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Protein

2'-hydroxybiphenyl-2-sulfinate desulfinase

Gene

soxB

Organism
Rhodococcus sp. (strain IGTS8)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Part of a pathway to remove covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. This enzyme metabolizes DBT-sulfone (DBTO2 or DBT 5,5-dioxide) to 2-hydroxybiphenyl (2-HBP).

Catalytic activityi

2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite.

Cofactori

FMNCurated

Pathwayi: dibenzothiophene degradation

This protein is involved in the pathway dibenzothiophene degradation, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway dibenzothiophene degradation and in Sulfur metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Monooxygenase, Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-266.
BRENDAi3.13.1.3. 5389.
UniPathwayiUPA00346.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-hydroxybiphenyl-2-sulfinate desulfinase (EC:3.13.1.3)
Alternative name(s):
Dibenzothiophene desulfurization enzyme B
Gene namesi
Name:soxB
Synonyms:dszB
Encoded oniPlasmid unnamed1 Publication
OrganismiRhodococcus sp. (strain IGTS8)
Taxonomic identifieri54064 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3653652'-hydroxybiphenyl-2-sulfinate desulfinasePRO_0000072047Add
BLAST

Interactioni

Subunit structurei

Heterodimer of two subunits, SoxA and SoxB.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 266Combined sources
Helixi32 – 387Combined sources
Helixi41 – 444Combined sources
Beta strandi48 – 514Combined sources
Helixi54 – 585Combined sources
Helixi59 – 624Combined sources
Beta strandi68 – 725Combined sources
Helixi75 – 828Combined sources
Beta strandi88 – 9710Combined sources
Beta strandi100 – 1067Combined sources
Helixi114 – 1174Combined sources
Beta strandi121 – 1244Combined sources
Helixi126 – 1338Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1518Combined sources
Helixi154 – 16613Combined sources
Helixi171 – 1733Combined sources
Beta strandi174 – 1785Combined sources
Turni182 – 1843Combined sources
Helixi188 – 1936Combined sources
Beta strandi194 – 1985Combined sources
Helixi199 – 2024Combined sources
Helixi206 – 21510Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi220 – 2256Combined sources
Helixi226 – 2349Combined sources
Beta strandi237 – 2415Combined sources
Helixi243 – 2453Combined sources
Helixi247 – 2493Combined sources
Beta strandi251 – 2588Combined sources
Helixi259 – 2646Combined sources
Helixi266 – 28318Combined sources
Helixi287 – 29812Combined sources
Helixi302 – 3098Combined sources
Helixi313 – 3153Combined sources
Helixi323 – 33816Combined sources
Helixi348 – 3514Combined sources
Helixi355 – 3617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DE2X-ray1.80A1-365[»]
2DE3X-ray1.60A/B1-365[»]
2DE4X-ray1.80A/B1-365[»]
ProteinModelPortaliP54997.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54997.

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Complete.

P54997-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSRVDPANP GSELDSAIRD TLTYSNCPVP NALLTASESG FLDAAGIELD
60 70 80 90 100
VLSGQQGTVH FTYDQPAYTR FGGEIPPLLS EGLRAPGRTR LLGITPLLGR
110 120 130 140 150
QGFFVRDDSP ITAAADLAGR RIGVSASAIR ILRGQLGDYL ELDPWRQTLV
160 170 180 190 200
ALGSWEARAL LHTLEHGELG VDDVELVPIS SPGVDVPAEQ LEESATVKGA
210 220 230 240 250
DLFPDVARGQ AAVLASGDVD ALYSWLPWAG ELQATGARPV VDLGLDERNA
260 270 280 290 300
YASVWTVSSG LVRQRPGLVQ RLVDAAVDAG LWARDHSDAV TSLHAANLGV
310 320 330 340 350
STGAVGQGFG ADFQQRLVPR LDHDALALLE RTQQFLLTNN LLQEPVALDQ
360
WAAPEFLNNS LNRHR
Length:365
Mass (Da):39,045
Last modified:October 1, 1996 - v1
Checksum:iDA6A867756DA23D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08850 Genomic DNA. Translation: AAA56672.1.
L37363 Genomic DNA. Translation: AAA99483.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08850 Genomic DNA. Translation: AAA56672.1.
L37363 Genomic DNA. Translation: AAA99483.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DE2X-ray1.80A1-365[»]
2DE3X-ray1.60A/B1-365[»]
2DE4X-ray1.80A/B1-365[»]
ProteinModelPortaliP54997.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00346.
BioCyciMetaCyc:MONOMER-266.
BRENDAi3.13.1.3. 5389.

Miscellaneous databases

EvolutionaryTraceiP54997.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiSOXB_RHOSG
AccessioniPrimary (citable) accession number: P54997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Encoded on an unnamed 120 kb plasmid.1 Publication

Keywords - Technical termi

3D-structure, Plasmid

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.