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Protein

4-hydroxybenzoyl-CoA reductase subunit gamma

Gene

hcrC

Organism
Thauera aromatica
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of a complex that catalyzes the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not reversible. Is a key enzyme in the anaerobic degradation of phenolic compounds.1 Publication

Catalytic activityi

Benzoyl-CoA + oxidized ferredoxin = 4-hydroxybenzoyl-CoA + reduced ferredoxin.1 Publication

Cofactori

[2Fe-2S] cluster2 PublicationsNote: Binds 2 [2Fe-2S] clusters per subunit.2 Publications

Enzyme regulationi

Inactivated by low concentrations of cyanide in vitro.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Iron-sulfur 1 (2Fe-2S)1
Metal bindingi46Iron-sulfur 1 (2Fe-2S)1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)1
Metal bindingi61Iron-sulfur 1 (2Fe-2S)1
Metal bindingi100Iron-sulfur 2 (2Fe-2S)1
Metal bindingi103Iron-sulfur 2 (2Fe-2S)1
Metal bindingi135Iron-sulfur 2 (2Fe-2S)1
Metal bindingi137Iron-sulfur 2 (2Fe-2S)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:COHBENREDTHAUERA-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxybenzoyl-CoA reductase subunit gamma (EC:1.3.7.9)
Short name:
4-HBCR subunit gamma
Gene namesi
Name:hcrC
OrganismiThauera aromatica
Taxonomic identifieri59405 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeThauera

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839271 – 1614-hydroxybenzoyl-CoA reductase subunit gammaAdd BLAST161

Interactioni

Subunit structurei

Heterohexamer of two alpha, two beta and two gamma subunits.2 Publications

Protein-protein interaction databases

DIPiDIP-48468N.

Structurei

Secondary structure

1161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Beta strandi12 – 19Combined sources8
Helixi24 – 30Combined sources7
Beta strandi41 – 46Combined sources6
Beta strandi50 – 53Combined sources4
Beta strandi56 – 59Combined sources4
Helixi60 – 62Combined sources3
Helixi65 – 68Combined sources4
Beta strandi71 – 74Combined sources4
Helixi76 – 78Combined sources3
Beta strandi79 – 81Combined sources3
Helixi87 – 94Combined sources8
Helixi104 – 117Combined sources14
Helixi123 – 129Combined sources7
Turni130 – 132Combined sources3
Beta strandi136 – 138Combined sources3
Helixi141 – 155Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60C/F1-161[»]
1SB3X-ray2.20C/F1-161[»]
ProteinModelPortaliO33818.
SMRiO33818.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST77

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK04107.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017606. 4hydrxbenzoyl-CoA_Rdtase_gsu.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR03193. 4hydroxCoAred. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O33818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNILRLTLN GRAREDLVPD NMLLLDYLRE TVGLTGTKQG CDGGECGACT
60 70 80 90 100
VLVDDRPRLA CSTLAHQVAG KKVETVESLA TQGTLSKLQA AFHEKLGTQC
110 120 130 140 150
GFCTPGMIMA SEALLRKNPS PSRDEIKAAL AGNLCRCTGY VRSSKSVETA
160
AAARLCEEGA R
Length:161
Mass (Da):17,158
Last modified:January 1, 1998 - v1
Checksum:iCC2D8172F8EBA03B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05037.1.

Genome annotation databases

KEGGiag:CAA05037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05037.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60C/F1-161[»]
1SB3X-ray2.20C/F1-161[»]
ProteinModelPortaliO33818.
SMRiO33818.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48468N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA05037.

Phylogenomic databases

KOiK04107.

Enzyme and pathway databases

BioCyciMetaCyc:COHBENREDTHAUERA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO33818.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017606. 4hydrxbenzoyl-CoA_Rdtase_gsu.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR03193. 4hydroxCoAred. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHCRC_THAAR
AccessioniPrimary (citable) accession number: O33818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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.