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Protein

Pyrogallol hydroxytransferase small subunit

Gene

bthL

Organism
Pelobacter acidigallici
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Isomerization of pyrogallol to phloroglucin.

Catalytic activityi

1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene.

Cofactori

[4Fe-4S] clusterNote: Binds 3 [4Fe-4S] clusters.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi16Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi19Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi23Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi68Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi71Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi76Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi109Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi126Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi129Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi145Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi149Iron-sulfur 1 (4Fe-4S)By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi1.97.1.2. 4585.

Protein family/group databases

TCDBi5.A.3.7.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrogallol hydroxytransferase small subunit (EC:1.97.1.2)
Alternative name(s):
Transhydroxylase subunit beta
Gene namesi
Name:bthL
OrganismiPelobacter acidigallici
Taxonomic identifieri35816 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesDesulfuromonadaceaePelobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000583661 – 274Pyrogallol hydroxytransferase small subunitAdd BLAST274

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi10 – 12Combined sources3
Helixi18 – 27Combined sources10
Turni33 – 35Combined sources3
Beta strandi45 – 54Combined sources10
Beta strandi60 – 66Combined sources7
Helixi75 – 79Combined sources5
Turni80 – 82Combined sources3
Beta strandi83 – 86Combined sources4
Beta strandi92 – 94Combined sources3
Turni96 – 101Combined sources6
Helixi103 – 108Combined sources6
Beta strandi115 – 117Combined sources3
Turni118 – 121Combined sources4
Beta strandi122 – 124Combined sources3
Helixi130 – 133Combined sources4
Helixi144 – 148Combined sources5
Beta strandi154 – 159Combined sources6
Helixi161 – 171Combined sources11
Helixi178 – 180Combined sources3
Beta strandi185 – 190Combined sources6
Helixi192 – 195Combined sources4
Beta strandi197 – 205Combined sources9
Beta strandi214 – 219Combined sources6
Beta strandi222 – 228Combined sources7
Beta strandi233 – 240Combined sources8
Beta strandi242 – 251Combined sources10
Beta strandi254 – 265Combined sources12
Beta strandi267 – 274Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V4CX-ray2.35B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
4V4DX-ray2.20B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
4V4EX-ray2.00B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
ProteinModelPortaliP80564.
SMRiP80564.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80564.

Family & Domainsi

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQYYMVIDV AKCQDCNNCF MGCMDEHELN EWPGYTASMQ RGHRWMNIER
60 70 80 90 100
RERGTYPRND INYRPTPCMH CENAPCVAKG NGAVYQREDG IVLIDPEKAK
110 120 130 140 150
GKKELLDTCP YGVMYWNEEE NVAQKCTMCA HLLDDESWAP KMPRCAHNCG
160 170 180 190 200
SFVYEFLKTT PEAMAKKVEE EGLEVIKPEL GTKPRVYYKN LYRFEKNYVT
210 220 230 240 250
AGILVQGDCF EGAKVVLKSG GKEVASAETN FFGEFKFDAL DNGEYTVEID
260 270
ADGKSYSDTV VIDDKSVDLG FIKL
Length:274
Mass (Da):31,221
Last modified:January 16, 2004 - v2
Checksum:i2F9A9CD24082F5A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243850 Genomic DNA. Translation: CAB50914.1.
PIRiS65429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243850 Genomic DNA. Translation: CAB50914.1.
PIRiS65429.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V4CX-ray2.35B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
4V4DX-ray2.20B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
4V4EX-ray2.00B/D/F/H/J/L/N/P/R/T/V/X1-274[»]
ProteinModelPortaliP80564.
SMRiP80564.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi5.A.3.7.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.97.1.2. 4585.

Miscellaneous databases

EvolutionaryTraceiP80564.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGTS_PELAC
AccessioniPrimary (citable) accession number: P80564
Secondary accession number(s): Q9XAY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 16, 2004
Last modified: November 2, 2016
This is version 73 of the entry and version 2 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

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.