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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Iron-sulfur 1 (2Fe-2S)
Metal bindingi46 – 461Iron-sulfur 1 (2Fe-2S)
Metal bindingi49 – 491Iron-sulfur 1 (2Fe-2S)
Metal bindingi61 – 611Iron-sulfur 1 (2Fe-2S)
Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)
Metal bindingi103 – 1031Iron-sulfur 2 (2Fe-2S)
Metal bindingi135 – 1351Iron-sulfur 2 (2Fe-2S)
Metal bindingi137 – 1371Iron-sulfur 2 (2Fe-2S)

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.
RETL1328306-WGS:GSTH-4498-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1611614-hydroxybenzoyl-CoA reductase subunit gammaPRO_0000083927Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48468N.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi12 – 198Combined sources
Helixi24 – 307Combined sources
Beta strandi41 – 466Combined sources
Beta strandi50 – 534Combined sources
Beta strandi56 – 594Combined sources
Helixi60 – 623Combined sources
Helixi65 – 684Combined sources
Beta strandi71 – 744Combined sources
Helixi76 – 783Combined sources
Beta strandi79 – 813Combined sources
Helixi87 – 948Combined sources
Helixi104 – 11714Combined sources
Helixi123 – 1297Combined sources
Turni130 – 1323Combined sources
Beta strandi136 – 1383Combined sources
Helixi141 – 15515Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO33818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 79772Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

KOiK04107.

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60C/F1-161[»]
1SB3X-ray2.20C/F1-161[»]
ProteinModelPortaliO33818.
SMRiO33818. Positions 1-161.
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.
RETL1328306-WGS:GSTH-4498-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO33818.

Family and domain databases

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...

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 1-19, 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 2 [2FE-2S] CLUSTERS AND SUBUNIT ALPHA AND BETA, COFACTOR, SUBUNIT.

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: May 11, 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.