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P11568 (HGDC_ACIFV) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Activator of (R)-2-hydroxyglutaryl-CoA dehydratase
Alternative name(s):
2-hydroxyglutaryl-CoA dehydratase component A
Gene names
Name:hgdC
Ordered Locus Names:Acfer_1816
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP]
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

Binds 1 4Fe-4S cluster per dimer.

Subunit structure

Homodimer.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Activator of (R)-2-hydroxyglutaryl-CoA dehydratase
PRO_0000083965

Sites

Metal binding1271Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal binding1661Iron-sulfur (4Fe-4S); shared with dimeric partner

Experimental info

Sequence conflict1961A → P in CAA32464. Ref.3
Sequence conflict2091V → L in CAA32464. Ref.3
Sequence conflict214 – 22411MTGGVAQNYGV → HDRRCSPELWL in CAA32464. Ref.3

Secondary structure

......................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11568 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 7E97044DB6E805AC

FASTA26027,269
        10         20         30         40         50         60 
MSIYTLGIDV GSTASKCIIL KDGKEIVAKS LVAVGTGTSG PARSISEVLE NAHMKKEDMA 

        70         80         90        100        110        120 
FTLATGYGRN SLEGIADKQM SELSCHAMGA SFIWPNVHTV IDIGGQDVKV IHVENGTMTN 

       130        140        150        160        170        180 
FQMNDKCAAG TGRFLDVMAN ILEVKVSDLA ELGAKSTKRV AISSTCTVFA ESEVISQLSK 

       190        200        210        220        230        240 
GTDKIDIIAG IHRSVASRVI GLANRVGIVK DVVMTGGVAQ NYGVRGALEE GLGVEIKTSP 

       250        260 
LAQYNGALGA ALYAYKKAAK 

« Hide

References

« Hide 'large scale' references
[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]"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]"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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59645 Genomic DNA. Translation: CAA42196.1.
CP001859 Genomic DNA. Translation: ADB48170.1.
X14252 Genomic DNA. Translation: CAA32464.1.
PIRS36105.
RefSeqYP_003399485.1. NC_013740.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HUXX-ray3.00A/B1-260[»]
ProteinModelPortalP11568.
SMRP11568. Positions 2-249.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB48170; ADB48170; Acfer_1816.
GeneID8738319.
KEGGafn:Acfer_1816.
PATRIC31910223. VBIAciFer109666_1807.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000282733.
OMAQETEMIA.

Enzyme and pathway databases

BioCycAFER591001:GHUL-1889-MONOMER.

Family and domain databases

InterProIPR002731. ATPase_BadF.
IPR008275. CoA_E_activase.
[Graphical view]
PfamPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]
TIGRFAMsTIGR00241. CoA_E_activ. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11568.

Entry information

Entry nameHGDC_ACIFV
AccessionPrimary (citable) accession number: P11568
Secondary accession number(s): D2RM68, Q44042
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references