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P11568

- HGDC_ACIFV

UniProt

P11568 - HGDC_ACIFV

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Protein

Activator of (R)-2-hydroxyglutaryl-CoA dehydratase

Gene

hgdC

Organism
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Required for the activation of (R)-2-hydroxyglutaryl-CoA dehydratase. This protein is extremely sensitive towards oxygen.

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster per dimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal bindingi166 – 1661Iron-sulfur (4Fe-4S); shared with dimeric partner

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciAFER591001:GHUL-1889-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Activator of (R)-2-hydroxyglutaryl-CoA dehydratase
Alternative name(s):
2-hydroxyglutaryl-CoA dehydratase component A
Gene namesi
Name:hgdC
Ordered Locus Names:Acfer_1816
OrganismiAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Taxonomic identifieri591001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus
ProteomesiUP000001902: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Activator of (R)-2-hydroxyglutaryl-CoA dehydratasePRO_0000083965Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi12 – 2110Combined sources
Turni22 – 243Combined sources
Beta strandi25 – 339Combined sources
Helixi40 – 5213Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 667Combined sources
Turni67 – 759Combined sources
Beta strandi77 – 804Combined sources
Helixi82 – 9312Combined sources
Beta strandi99 – 1046Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi117 – 12610Combined sources
Helixi132 – 14211Combined sources
Turni146 – 1483Combined sources
Helixi149 – 1535Combined sources
Helixi167 – 17913Combined sources
Helixi184 – 20421Combined sources
Beta strandi210 – 2167Combined sources
Helixi217 – 2204Combined sources
Helixi222 – 23211Combined sources
Helixi240 – 2445Combined sources
Helixi245 – 25713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HUXX-ray3.00A/B1-260[»]
ProteinModelPortaliP11568.
SMRiP11568. Positions 2-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11568.

Family & Domainsi

Sequence similaritiesi

To E.coli YjiL and M.jannaschii MJ0004 and MJ0800.Curated

Phylogenomic databases

HOGENOMiHOG000282733.
OMAiQETEMIA.

Family and domain databases

InterProiIPR002731. ATPase_BadF.
IPR008275. CoA_E_activase.
[Graphical view]
PfamiPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00241. CoA_E_activ. 1 hit.

Sequencei

Sequence statusi: Complete.

P11568-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIYTLGIDV GSTASKCIIL KDGKEIVAKS LVAVGTGTSG PARSISEVLE
60 70 80 90 100
NAHMKKEDMA FTLATGYGRN SLEGIADKQM SELSCHAMGA SFIWPNVHTV
110 120 130 140 150
IDIGGQDVKV IHVENGTMTN FQMNDKCAAG TGRFLDVMAN ILEVKVSDLA
160 170 180 190 200
ELGAKSTKRV AISSTCTVFA ESEVISQLSK GTDKIDIIAG IHRSVASRVI
210 220 230 240 250
GLANRVGIVK DVVMTGGVAQ NYGVRGALEE GLGVEIKTSP LAQYNGALGA
260
ALYAYKKAAK
Length:260
Mass (Da):27,269
Last modified:November 1, 1997 - v2
Checksum:i7E97044DB6E805AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961A → P in CAA32464. (PubMed:2659350)Curated
Sequence conflicti209 – 2091V → L in CAA32464. (PubMed:2659350)Curated
Sequence conflicti214 – 22411MTGGVAQNYGV → HDRRCSPELWL in CAA32464. (PubMed:2659350)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59645 Genomic DNA. Translation: CAA42196.1.
CP001859 Genomic DNA. Translation: ADB48170.1.
X14252 Genomic DNA. Translation: CAA32464.1.
PIRiS36105.
RefSeqiWP_012939153.1. NC_013740.1.
YP_003399485.1. NC_013740.1.

Genome annotation databases

EnsemblBacteriaiADB48170; ADB48170; Acfer_1816.
GeneIDi8738319.
KEGGiafn:Acfer_1816.
PATRICi31910223. VBIAciFer109666_1807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59645 Genomic DNA. Translation: CAA42196.1 .
CP001859 Genomic DNA. Translation: ADB48170.1 .
X14252 Genomic DNA. Translation: CAA32464.1 .
PIRi S36105.
RefSeqi WP_012939153.1. NC_013740.1.
YP_003399485.1. NC_013740.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HUX X-ray 3.00 A/B 1-260 [» ]
ProteinModelPortali P11568.
SMRi P11568. Positions 2-249.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADB48170 ; ADB48170 ; Acfer_1816 .
GeneIDi 8738319.
KEGGi afn:Acfer_1816.
PATRICi 31910223. VBIAciFer109666_1807.

Phylogenomic databases

HOGENOMi HOG000282733.
OMAi QETEMIA.

Enzyme and pathway databases

BioCyci AFER591001:GHUL-1889-MONOMER.

Miscellaneous databases

EvolutionaryTracei P11568.

Family and domain databases

InterProi IPR002731. ATPase_BadF.
IPR008275. CoA_E_activase.
[Graphical view ]
Pfami PF01869. BcrAD_BadFG. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00241. CoA_E_activ. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans by gene expression in Escherichia coli."
    Bendrat K., Mueller U., Klees A.-G., Buckel W.
    FEBS Lett. 329:329-331(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25085 / DSM 20731 / VR4.
  3. "Cloning and sequencing of the genes of 2-hydoxyglutaryl-CoA dehydratase from Acidaminococcus fermentans."
    Dutscho R., Wohlfarth G., Buckel P., Buckel W.
    Eur. J. Biochem. 181:741-746(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-260.
  4. "Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans."
    Mueller U., Buckel W.
    Eur. J. Biochem. 230:698-704(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations."
    Hans M., Buckel W., Bill E.
    Eur. J. Biochem. 267:7082-7093(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A."
    Locher K.P., Hans M., Yeh A.P., Schmid B., Buckel W., Rees D.C.
    J. Mol. Biol. 307:297-308(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiHGDC_ACIFV
AccessioniPrimary (citable) accession number: P11568
Secondary accession number(s): D2RM68, Q44042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3