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Protein

4-hydroxybenzoyl-CoA reductase subunit alpha

Gene

hcrA

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

Mo-molybdopterin cytosine dinucleotide2 PublicationsNote: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.2 Publications

Enzyme regulationi

Inactivated by low concentrations of cyanide in vitro.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei214 – 2141Molybdopterin cytosine dinucleotide

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:AOHBENREDTHAUERA-MONOMER.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7697694-hydroxybenzoyl-CoA reductase subunit alphaPRO_0000083925Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiO33819.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48466N.

Structurei

Secondary structure

1
769
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 245Combined sources
Helixi31 – 333Combined sources
Beta strandi40 – 467Combined sources
Beta strandi48 – 5811Combined sources
Helixi60 – 645Combined sources
Beta strandi68 – 736Combined sources
Helixi74 – 763Combined sources
Beta strandi95 – 984Combined sources
Beta strandi104 – 1129Combined sources
Helixi113 – 12210Combined sources
Beta strandi124 – 1296Combined sources
Helixi136 – 1405Combined sources
Beta strandi154 – 16411Combined sources
Helixi166 – 1716Combined sources
Beta strandi174 – 18310Combined sources
Beta strandi195 – 2017Combined sources
Turni202 – 2054Combined sources
Beta strandi206 – 2116Combined sources
Helixi216 – 22712Combined sources
Helixi231 – 2333Combined sources
Beta strandi234 – 2374Combined sources
Turni245 – 2484Combined sources
Helixi253 – 26513Combined sources
Beta strandi267 – 2726Combined sources
Helixi275 – 2817Combined sources
Beta strandi287 – 29610Combined sources
Beta strandi302 – 31211Combined sources
Helixi320 – 32910Combined sources
Beta strandi332 – 3354Combined sources
Beta strandi340 – 3478Combined sources
Beta strandi350 – 3523Combined sources
Turni360 – 3623Combined sources
Helixi363 – 38018Combined sources
Helixi384 – 3907Combined sources
Beta strandi394 – 3996Combined sources
Helixi411 – 42212Combined sources
Helixi424 – 4274Combined sources
Beta strandi435 – 44713Combined sources
Beta strandi459 – 4668Combined sources
Beta strandi472 – 4765Combined sources
Beta strandi481 – 4833Combined sources
Helixi485 – 49713Combined sources
Helixi501 – 5033Combined sources
Beta strandi504 – 5107Combined sources
Turni511 – 5133Combined sources
Helixi525 – 55127Combined sources
Helixi556 – 5583Combined sources
Beta strandi559 – 5624Combined sources
Beta strandi565 – 5684Combined sources
Helixi578 – 5869Combined sources
Turni587 – 5893Combined sources
Beta strandi591 – 5988Combined sources
Helixi602 – 6043Combined sources
Helixi611 – 6144Combined sources
Beta strandi621 – 63212Combined sources
Turni634 – 6363Combined sources
Beta strandi639 – 64911Combined sources
Helixi656 – 67520Combined sources
Beta strandi685 – 6873Combined sources
Turni691 – 6933Combined sources
Turni699 – 7013Combined sources
Beta strandi704 – 7107Combined sources
Helixi718 – 7203Combined sources
Helixi732 – 74413Combined sources
Beta strandi750 – 7523Combined sources
Helixi755 – 76713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60A/D1-769[»]
1SB3X-ray2.20A/D1-769[»]
ProteinModelPortaliO33819.
SMRiO33819. Positions 9-769.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33819.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 2452Molybdopterin cytosine dinucleotide binding
Regioni522 – 5265Molybdopterin cytosine dinucleotide binding
Regioni650 – 6556Molybdopterin cytosine dinucleotide binding
Regioni722 – 7254Molybdopterin cytosine dinucleotide binding

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

KOiK04108.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR017607. 4hydrxbenzoyl-CoA_Rdtase_asu.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsiTIGR03194. 4hydrxCoA_A. 1 hit.

Sequencei

Sequence statusi: Complete.

O33819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPKLPQHGT VGVRTPLVDG VEKVTGKAKY TADIAAPDAL VGRILRSPHA
60 70 80 90 100
HARILAIDTS AAEALEGVIA VCTGAETPVP FGVLPIAENE YPLARDKVRY
110 120 130 140 150
RGDPVAAVAA IDEVTAEKAL ALIKVDYEVL PAYMTPKAAM KAGAIALHDD
160 170 180 190 200
KPNNILREVH AEFGDVAAAF AEADLIREKT YTFAEVNHVH MELNATLAEY
210 220 230 240 250
DPVRDMLTLN TTTQVPYYVH LKVAACLQMD SARIRVIKPF LGGGFGARTE
260 270 280 290 300
GLHFEIIAGL LARKAKGTVR LLQTREETFI AHRGRPWTEV KMKIGLKKDG
310 320 330 340 350
KIAALALEAT QAGGAYAGYG IITILYTGAL MHGLYHIPAI KHDAWRVYTN
360 370 380 390 400
TPPCGAMRGH GTVDTRAAFE ALLTEMGEEL GIDSLKIRQI NMLPQIPYVT
410 420 430 440 450
MYAQRVMSYG VPECLEKVKA ASGWEERKGK LPKGRGLGIA LSHFVSGTST
460 470 480 490 500
PKHWTGEPHA TVNLKLDFDG GITLLTGAAD IGQGSNTMAS QVAAEVLGVR
510 520 530 540 550
LSRIRVISAD SALTPKDNGS YSSRVTFMVG NASISAAEEL KGVLVKAAAK
560 570 580 590 600
KLDAREEDIE VIDEMFMVSG SQDPGLSFQE VVKAAMVDSG TITVKGTYTC
610 620 630 640 650
PTEFQGDKKI RGSAIGATMG FCYAAQVVEA SVDEITGKVT AHKVWVAVDV
660 670 680 690 700
GKALNPLAVE GQTQGGVWMG MGQALSEETV YDNGRMVHGN ILDYRVPTIV
710 720 730 740 750
ESPDIEVIIV ESMDPNGPFG AKEASEGMLA GFLPAIHEAV YEAVGVRATD
760
FPLSPDRITE LLDAKEAAA
Length:769
Mass (Da):82,267
Last modified:January 1, 1998 - v1
Checksum:i389F7BACFA4D5019
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71Q → E AA sequence (PubMed:9490068).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05038.1.

Genome annotation databases

KEGGiag:CAA05038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001830 Genomic DNA. Translation: CAA05038.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60A/D1-769[»]
1SB3X-ray2.20A/D1-769[»]
ProteinModelPortaliO33819.
SMRiO33819. Positions 9-769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48466N.

Proteomic databases

PRIDEiO33819.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA05038.

Phylogenomic databases

KOiK04108.

Enzyme and pathway databases

BioCyciMetaCyc:AOHBENREDTHAUERA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO33819.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR017607. 4hydrxbenzoyl-CoA_Rdtase_asu.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsiTIGR03194. 4hydrxCoA_A. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHCRA_THAAR
AccessioniPrimary (citable) accession number: O33819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 90 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.