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Protein

4-hydroxyphenylacetate 3-monooxygenase oxygenase component

Gene

TTHA0960

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Utilizes FADH2 supplied by HpaC, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).1 Publication

Catalytic activityi

4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O.1 Publication

Pathwayi: 4-hydroxyphenylacetate degradation

This protein is involved in step 1 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. 4-hydroxyphenylacetate 3-monooxygenase reductase component (TTHA0961), 4-hydroxyphenylacetate 3-monooxygenase oxygenase component (TTHA0960)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421Substrate1 Publication
Binding sitei185 – 1851FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1443FAD1 Publication
Nucleotide bindingi148 – 1514FAD1 Publication
Nucleotide bindingi444 – 4474FAD1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-991-MONOMER.
BRENDAi1.14.14.9. 2305.
UniPathwayiUPA00208; UER00416.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxyphenylacetate 3-monooxygenase oxygenase component (EC:1.14.14.9)
Alternative name(s):
4-HPA 3-hydroxylase
4-HPA 3-monooxygenase large component
Gene namesi
Ordered Locus Names:TTHA0960
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4814814-hydroxyphenylacetate 3-monooxygenase oxygenase componentPRO_0000387994Add
BLAST

Interactioni

Subunit structurei

Homotetramer consisting of a dimer of dimers. 4-HPA 3-monooxygenase consists of a reductase component HpaC and an oxygenase component HpaB.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0960.

Structurei

Secondary structure

1
481
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Beta strandi19 – 213Combined sources
Turni29 – 313Combined sources
Turni33 – 353Combined sources
Helixi36 – 4813Combined sources
Turni52 – 543Combined sources
Helixi55 – 584Combined sources
Beta strandi59 – 624Combined sources
Beta strandi65 – 684Combined sources
Helixi69 – 713Combined sources
Helixi77 – 9317Combined sources
Turni94 – 963Combined sources
Helixi103 – 11412Combined sources
Helixi116 – 1227Combined sources
Helixi123 – 13614Combined sources
Beta strandi140 – 1445Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi172 – 18514Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi198 – 2003Combined sources
Helixi205 – 2073Combined sources
Beta strandi209 – 2146Combined sources
Beta strandi220 – 2245Combined sources
Turni234 – 2363Combined sources
Turni238 – 2425Combined sources
Beta strandi247 – 25812Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 27811Combined sources
Helixi280 – 30930Combined sources
Helixi312 – 3143Combined sources
Helixi316 – 34126Combined sources
Helixi355 – 38026Combined sources
Helixi381 – 3844Combined sources
Helixi390 – 3945Combined sources
Helixi398 – 4047Combined sources
Beta strandi408 – 4103Combined sources
Helixi412 – 42413Combined sources
Turni425 – 4273Combined sources
Helixi429 – 44012Combined sources
Helixi445 – 45511Combined sources
Helixi459 – 46810Combined sources
Helixi470 – 4734Combined sources
Helixi474 – 4763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YYGX-ray2.00A1-481[»]
2YYIX-ray1.66A1-481[»]
2YYJX-ray1.66A1-481[»]
2YYKX-ray1.60A1-481[»]
2YYLX-ray1.75A1-481[»]
2YYMX-ray1.70A1-481[»]
ProteinModelPortaliQ5SJP8.
SMRiQ5SJP8. Positions 2-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SJP8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1045Substrate binding
Regioni197 – 1982Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EFA. Bacteria.
COG2368. LUCA.
HOGENOMiHOG000145842.
KOiK00483.
OMAiRIWEINS.
OrthoDBiEOG6P3337.
PhylomeDBiQ5SJP8.

Family and domain databases

InterProiIPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
IPR004925. HpaB/PvcC/4-BUDH.
IPR024719. HpaB/PvcC/4-BUDH_C.
IPR024674. HpaB/PvcC/4-BUDH_N.
IPR012687. HpaB_Deino-type.
[Graphical view]
PfamiPF03241. HpaB. 1 hit.
PF11794. HpaB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000331. HpaA_HpaB. 1 hit.
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
TIGRFAMsiTIGR02309. HpaB-1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SJP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTGAEYIE ALKTRPPNLW YKGEKVEDPT THPVFRGIVR TMAALYDLQH
60 70 80 90 100
DPRYREVLTY EEEGKRHGMS FLIPKTKEDL KRRGQAYKLW ADQNLGMMGR
110 120 130 140 150
SPDYLNAVVM AYAASADYFG EFAENVRNYY RYLRDQDLAT THALTNPQVN
160 170 180 190 200
RARPPSGQPD PYIPVGVVKQ TEKGIVVRGA RMTATFPLAD EVLIFPSTLL
210 220 230 240 250
QAGSEKYALA FALPTSTPGL HFVCREALVG GDSPFDHPLS SRVEEMDCLV
260 270 280 290 300
IFDDVLVPWE RVFILGNVEL CNNAYAATGA LNHMAHQVVA LKTAKTEAFL
310 320 330 340 350
GVAALMAEGI GADVYGHVQE KIAEIIVYLE AMRAFWTRAE EEAKENAYGL
360 370 380 390 400
LVPDRGALDG ARNLYPRLYP RIREILEQIG ASGLITLPSE KDFKGPLGPF
410 420 430 440 450
LEKFLQGAAL EAKERVALFR LAWDMTLSGF GARQELYERF FFGDPVRMYQ
460 470 480
TLYNVYNKEP YKERIRAFLK ESLKVFEEVQ A
Length:481
Mass (Da):54,303
Last modified:December 21, 2004 - v1
Checksum:i29ED75B3C034FBC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70783.1.
RefSeqiWP_011228328.1. NC_006461.1.
YP_144226.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70783; BAD70783; BAD70783.
GeneIDi3170066.
KEGGittj:TTHA0960.
PATRICi23956882. VBITheThe93045_0942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70783.1.
RefSeqiWP_011228328.1. NC_006461.1.
YP_144226.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YYGX-ray2.00A1-481[»]
2YYIX-ray1.66A1-481[»]
2YYJX-ray1.66A1-481[»]
2YYKX-ray1.60A1-481[»]
2YYLX-ray1.75A1-481[»]
2YYMX-ray1.70A1-481[»]
ProteinModelPortaliQ5SJP8.
SMRiQ5SJP8. Positions 2-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70783; BAD70783; BAD70783.
GeneIDi3170066.
KEGGittj:TTHA0960.
PATRICi23956882. VBITheThe93045_0942.

Phylogenomic databases

eggNOGiENOG4105EFA. Bacteria.
COG2368. LUCA.
HOGENOMiHOG000145842.
KOiK00483.
OMAiRIWEINS.
OrthoDBiEOG6P3337.
PhylomeDBiQ5SJP8.

Enzyme and pathway databases

UniPathwayiUPA00208; UER00416.
BioCyciTTHE300852:GH8R-991-MONOMER.
BRENDAi1.14.14.9. 2305.

Miscellaneous databases

EvolutionaryTraceiQ5SJP8.

Family and domain databases

InterProiIPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
IPR004925. HpaB/PvcC/4-BUDH.
IPR024719. HpaB/PvcC/4-BUDH_C.
IPR024674. HpaB/PvcC/4-BUDH_N.
IPR012687. HpaB_Deino-type.
[Graphical view]
PfamiPF03241. HpaB. 1 hit.
PF11794. HpaB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000331. HpaA_HpaB. 1 hit.
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
TIGRFAMsiTIGR02309. HpaB-1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystal structure of the oxygenase component (hpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8."
    Kim S.-H., Hisano T., Takeda K., Iwasaki W., Ebihara A., Miki K.
    J. Biol. Chem. 282:33107-33117(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FAD, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBUNIT.

Entry informationi

Entry nameiHPAB_THET8
AccessioniPrimary (citable) accession number: Q5SJP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: December 21, 2004
Last modified: November 11, 2015
This is version 74 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, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.