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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)DescriptionActionsGraphical viewLength
Binding sitei214Molybdopterin cytosine dinucleotide1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000839251 – 7694-hydroxybenzoyl-CoA reductase subunit alphaAdd BLAST769

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

1769
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 24Combined sources5
Helixi31 – 33Combined sources3
Beta strandi40 – 46Combined sources7
Beta strandi48 – 58Combined sources11
Helixi60 – 64Combined sources5
Beta strandi68 – 73Combined sources6
Helixi74 – 76Combined sources3
Beta strandi95 – 98Combined sources4
Beta strandi104 – 112Combined sources9
Helixi113 – 122Combined sources10
Beta strandi124 – 129Combined sources6
Helixi136 – 140Combined sources5
Beta strandi154 – 164Combined sources11
Helixi166 – 171Combined sources6
Beta strandi174 – 183Combined sources10
Beta strandi195 – 201Combined sources7
Turni202 – 205Combined sources4
Beta strandi206 – 211Combined sources6
Helixi216 – 227Combined sources12
Helixi231 – 233Combined sources3
Beta strandi234 – 237Combined sources4
Turni245 – 248Combined sources4
Helixi253 – 265Combined sources13
Beta strandi267 – 272Combined sources6
Helixi275 – 281Combined sources7
Beta strandi287 – 296Combined sources10
Beta strandi302 – 312Combined sources11
Helixi320 – 329Combined sources10
Beta strandi332 – 335Combined sources4
Beta strandi340 – 347Combined sources8
Beta strandi350 – 352Combined sources3
Turni360 – 362Combined sources3
Helixi363 – 380Combined sources18
Helixi384 – 390Combined sources7
Beta strandi394 – 399Combined sources6
Helixi411 – 422Combined sources12
Helixi424 – 427Combined sources4
Beta strandi435 – 447Combined sources13
Beta strandi459 – 466Combined sources8
Beta strandi472 – 476Combined sources5
Beta strandi481 – 483Combined sources3
Helixi485 – 497Combined sources13
Helixi501 – 503Combined sources3
Beta strandi504 – 510Combined sources7
Turni511 – 513Combined sources3
Helixi525 – 551Combined sources27
Helixi556 – 558Combined sources3
Beta strandi559 – 562Combined sources4
Beta strandi565 – 568Combined sources4
Helixi578 – 586Combined sources9
Turni587 – 589Combined sources3
Beta strandi591 – 598Combined sources8
Helixi602 – 604Combined sources3
Helixi611 – 614Combined sources4
Beta strandi621 – 632Combined sources12
Turni634 – 636Combined sources3
Beta strandi639 – 649Combined sources11
Helixi656 – 675Combined sources20
Beta strandi685 – 687Combined sources3
Turni691 – 693Combined sources3
Turni699 – 701Combined sources3
Beta strandi704 – 710Combined sources7
Helixi718 – 720Combined sources3
Helixi732 – 744Combined sources13
Beta strandi750 – 752Combined sources3
Helixi755 – 767Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO33819.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 245Molybdopterin cytosine dinucleotide binding2
Regioni522 – 526Molybdopterin cytosine dinucleotide binding5
Regioni650 – 655Molybdopterin cytosine dinucleotide binding6
Regioni722 – 725Molybdopterin cytosine dinucleotide binding4

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)DescriptionActionsGraphical viewLength
Sequence conflicti7Q → E AA sequence (PubMed:9490068).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RM6X-ray1.60A/D1-769[»]
1SB3X-ray2.20A/D1-769[»]
ProteinModelPortaliO33819.
SMRiO33819.
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: November 2, 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.