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Protein

4-hydroxybenzoyl-CoA reductase subunit beta

Gene

hcrB

Organism
Thauera aromatica
Status
Reviewed-Annotation score: Annotation score: 5 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

Protein has several cofactor binding sites:

Enzyme regulationi

Inactivated by low concentrations of cyanide in vitro.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111FAD1 Publication1
Binding sitei115FAD1 Publication1
Binding sitei118FAD1 Publication1
Metal bindingi122Iron-sulfur (4Fe-4S)1
Metal bindingi138Iron-sulfur (4Fe-4S)1
Metal bindingi146Iron-sulfur (4Fe-4S)1
Metal bindingi155Iron-sulfur (4Fe-4S)1
Binding sitei162FAD1 Publication1
Binding sitei224FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 36FAD1 Publication8

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:BOHBENREDTHAUERA-MONOMER.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839261 – 3244-hydroxybenzoyl-CoA reductase subunit betaAdd BLAST324

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48467N.

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi15 – 21Combined sources7
Beta strandi27 – 32Combined sources6
Helixi36 – 41Combined sources6
Beta strandi48 – 52Combined sources5
Turni57 – 60Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi70 – 73Combined sources4
Helixi78 – 83Combined sources6
Helixi85 – 90Combined sources6
Helixi92 – 100Combined sources9
Helixi104 – 109Combined sources6
Helixi112 – 116Combined sources5
Turni123 – 125Combined sources3
Helixi129 – 134Combined sources6
Beta strandi141 – 144Combined sources4
Beta strandi147 – 149Combined sources3
Helixi163 – 169Combined sources7
Beta strandi173 – 178Combined sources6
Beta strandi181 – 186Combined sources6
Helixi187 – 190Combined sources4
Beta strandi206 – 212Combined sources7
Beta strandi219 – 225Combined sources7
Beta strandi227 – 231Combined sources5
Beta strandi235 – 245Combined sources11
Beta strandi248 – 262Combined sources15
Helixi269 – 271Combined sources3
Helixi278 – 291Combined sources14
Beta strandi298 – 300Combined sources3
Helixi302 – 322Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60B/E1-324[»]
1SB3X-ray2.20B/E1-324[»]
ProteinModelPortaliO33820.
SMRiO33820.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33820.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 217FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST216

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK04109.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 2 hits.
InterProiIPR017608. 4hydrxbenzoyl-CoA_Rdtase_bsu.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR03195. 4hydrxCoA_B. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O33820-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNILTDFRTH RPATLADAVN ALAAEATLPL GAGTDLLPNL RRGLGHPAAL
60 70 80 90 100
VDLTGIDGLA TISTLADGSL RIGAGATLEA IAEHDAIRTT WPALAQAAES
110 120 130 140 150
VAGPTHRAAA TLGGNLCQDT RCTFYNQSEW WRSGNGYCLK YKGDKCHVIV
160 170 180 190 200
KSDRCYATYH GDVAPALMVL DARAEIVGPA GKRTVPVAQL FRESGAEHLT
210 220 230 240 250
LEKGELLAAI EVPPTGAWSA AYSKVRIRDA VDFPLAGVAA ALQRDGDRIA
260 270 280 290 300
GLRVAITGSN SAPLMVPVDA LLGGNWDDAA AETLAQLVRK TSNVLRTTIT
310 320
GVKYRRRVLL AISRKVVDQL WEAR
Length:324
Mass (Da):34,374
Last modified:January 1, 1998 - v1
Checksum:iC3C5ECAAD093F9DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22 – 30LAAEATLPL → GTVPVAQLF AA sequence (PubMed:9490068).Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05039.1.

Genome annotation databases

KEGGiag:CAA05039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05039.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60B/E1-324[»]
1SB3X-ray2.20B/E1-324[»]
ProteinModelPortaliO33820.
SMRiO33820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48467N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA05039.

Phylogenomic databases

KOiK04109.

Enzyme and pathway databases

BioCyciMetaCyc:BOHBENREDTHAUERA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO33820.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 2 hits.
InterProiIPR017608. 4hydrxbenzoyl-CoA_Rdtase_bsu.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR03195. 4hydrxCoA_B. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHCRB_THAAR
AccessioniPrimary (citable) accession number: O33820
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 94 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.