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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
Binding sitei93NADP; via carbonyl oxygen1 Publication1
Binding sitei99Substrate1 Publication1
Binding sitei116NADP1 Publication1
Binding sitei145Substrate1 Publication1
Binding sitei158NADP1 Publication1
Binding sitei158Substrate1 Publication1
Binding sitei162NADP1 Publication1
Binding sitei196Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 15NADP1 Publication7
Nucleotide bindingi40 – 42NADP1 Publication3
Nucleotide bindingi66 – 67NADP1 Publication2
Nucleotide bindingi191 – 196NADP1 Publication6

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc: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)DescriptionActionsGraphical viewLength
Mutagenesisi99F → A: Drastically reduces activity. Complete loss of activity; when associated with A-196. 1 Publication1
Mutagenesisi196W → A: Drastically reduces activity. Complete loss of activity; when associated with A-99. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004241531 – 244Sepiapterin reductaseAdd BLAST244

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi194439.CT0609.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Turni9 – 11Combined sources3
Helixi13 – 25Combined sources13
Turni26 – 28Combined sources3
Beta strandi34 – 41Combined sources8
Helixi43 – 54Combined sources12
Turni55 – 57Combined sources3
Beta strandi59 – 64Combined sources6
Helixi70 – 83Combined sources14
Beta strandi88 – 92Combined sources5
Helixi102 – 104Combined sources3
Helixi107 – 117Combined sources11
Helixi119 – 135Combined sources17
Beta strandi138 – 143Combined sources6
Helixi146 – 148Combined sources3
Helixi156 – 176Combined sources21
Turni177 – 180Combined sources4
Beta strandi181 – 188Combined sources8
Turni194 – 196Combined sources3
Helixi204 – 206Combined sources3
Helixi210 – 221Combined sources12
Beta strandi227 – 236Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BD0X-ray1.70A/B/C/D1-244[»]
ProteinModelPortaliQ8KES3.
SMRiQ8KES3.
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.
OMAiVRITNVM.
OrthoDBiPOG091H00PO.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BD0X-ray1.70A/B/C/D1-244[»]
ProteinModelPortaliQ8KES3.
SMRiQ8KES3.
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.
OMAiVRITNVM.
OrthoDBiPOG091H00PO.

Enzyme and pathway databases

BioCyciMetaCyc: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...

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: November 2, 2016
This is version 96 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.