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Protein

Sepiapterin reductase

Gene

CT0609

Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Status
Reviewed-Annotation score: -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)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

Keywordsi

Molecular functionOxidoreductase
LigandNADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciCTEP194439:G1FZE-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
OrganismiChlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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
OMAiNIQPDSH
OrthoDBiPOG091H00PO

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
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
PATRICifig|194439.7.peg.566

Similar proteinsi

Entry informationi

Entry nameiSPRE_CHLTE
AccessioniPrimary (citable) accession number: Q8KES3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 1, 2002
Last modified: March 28, 2018
This is version 103 of the entry and version 1 of the sequence. See 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

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