Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Iron-dependent extradiol dioxygenase

Gene

hsaC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the meta-cleavage of 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (3,4-DHSA) to produce 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid (4,9-DSHA).1 Publication

Catalytic activityi

3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 = 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate.1 Publication

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Kineticsi

  1. KM=0.9 µM for 3,4-DHSA (at pH 8 and at 25 degrees Celsius)1 Publication
  2. KM=8.5 µM for 2,3-dihydroxybiphenyl (DHB) (at pH 8 and at 25 degrees Celsius)1 Publication
  1. Vmax=12 µmol/sec/mg enzyme with 3,4-DHSA as substrate (at pH 8 and at 25 degrees Celsius)1 Publication
  2. Vmax=2.5 µmol/sec/mg enzyme with DHB as substrate (at pH 8 and at 25 degrees Celsius)1 Publication

Pathwayi: cholesterol metabolism

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi145 – 1451Iron
Binding sitei200 – 2001Substrate1 Publication
Metal bindingi215 – 2151Iron
Binding sitei215 – 2151Substrate1 Publication
Binding sitei250 – 2501Substrate1 Publication
Binding sitei256 – 2561Substrate1 Publication
Metal bindingi266 – 2661Iron

GO - Molecular functioni

  • 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity Source: MTBBASE
  • ferrous iron binding Source: InterPro
  • iron ion binding Source: MTBBASE

GO - Biological processi

  • aromatic compound catabolic process Source: UniProtKB-KW
  • cholesterol catabolic process Source: MTBBASE
  • pathogenesis Source: MTBBASE
  • response to cholesterol Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Cholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00296.

Chemistry

SwissLipidsiSLP:000001005.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-dependent extradiol dioxygenase (EC:1.13.11.251 Publication)
Gene namesi
Name:hsaC
Synonyms:bphC
Ordered Locus Names:Rv3568c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3568c.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene completely fail to grow on cholesterol due the blockage of the catabolic pathway and develop a pink color consistent with the accumulation of toxic catechols. Mice intravenously infected with the mutant survive substantially longer than those infected with the wild-type.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300Iron-dependent extradiol dioxygenasePRO_0000404507Add
BLAST

Proteomic databases

PaxDbiP9WNW7.

Expressioni

Inductioni

Induced by KstR.1 Publication

Interactioni

Subunit structurei

Homodimer, but may form a homooctamer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3568c.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi16 – 2510Combined sources
Beta strandi40 – 489Combined sources
Beta strandi50 – 556Combined sources
Beta strandi60 – 678Combined sources
Helixi71 – 8414Combined sources
Helixi93 – 997Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi114 – 1196Combined sources
Helixi139 – 1413Combined sources
Beta strandi145 – 1495Combined sources
Helixi153 – 1619Combined sources
Turni162 – 1643Combined sources
Beta strandi167 – 1748Combined sources
Helixi176 – 1794Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi188 – 19912Combined sources
Beta strandi201 – 2077Combined sources
Beta strandi210 – 22213Combined sources
Helixi223 – 23513Combined sources
Beta strandi240 – 25011Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi262 – 2698Combined sources
Turni276 – 2783Combined sources
Beta strandi287 – 2915Combined sources
Helixi294 – 2963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZI8X-ray2.20A/B1-300[»]
2ZYQX-ray2.00A/B1-300[»]
ProteinModelPortaliP9WNW7.
SMRiP9WNW7. Positions 2-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105H37. Bacteria.
COG0346. LUCA.
KOiK16049.
OMAiKMSATLG.
PhylomeDBiP9WNW7.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WNW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIRSLGYLR IEATDMAAWR EYGLKVLGMV EGKGAPEGAL YLRMDDFPAR
60 70 80 90 100
LVVVPGEHDR LLEAGWECAN AEGLQEIRNR LDLEGTPYKE ATAAELADRR
110 120 130 140 150
VDEMIRFADP SGNCLEVFHG TALEHRRVVS PYGHRFVTGE QGMGHVVLST
160 170 180 190 200
RDDAEALHFY RDVLGFRLRD SMRLPPQMVG RPADGPPAWL RFFGCNPRHH
210 220 230 240 250
SLAFLPMPTS SGIVHLMVEV EQADDVGLCL DRALRRKVPM SATLGRHVND
260 270 280 290 300
LMLSFYMKTP GGFDIEFGCE GRQVDDRDWI ARESTAVSLW GHDFTVGARG
Length:300
Mass (Da):33,582
Last modified:April 16, 2014 - v1
Checksum:i2AA94528D119ACB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46391.1.
PIRiF70605.
RefSeqiNP_218085.1. NC_000962.3.
WP_003419378.1. NZ_KK339374.1.

Genome annotation databases

EnsemblBacteriaiCCP46391; CCP46391; Rv3568c.
GeneIDi887886.
KEGGimtu:Rv3568c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46391.1.
PIRiF70605.
RefSeqiNP_218085.1. NC_000962.3.
WP_003419378.1. NZ_KK339374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZI8X-ray2.20A/B1-300[»]
2ZYQX-ray2.00A/B1-300[»]
ProteinModelPortaliP9WNW7.
SMRiP9WNW7. Positions 2-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3568c.

Chemistry

SwissLipidsiSLP:000001005.

Proteomic databases

PaxDbiP9WNW7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46391; CCP46391; Rv3568c.
GeneIDi887886.
KEGGimtu:Rv3568c.

Organism-specific databases

TubercuListiRv3568c.

Phylogenomic databases

eggNOGiENOG4105H37. Bacteria.
COG0346. LUCA.
KOiK16049.
OMAiKMSATLG.
PhylomeDBiP9WNW7.

Enzyme and pathway databases

UniPathwayiUPA00296.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSAC_MYCTU
AccessioniPrimary (citable) accession number: P9WNW7
Secondary accession number(s): L0TFW3, P96850, Q7D597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 9, 2015
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cholesterol metabolism contributes to the survival of M.tuberculosis in the host by helping the bacterial multiplication during earlier stages of infection and to the dissemination of the pathogen in the host.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.