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Protein
Submitted name:

Phenol 2-hydroxylase component B

Gene

pheA2

Organism
Geobacillus thermoglucosidasius (Bacillus thermoglucosidasius)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71NADCombined sources
Binding sitei28 – 281FAD; via carbonyl oxygenCombined sources
Binding sitei34 – 341NADCombined sources
Binding sitei38 – 381NADCombined sources
Binding sitei123 – 1231NADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 354FADCombined sources
Nucleotide bindingi49 – 513FADCombined sources
Nucleotide bindingi55 – 562FADCombined sources
Nucleotide bindingi81 – 833FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, NADCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

SABIO-RKQ9LAG2.

Names & Taxonomyi

Protein namesi
Submitted name:
Phenol 2-hydroxylase component BImported
Gene namesi
Name:pheA2Imported
OrganismiGeobacillus thermoglucosidasius (Bacillus thermoglucosidasius)Imported
Taxonomic identifieri1426 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZ0X-ray2.20A/B/C/D/E/F/G/H1-161[»]
1RZ1X-ray2.10A/B/C/D/E/F/G/H1-161[»]
ProteinModelPortaliQ9LAG2.
SMRiQ9LAG2. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LAG2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 150141Flavin_ReductInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR002563. Flavin_Rdtase-like_dom.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01613. Flavin_Reduct. 1 hit.
[Graphical view]
SMARTiSM00903. Flavin_Reduct. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LAG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDRLFRNAM GKFATGVTVI TTELNGAVHG MTANAFMSVS LNPKLVLVSI
60 70 80 90 100
GEKAKMLEKI QQSKKYAVNI LSQDQKVLSM NFAGQLEKPV DVQFEELGGL
110 120 130 140 150
PVIKDALAQI SCQVVNEVQA GDHTLFIGEV TDIKITEQDP LLFFSGKYHQ
160
LAQNEKVETS S
Length:161
Mass (Da):17,658
Last modified:October 1, 2000 - v1
Checksum:iA13D8802E021350D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140605 Genomic DNA. Translation: AAF66547.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140605 Genomic DNA. Translation: AAF66547.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZ0X-ray2.20A/B/C/D/E/F/G/H1-161[»]
1RZ1X-ray2.10A/B/C/D/E/F/G/H1-161[»]
ProteinModelPortaliQ9LAG2.
SMRiQ9LAG2. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ9LAG2.

Miscellaneous databases

EvolutionaryTraceiQ9LAG2.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR002563. Flavin_Rdtase-like_dom.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01613. Flavin_Reduct. 1 hit.
[Graphical view]
SMARTiSM00903. Flavin_Reduct. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Phenol/cresol degradation by the thermophilic Bacillus thermoglucosidasius A7: cloning and sequence analysis of five genes involved in the pathway."
    Duffner F.M., Kirchner U., Bauer M.P., Muller R.
    Gene 256:215-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A7Imported.
  2. "Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action."
    van den Heuvel R.H., Westphal A.H., Heck A.J., Walsh M.A., Rovida S., van Berkel W.J., Mattevi A.
    J. Biol. Chem. 279:12860-12867(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FAD AND NAD.

Entry informationi

Entry nameiQ9LAG2_GEOTM
AccessioniPrimary (citable) accession number: Q9LAG2
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.