Reviewed, UniProtKB/Swiss-Prot P16544 (ACT3_STRCO)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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

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261

Helix Strand Turn

Details...

Beta strand

8 – 13

6

Helix

17 – 28

12

Beta strand

32 – 38

7

Helix

40 – 51

12

Turn

52 – 54

3

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 – 130

4

Turn

132 – 135

4

Beta strand

137 – 142

6

Helix

145 – 147

3

Helix

155 – 174

20

Turn

175 – 179

5

Beta strand

180 – 187

8

Helix

193 – 205

13

Helix

210 – 218

9

Helix

229 – 240

12

Helix

242 – 244

3

Beta strand

251 – 255

5

Sequences

	Sequence		Length	Mass (Da)
	P16544-1 [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: 2469622] [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: 12000953] [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: 15544323] [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: 15458634] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADPH, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PIR

A28788. JS0108.

RefSeq

NP_629236.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

1100527.

GenomeReviews

Gene locus SCO5086 in contig AL645882_GR.

KEGG

sco:SCO5086.

NMPDR

fig|100226.1.peg.5041.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P16544.

OMA

P16544. GGKQGVV.

Enzyme and pathway databases

BioCyc

SCOE100226:SCO5086-MON.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)