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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111FAD1 Publication
Binding sitei115 – 1151FAD1 Publication
Binding sitei118 – 1181FAD1 Publication
Metal bindingi122 – 1221Iron-sulfur (4Fe-4S)
Metal bindingi138 – 1381Iron-sulfur (4Fe-4S)
Metal bindingi146 – 1461Iron-sulfur (4Fe-4S)
Metal bindingi155 – 1551Iron-sulfur (4Fe-4S)
Binding sitei162 – 1621FAD1 Publication
Binding sitei224 – 2241FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368FAD1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3243244-hydroxybenzoyl-CoA reductase subunit betaPRO_0000083926Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48467N.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi15 – 217Combined sources
Beta strandi27 – 326Combined sources
Helixi36 – 416Combined sources
Beta strandi48 – 525Combined sources
Turni57 – 604Combined sources
Beta strandi62 – 643Combined sources
Beta strandi70 – 734Combined sources
Helixi78 – 836Combined sources
Helixi85 – 906Combined sources
Helixi92 – 1009Combined sources
Helixi104 – 1096Combined sources
Helixi112 – 1165Combined sources
Turni123 – 1253Combined sources
Helixi129 – 1346Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi147 – 1493Combined sources
Helixi163 – 1697Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi181 – 1866Combined sources
Helixi187 – 1904Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi235 – 24511Combined sources
Beta strandi248 – 26215Combined sources
Helixi269 – 2713Combined sources
Helixi278 – 29114Combined sources
Beta strandi298 – 3003Combined sources
Helixi302 – 32221Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60B/E1-324[»]
1SB3X-ray2.20B/E1-324[»]
ProteinModelPortaliO33820.
SMRiO33820. Positions 1-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33820.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 217216FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 309LAAEATLPL → GTVPVAQLF AA sequence (PubMed:9490068).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60B/E1-324[»]
1SB3X-ray2.20B/E1-324[»]
ProteinModelPortaliO33820.
SMRiO33820. Positions 1-323.
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...

Publicationsi

  1. "4-hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica -- prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins."
    Breese K., Fuchs G.
    Eur. J. Biochem. 251:916-923(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30 AND 169-185, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
    Strain: DSM 6984 / K172.
  2. "Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine oxidase family of molybdenum-containing enzymes."
    Boll M., Fuchs G., Meier C., Trautwein A., El Kasmi A., Ragsdale S.W., Buchanan G., Lowe D.J.
    J. Biol. Chem. 276:47853-47862(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, EPR SPECTROSCOPY, MOSSBAUER SPECTROSCOPY.
    Strain: DSM 6984 / K172.
  3. "Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow."
    Unciuleac M., Warkentin E., Page C.C., Boll M., Ermler U.
    Structure 12:2249-2256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FAD; [4FE-4S] CLUSTER AND SUBUNIT ALPHA AND GAMMA, COFACTOR, SUBUNIT.

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: May 11, 2016
This is version 92 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.