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O33819 (HCRA_THAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-hydroxybenzoyl-CoA reductase subunit alpha
EC=1.3.7.9
Gene names
Name:hcrA
OrganismThauera aromatica
Taxonomic identifier59405 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes reductive dehydroxylation of 4-hydroxybenzoyl-CoA. Reaction is not reversible.

Catalytic activity

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

Cofactor

FAD.

Iron-sulfur.

Molybdenum.

Enzyme regulation

Inactivated by low concentrations of cyanide.

Subunit structure

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

Post-translational modification

The N-terminus is blocked.

Sequence similarities

To xanthine oxidases.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7697694-hydroxybenzoyl-CoA reductase subunit alpha
PRO_0000083925

Experimental info

Sequence conflict71Q → E AA sequence Ref.1

Secondary structure

1 ........................................................................................................................... 769
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33819 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 389F7BACFA4D5019

FASTA76982,267
        10         20         30         40         50         60 
MSPKLPQHGT VGVRTPLVDG VEKVTGKAKY TADIAAPDAL VGRILRSPHA HARILAIDTS 

        70         80         90        100        110        120 
AAEALEGVIA VCTGAETPVP FGVLPIAENE YPLARDKVRY RGDPVAAVAA IDEVTAEKAL 

       130        140        150        160        170        180 
ALIKVDYEVL PAYMTPKAAM KAGAIALHDD KPNNILREVH AEFGDVAAAF AEADLIREKT 

       190        200        210        220        230        240 
YTFAEVNHVH MELNATLAEY DPVRDMLTLN TTTQVPYYVH LKVAACLQMD SARIRVIKPF 

       250        260        270        280        290        300 
LGGGFGARTE GLHFEIIAGL LARKAKGTVR LLQTREETFI AHRGRPWTEV KMKIGLKKDG 

       310        320        330        340        350        360 
KIAALALEAT QAGGAYAGYG IITILYTGAL MHGLYHIPAI KHDAWRVYTN TPPCGAMRGH 

       370        380        390        400        410        420 
GTVDTRAAFE ALLTEMGEEL GIDSLKIRQI NMLPQIPYVT MYAQRVMSYG VPECLEKVKA 

       430        440        450        460        470        480 
ASGWEERKGK LPKGRGLGIA LSHFVSGTST PKHWTGEPHA TVNLKLDFDG GITLLTGAAD 

       490        500        510        520        530        540 
IGQGSNTMAS QVAAEVLGVR LSRIRVISAD SALTPKDNGS YSSRVTFMVG NASISAAEEL 

       550        560        570        580        590        600 
KGVLVKAAAK KLDAREEDIE VIDEMFMVSG SQDPGLSFQE VVKAAMVDSG TITVKGTYTC 

       610        620        630        640        650        660 
PTEFQGDKKI RGSAIGATMG FCYAAQVVEA SVDEITGKVT AHKVWVAVDV GKALNPLAVE 

       670        680        690        700        710        720 
GQTQGGVWMG MGQALSEETV YDNGRMVHGN ILDYRVPTIV ESPDIEVIIV ESMDPNGPFG 

       730        740        750        760 
AKEASEGMLA GFLPAIHEAV YEAVGVRATD FPLSPDRITE LLDAKEAAA

« Hide

References

[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: 9490068] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-11.
Strain: DSM 6984 / K172.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ001830 Genomic DNA. Translation: CAA05038.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60A/D1-769[»]
1SB3X-ray2.20A/D1-769[»]
ProteinModelPortalO33819.
SMRO33819. Positions 9-769.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48466N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017607. 4hydrxbenzoyl-CoA_Rdtase_asu.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
Gene3DG3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 6 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF56003. Ald_xan_DH_mo_bd. 1 hit.
SSF54665. Aldxan_dh_hamm. 1 hit.
TIGRFAMsTIGR03194. 4hydrxCoA_A. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHCRA_THAAR
AccessionPrimary (citable) accession number: O33819
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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