Protein-protein interaction databases

DIPiDIP-6200N.
IntActiQ59111. 1 interaction.

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 148
Beta strandi20 – 234
Helixi33 – 419
Beta strandi47 – 504
Beta strandi52 – 543
Helixi56 – 638
Beta strandi67 – 759
Turni78 – 803
Beta strandi81 – 833
Helixi85 – 939
Beta strandi96 – 1005
Helixi103 – 11513
Beta strandi118 – 1236
Helixi129 – 1324
Helixi138 – 1425
Beta strandi153 – 1575
Beta strandi160 – 16910
Beta strandi174 – 18310
Helixi198 – 2047
Beta strandi205 – 21511
Helixi218 – 2225
Helixi225 – 2273
Helixi232 – 2343
Beta strandi237 – 2404
Turni242 – 2476
Beta strandi248 – 2503
Turni251 – 2533
Helixi258 – 26710
Helixi271 – 28111
Turni282 – 2843
Helixi288 – 2958
Helixi297 – 3015
Turni307 – 3093
Helixi315 – 3173

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POIX-ray2.50A/C2-318[»]
ProteinModelPortaliQ59111.
SMRiQ59111. Positions 2-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59111.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000011749.
KOiK01039.
OMAiTHLIPFA.

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.

Q59111-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKVMTLKDA IAKYVHSGDH IALGGFTTDR KPYAAVFEIL RQGITDLTGL
60 70 80 90 100
GGAAGGDWDM LIGNGRVKAY INCYTANSGV TNVSRRFRKW FEAGKLTMED
110 120 130 140 150
YSQDVIYMMW HAAALGLPFL PVTLMQGSGL TDEWGISKEV RKTLDKVPDD
160 170 180 190 200
KFKYIDNPFK PGEKVVAVPV PQVDVAIIHA QQASPDGTVR IWGGKFQDVD
210 220 230 240 250
IAEAAKYTIV TCEEIISDEE IRRDPTKNDI PGMCVDAVVL APYGAHPSQC
260 270 280 290 300
YGLYDYDNPF LKVYDKVSKT QEDFDAFCKE WVFDLKDHDE YLNKLGATRL
310 320
INLKVVPGLG YHIDMTKEDK
Length:320
Mass (Da):35,722
Last modified:January 23, 2007 - v3
Checksum:iC51B214FE17FEB46
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81440 Genomic DNA. Translation: CAA57199.1.
CP001859 Genomic DNA. Translation: ADB48173.1.
PIRiS51051.
RefSeqiWP_012939156.1. NC_013740.1.
YP_003399488.1. NC_013740.1.

Genome annotation databases

EnsemblBacteriaiADB48173; ADB48173; Acfer_1819.
GeneIDi8738322.
KEGGiafn:Acfer_1819.
PATRICi31910229. VBIAciFer109666_1810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81440 Genomic DNA. Translation: CAA57199.1 .
CP001859 Genomic DNA. Translation: ADB48173.1 .
PIRi S51051.
RefSeqi WP_012939156.1. NC_013740.1.
YP_003399488.1. NC_013740.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1POI X-ray 2.50 A/C 2-318 [» ]
ProteinModelPortali Q59111.
SMRi Q59111. Positions 2-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6200N.
IntActi Q59111. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADB48173 ; ADB48173 ; Acfer_1819 .
GeneIDi 8738322.
KEGGi afn:Acfer_1819.
PATRICi 31910229. VBIAciFer109666_1810.

Phylogenomic databases

HOGENOMi HOG000011749.
KOi K01039.
OMAi THLIPFA.

Enzyme and pathway databases

UniPathwayi UPA00533 ; UER00686 .
BioCyci AFER591001:GHUL-1892-MONOMER.
MetaCyc:MONOMER-1028.
SABIO-RK Q59111.

Miscellaneous databases

EvolutionaryTracei Q59111.

Family and domain databases

InterProi IPR004165. CoA_trans_fam_I.
[Graphical view ]
PANTHERi PTHR13707. PTHR13707. 1 hit.
Pfami PF01144. CoA_trans. 1 hit.
[Graphical view ]
SMARTi SM00882. CoA_trans. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 2-13.
  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 nameiGCTA_ACIFV
AccessioniPrimary (citable) accession number: Q59111
Secondary accession number(s): D2RM71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 92 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