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

Sepiapterin reductase

Gene

CT0609

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.3 Publications

Catalytic activityi

L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH.2 Publications
L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH.1 Publication

Enzyme regulationi

Slightly inhibited by N-acetyldopamine but not by N-acetylserotonin or melatonin.1 Publication

Kineticsi

For the reverse reaction, accepts L-threo-dihydrobiopterin, D-threo-dihydrobiopterin, L-threo-dihydroneopterin, dihydrotepidopterin and L-erythro-dihydrobiopterin as substrates.1 Publication

  1. KM=21 µM for sepiapterin (at pH 8.8 and 45 degrees Celsius)2 Publications
  2. KM=0.18 µM for sepiapterin (at pH 6.5 and 37 degrees Celsius)2 Publications
  3. KM=6.2 µM for NADPH (at pH 8.8 and 45 degrees Celsius)2 Publications
  1. Vmax=12.0 pmol/min/mg enzyme for the reverse reaction reducing sepapterin (at 37 degrees Celsius)2 Publications

pH dependencei

Optimum pH is around 8.8. Activity drops sharply above and below the optimum and is absent at pH 3 and virtually so at pH 10.6.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Stable at 25 and 50 degrees Celsius for 2 h but loses activity at 70 degrees Celsius in 20 min.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931NADP; via carbonyl oxygen1 Publication
Binding sitei99 – 991Substrate1 Publication
Binding sitei116 – 1161NADP1 Publication
Binding sitei145 – 1451Substrate1 Publication
Binding sitei158 – 1581NADP1 Publication
Binding sitei158 – 1581Substrate1 Publication
Binding sitei162 – 1621NADP1 Publication
Binding sitei196 – 1961Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 157NADP1 Publication
Nucleotide bindingi40 – 423NADP1 Publication
Nucleotide bindingi66 – 672NADP1 Publication
Nucleotide bindingi191 – 1966NADP1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-634-MONOMER.
MetaCyc:MONOMER-13404.

Names & Taxonomyi

Protein namesi
Recommended name:
Sepiapterin reductaseImported (EC:1.1.1.3252 Publications)
Short name:
SPRBy similarity
Short name:
cSR1 Publication
Gene namesi
Ordered Locus Names:CT0609
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991F → A: Drastically reduces activity. Complete loss of activity; when associated with A-196. 1 Publication
Mutagenesisi196 – 1961W → A: Drastically reduces activity. Complete loss of activity; when associated with A-99. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Sepiapterin reductasePRO_0000424153Add
BLAST

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi194439.CT0609.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Turni9 – 113Combined sources
Helixi13 – 2513Combined sources
Turni26 – 283Combined sources
Beta strandi34 – 418Combined sources
Helixi43 – 5412Combined sources
Turni55 – 573Combined sources
Beta strandi59 – 646Combined sources
Helixi70 – 8314Combined sources
Beta strandi88 – 925Combined sources
Helixi102 – 1043Combined sources
Helixi107 – 11711Combined sources
Helixi119 – 13517Combined sources
Beta strandi138 – 1436Combined sources
Helixi146 – 1483Combined sources
Helixi156 – 17621Combined sources
Turni177 – 1804Combined sources
Beta strandi181 – 1888Combined sources
Turni194 – 1963Combined sources
Helixi204 – 2063Combined sources
Helixi210 – 22112Combined sources
Beta strandi227 – 23610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BD0X-ray1.70A/B/C/D1-244[»]
ProteinModelPortaliQ8KES3.
SMRiQ8KES3. Positions 2-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KES3.

Family & Domainsi

Sequence similaritiesi

Belongs to the short-chain dehydrogenases/reductases (SDR) family.By similarity

Phylogenomic databases

eggNOGiENOG4108RZ4. Bacteria.
ENOG4111F16. LUCA.
KOiK17745.
OMAiSGHIFFI.
OrthoDBiEOG6N3CR8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8KES3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHILLITGA GKGIGRAIAL EFARAARHHP DFEPVLVLSS RTAADLEKIS
60 70 80 90 100
LECRAEGALT DTITADISDM ADVRRLTTHI VERYGHIDCL VNNAGVGRFG
110 120 130 140 150
ALSDLTEEDF DYTMNTNLKG TFFLTQALFA LMERQHSGHI FFITSVAATK
160 170 180 190 200
AFRHSSIYCM SKFGQRGLVE TMRLYARKCN VRITDVQPGA VYTPMWGKVD
210 220 230 240
DEMQALMMMP EDIAAPVVQA YLQPSRTVVE EIILRPTSGD IQDD
Length:244
Mass (Da):27,114
Last modified:October 1, 2002 - v1
Checksum:i754CE7BC0363D9DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM71851.1.
RefSeqiNP_661509.1. NC_002932.3.
WP_010932296.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM71851; AAM71851; CT0609.
GeneIDi1006254.
KEGGicte:CT0609.
PATRICi21399285. VBIChlTep116050_0566.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM71851.1.
RefSeqiNP_661509.1. NC_002932.3.
WP_010932296.1. NC_002932.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BD0X-ray1.70A/B/C/D1-244[»]
ProteinModelPortaliQ8KES3.
SMRiQ8KES3. Positions 2-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi194439.CT0609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM71851; AAM71851; CT0609.
GeneIDi1006254.
KEGGicte:CT0609.
PATRICi21399285. VBIChlTep116050_0566.

Phylogenomic databases

eggNOGiENOG4108RZ4. Bacteria.
ENOG4111F16. LUCA.
KOiK17745.
OMAiSGHIFFI.
OrthoDBiEOG6N3CR8.

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-634-MONOMER.
MetaCyc:MONOMER-13404.

Miscellaneous databases

EvolutionaryTraceiQ8KES3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / NBRC 103806 / TLS.
  2. "Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum."
    Cho S.H., Na J.U., Youn H., Hwang C.S., Lee C.H., Kang S.O.
    Biochem. J. 340:497-503(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT.
  3. "Sepiapterin reductases from Chlorobium tepidum and Chlorobium limicola catalyze the synthesis of L-threo-tetrahydrobiopterin from 6-pyruvoyltetrahydropterin."
    Choi Y.K., Jun S.R., Cha E.Y., Park J.S., Park Y.S.
    FEMS Microbiol. Lett. 242:95-99(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  4. "Role of Phe-99 and Trp-196 of sepiapterin reductase from Chlorobium tepidum in the production of L-threo-tetrahydrobiopterin."
    Supangat S., Park S.O., Seo K.H., Lee S.Y., Park Y.S., Lee K.H.
    Acta Biochim. Biophys. Sin. 40:513-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF PHE-99 AND TRP-196.
  5. "Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin."
    Supangat S., Seo K.H., Choi Y.K., Park Y.S., Son D., Han C.D., Lee K.H.
    J. Biol. Chem. 281:2249-2256(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH BIOPTERIN AND NADP, SUBUNIT.

Entry informationi

Entry nameiSPRE_CHLTE
AccessioniPrimary (citable) accession number: Q8KES3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 1, 2002
Last modified: April 13, 2016
This is version 93 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.