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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: 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)DescriptionActionsGraphical viewLength
Metal bindingi127Iron-sulfur (4Fe-4S); shared with dimeric partner1
Metal bindingi166Iron-sulfur (4Fe-4S); shared with dimeric partner1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

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

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 lineageiBacteriaFirmicutesNegativicutesAcidaminococcalesAcidaminococcaceaeAcidaminococcus
Proteomesi
  • UP000001902 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839651 – 260Activator of (R)-2-hydroxyglutaryl-CoA dehydrataseAdd BLAST260

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi591001.Acfer_1816.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi12 – 21Combined sources10
Turni22 – 24Combined sources3
Beta strandi25 – 33Combined sources9
Helixi40 – 52Combined sources13
Helixi56 – 58Combined sources3
Beta strandi60 – 66Combined sources7
Turni67 – 75Combined sources9
Beta strandi77 – 80Combined sources4
Helixi82 – 93Combined sources12
Beta strandi99 – 104Combined sources6
Beta strandi107 – 114Combined sources8
Beta strandi117 – 126Combined sources10
Helixi132 – 142Combined sources11
Turni146 – 148Combined sources3
Helixi149 – 153Combined sources5
Helixi167 – 179Combined sources13
Helixi184 – 204Combined sources21
Beta strandi210 – 216Combined sources7
Helixi217 – 220Combined sources4
Helixi222 – 232Combined sources11
Helixi240 – 244Combined sources5
Helixi245 – 257Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11568.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CIZ. Bacteria.
COG1924. LUCA.
HOGENOMiHOG000282733.
OMAiAIRMDER.
OrthoDBiPOG091H02AO.

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)DescriptionActionsGraphical viewLength
Sequence conflicti196A → P in CAA32464 (PubMed:2659350).Curated1
Sequence conflicti209V → L in CAA32464 (PubMed:2659350).Curated1
Sequence conflicti214 – 224MTGGVAQNYGV → HDRRCSPELWL in CAA32464 (PubMed:2659350).CuratedAdd BLAST11

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.

Genome annotation databases

EnsemblBacteriaiADB48170; ADB48170; Acfer_1816.
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.
PIRiS36105.
RefSeqiWP_012939153.1. NC_013740.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi591001.Acfer_1816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CIZ. Bacteria.
COG1924. LUCA.
HOGENOMiHOG000282733.
OMAiAIRMDER.
OrthoDBiPOG091H02AO.

Miscellaneous databases

EvolutionaryTraceiP11568.

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.
ProtoNetiSearch...

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 2, 2016
This is version 103 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

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 one 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.