P16544 (ACT3_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative ketoacyl reductase
EC=1.3.1.-

Gene names

Name:	actIII
Ordered Locus Names:	SCO5086
ORF Names:	SCBAC28G1.12c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Pathway	Antibiotic biosynthesis; actinorhodin biosynthesis.
Subunit structure	Homotetramer. Ref.4
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Putative ketoacyl reductase

PRO_0000054447

Regions

Nucleotide binding

11 – 39

29

NADP

Sites

Active site

157

1

Proton acceptor By similarity

Binding site

38

1

NADP

Binding site

63

1

NADP

Binding site

144

1

Substrate By similarity

Binding site

161

1

NADP

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

261

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

17 – 28

12

Beta strand

32 – 38

7

Helix

40 – 52

13

Beta strand

57 – 61

5

Helix

67 – 80

14

Beta strand

85 – 89

5

Helix

99 – 101

3

Helix

104 – 114

11

Helix

116 – 126

11

Turn

127 – 129

3

Helix

131 – 134

4

Beta strand

136 – 142

7

Helix

145 – 147

3

Helix

155 – 175

21

Turn

176 – 178

3

Beta strand

179 – 187

9

Beta strand

189 – 192

4

Helix

193 – 206

14

Helix

210 – 220

11

Helix

229 – 240

12

Helix

242 – 244

3

Beta strand

251 – 255

5

Sequences

	Sequence		Length	Mass (Da)
	P16544 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: B87C83F45A88B7A9	FASTA	261	27,265
	10 20 30 40 50 60 MATQDSEVAL VTGATSGIGL EIARRLGKEG LRVFVCARGE EGLRTTLKEL REAGVEADGR 70 80 90 100 110 120 TCDVRSVPEI EALVAAVVER YGPVDVLVNN AGRPGGGATA ELADELWLDV VETNLTGVFR 130 140 150 160 170 180 VTKQVLKAGG MLERGTGRIV NIASTGGKQG VVHAAPYSAS KHGVVGFTKA LGLELARTGI 190 200 210 220 230 240 TVNAVCPGFV ETPMAASVRE HYSDIWEVST EEAFDRITAR VPIGRYVQPS EVAEMVAYLI 250 260 GPGAAAVTAQ ALNVCGGLGN Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19536 Genomic DNA. Translation: AAA26688.1.
AL939122 Genomic DNA. Translation: CAC44199.1.

PIR

A28788. JS0108.

RefSeq

NP_629236.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W4Z	X-ray	2.50	A/B	1-261	[»]
1X7G	X-ray	2.30	A/B	1-261	[»]
1X7H	X-ray	2.30	A/B	1-261	[»]
1XR3	X-ray	2.71	A/B	1-261	[»]
2RH4	X-ray	2.30	A/B	1-261	[»]
2RHC	X-ray	2.10	A/B	1-261	[»]
2RHR	X-ray	2.50	A/B	1-261	[»]
3CSD	X-ray	2.29	A/B	1-261	[»]
3QRW	X-ray	2.79	A/B	1-261	[»]
3RI3	X-ray	2.29	A/B	1-261	[»]
4DBZ	X-ray	2.64	A/B	1-261	[»]
4DC0	X-ray	2.81	A/B	1-261	[»]
4DC1	X-ray	2.82	A/B	1-261	[»]

ProteinModelPortal

P16544.

SMR

P16544. Positions 1-261.

ModBase

Search...

Protein-protein interaction databases

STRING

100226.SCO5086.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAC44199; CAC44199; CAC44199.

GeneID

1100527.

KEGG

sco:SCO5086.

PATRIC

23740012. VBIStrCoe124346_5166.

Phylogenomic databases

eggNOG

COG1028.

KO

K12420.

ProtClustDB

CLSK636083.

Enzyme and pathway databases

UniPathway

UPA00173.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PIRSF

PIRSF000126. 11-beta-HSD1. 1 hit.

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16544.

Entry information

Entry name

ACT3_STRCO

Accession

Primary (citable) accession number: P16544

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program