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UniProtKB/Swiss-Prot entry O33819


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HCRA_THAAR
Primary accession number O33819
Secondary accession numbers None
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name 4-hydroxybenzoyl-CoA reductase subunit alpha
Synonym EC 1.3.99.20
Gene name
Name: hcrA
From
Thauera aromatica [TaxID: 59405] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Rhodocyclaceae; Thauera.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-11.
STRAIN=DSM 6984 / K172;
PubMed=9490068 [NCBI, ExPASy, EBI, Israel, Japan]
Breese K., Fuchs G.;
"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.";
Eur. J. Biochem. 251:916-923(1998).
Comments
  • FUNCTION: Catalyzes reductive dehydroxylation of 4-hydroxybenzoyl-CoA. Reaction is not reversible.
  • CATALYTIC ACTIVITY: Benzoyl-CoA + acceptor = 4-hydroxybenzoyl-CoA + reduced acceptor.
  • COFACTOR: FAD.
  • COFACTOR: Iron-sulfur.
  • COFACTOR: Molybdenum.
  • ENZYME REGULATION: Inactivated by low concentrations of cyanide.
  • SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
  • PTM: The N-terminus is blocked.
  • SIMILARITY: To xanthine oxidases.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ001830; CAA05038.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1RM6; X-ray; 1.60 A; A/D=1-769.[ExPASy / RCSB / EBI]
1SB3; X-ray; 2.20 A; A/D=1-769.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1RM6; -.
1SB3; -.
ModBase O33819.
Ontologies
GO
GO:0018525; Molecular function: 4-hydroxybenzoyl-CoA reductase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051536; Molecular function: iron-sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR017607; 4hydrxbenzoyl-CoA_Rdtase_asu.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
Pfam graphical view of domain structure.
Other
ProtoNet O33819.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   769  769     4-hydroxybenzoyl-CoA reductase subunit alpha. PRO_0000083925
CONFLICT   7     7        Q -> E (in Ref. 1; AA sequence). 
HELIX   20    24  5      
HELIX   31    33  3      
STRAND   40    46  7      
STRAND   48    58  11      
HELIX   60    64  5      
STRAND   68    73  6      
HELIX   74    76  3      
STRAND   95    98  4      
STRAND   104   112  9      
HELIX   113   122  10      
STRAND   124   129  6      
HELIX   136   140  5      
STRAND   154   164  11      
HELIX   166   171  6      
STRAND   174   183  10      
STRAND   195   201  7      
TURN   202   205  4      
STRAND   206   211  6      
HELIX   216   227  12      
HELIX   231   233  3      
STRAND   234   237  4      
TURN   245   248  4      
HELIX   253   265  13      
STRAND   267   272  6      
HELIX   275   281  7      
STRAND   287   296  10      
STRAND   302   312  11      
HELIX   320   329  10      
STRAND   332   335  4      
STRAND   340   347  8      
STRAND   350   352  3      
TURN   360   362  3      
HELIX   363   380  18      
HELIX   384   390  7      
STRAND   394   399  6      
HELIX   411   422  12      
HELIX   424   427  4      
STRAND   435   447  13      
STRAND   459   466  8      
STRAND   472   476  5      
STRAND   481   483  3      
HELIX   485   497  13      
HELIX   501   503  3      
STRAND   504   510  7      
TURN   511   513  3      
HELIX   525   551  27      
HELIX   556   558  3      
STRAND   559   562  4      
STRAND   565   568  4      
HELIX   578   586  9      
TURN   587   589  3      
STRAND   591   598  8      
HELIX   602   604  3      
HELIX   611   614  4      
STRAND   621   632  12      
TURN   634   636  3      
STRAND   639   649  11      
HELIX   656   675  20      
STRAND   685   687  3      
TURN   691   693  3      
TURN   699   701  3      
STRAND   704   710  7      
HELIX   718   720  3      
HELIX   732   744  13      
STRAND   750   752  3      
HELIX   755   767  13      
Sequence information
Length: 769 AA [This is the length of the unprocessed precursor] Molecular weight: 82267 Da [This is the MW of the unprocessed precursor] CRC64: 389F7BACFA4D5019 [This is a checksum on the sequence]
        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 

O33819 in FASTA format

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View entry in raw text format (no links)
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