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Protein

Putative ketoacyl reductase

Gene

actIII

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADP2 Publications
Binding sitei144 – 1441SubstrateBy similarity
Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation
Binding sitei161 – 1611NADP2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 3929NADP2 PublicationsAdd
BLAST

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00173.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ketoacyl reductase (EC:1.3.1.-)
Gene namesi
Name:actIII
Ordered Locus Names:SCO5086
ORF Names:SCBAC28G1.12c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Putative ketoacyl reductasePRO_0000054447Add
BLAST

Proteomic databases

PRIDEiP16544.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi100226.SCO5086.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi17 – 2812Combined sources
Beta strandi32 – 387Combined sources
Helixi40 – 5213Combined sources
Beta strandi57 – 615Combined sources
Helixi67 – 8014Combined sources
Beta strandi85 – 895Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 11411Combined sources
Helixi116 – 12611Combined sources
Turni127 – 1293Combined sources
Helixi131 – 1344Combined sources
Beta strandi136 – 1427Combined sources
Helixi145 – 1473Combined sources
Helixi155 – 17521Combined sources
Turni176 – 1783Combined sources
Beta strandi179 – 1879Combined sources
Beta strandi189 – 1924Combined sources
Helixi193 – 20614Combined sources
Helixi210 – 22011Combined sources
Helixi229 – 24012Combined sources
Helixi242 – 2443Combined sources
Beta strandi251 – 2555Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W4ZX-ray2.50A/B1-261[»]
1X7GX-ray2.30A/B1-261[»]
1X7HX-ray2.30A/B1-261[»]
1XR3X-ray2.71A/B1-261[»]
2RH4X-ray2.30A/B1-261[»]
2RHCX-ray2.10A/B1-261[»]
2RHRX-ray2.50A/B1-261[»]
3CSDX-ray2.29A/B1-261[»]
3QRWX-ray2.79A/B1-261[»]
3RI3X-ray2.29A/B1-261[»]
4DBZX-ray2.64A/B1-261[»]
4DC0X-ray2.81A/B1-261[»]
4DC1X-ray2.82A/B1-261[»]
ProteinModelPortaliP16544.
SMRiP16544. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16544.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
InParanoidiP16544.
KOiK12420.
OMAiYATSAPY.
OrthoDBiEOG6N3CR8.
PhylomeDBiP16544.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQDSEVAL VTGATSGIGL EIARRLGKEG LRVFVCARGE EGLRTTLKEL
60 70 80 90 100
REAGVEADGR TCDVRSVPEI EALVAAVVER YGPVDVLVNN AGRPGGGATA
110 120 130 140 150
ELADELWLDV VETNLTGVFR VTKQVLKAGG MLERGTGRIV NIASTGGKQG
160 170 180 190 200
VVHAAPYSAS KHGVVGFTKA LGLELARTGI TVNAVCPGFV ETPMAASVRE
210 220 230 240 250
HYSDIWEVST EEAFDRITAR VPIGRYVQPS EVAEMVAYLI GPGAAAVTAQ
260
ALNVCGGLGN Y
Length:261
Mass (Da):27,265
Last modified:August 1, 1990 - v1
Checksum:iB87C83F45A88B7A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19536 Genomic DNA. Translation: AAA26688.1.
AL939122 Genomic DNA. Translation: CAC44199.1.
PIRiJS0108. A28788.
RefSeqiNP_629236.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC44199; CAC44199; CAC44199.
GeneIDi1100527.
KEGGisco:SCO5086.
PATRICi23740012. VBIStrCoe124346_5166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19536 Genomic DNA. Translation: AAA26688.1.
AL939122 Genomic DNA. Translation: CAC44199.1.
PIRiJS0108. A28788.
RefSeqiNP_629236.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W4ZX-ray2.50A/B1-261[»]
1X7GX-ray2.30A/B1-261[»]
1X7HX-ray2.30A/B1-261[»]
1XR3X-ray2.71A/B1-261[»]
2RH4X-ray2.30A/B1-261[»]
2RHCX-ray2.10A/B1-261[»]
2RHRX-ray2.50A/B1-261[»]
3CSDX-ray2.29A/B1-261[»]
3QRWX-ray2.79A/B1-261[»]
3RI3X-ray2.29A/B1-261[»]
4DBZX-ray2.64A/B1-261[»]
4DC0X-ray2.81A/B1-261[»]
4DC1X-ray2.82A/B1-261[»]
ProteinModelPortaliP16544.
SMRiP16544. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5086.

Proteomic databases

PRIDEiP16544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC44199; CAC44199; CAC44199.
GeneIDi1100527.
KEGGisco:SCO5086.
PATRICi23740012. VBIStrCoe124346_5166.

Phylogenomic databases

eggNOGiCOG1028.
InParanoidiP16544.
KOiK12420.
OMAiYATSAPY.
OrthoDBiEOG6N3CR8.
PhylomeDBiP16544.

Enzyme and pathway databases

UniPathwayiUPA00173.

Miscellaneous databases

EvolutionaryTraceiP16544.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor."
    Hallam S., Malpartida F., Hopwood D.
    Gene 74:305-320(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  3. "Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity."
    Korman T.P., Hill J.A., Vu T.N., Tsai S.C.
    Biochemistry 43:14529-14538(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADPH.
  4. "The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding."
    Hadfield A.T., Limpkin C., Teartasin W., Simpson T.J., Crosby J., Crump M.P.
    Structure 12:1865-1875(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADPH, SUBUNIT.

Entry informationi

Entry nameiACT3_STRCO
AccessioniPrimary (citable) accession number: P16544
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: January 7, 2015
This is version 115 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, Reference proteome

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

External Data

Dasty 3

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 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.