Q00441 (CPXJ_SACEN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-deoxyerythronolide B hydroxylase
Short name=6-DEB hydroxylase
EC=1.14.-.-

Alternative name(s):
CYPCVIIA1
Cytochrome P450 107A1
Cytochrome P450eryF
Erythromycin A biosynthesis hydrolase

Gene names

Name:	eryF
Synonyms:	CYP107A1
Ordered Locus Names:	SACE_0730

Organism

Saccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]

Taxonomic identifier

405948 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora › Saccharopolyspora erythraea

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB.
Cofactor	Heme group.
Pathway	Antibiotic biosynthesis; erythromycin biosynthesis.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	A mutated form of this enzyme leads to the formation of deoxyerythromycin A, an antibiotic with improved pharmacological properties.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 404

404

6-deoxyerythronolide B hydroxylase

PRO_0000052220

Sites

Metal binding

351

1

Iron (heme axial ligand)

Experimental info

Sequence conflict

261

1

P → PDQ in CAA42927. Ref.1

Sequence conflict

302

1

G → R in CAA42927. Ref.1

Secondary structure

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404

Helix Strand Turn

Details...

Helix

10 – 12

3

Helix

16 – 26

11

Beta strand

28 – 34

7

Beta strand

37 – 42

6

Helix

45 – 53

9

Helix

73 – 75

3

Helix

80 – 86

7

Beta strand

87 – 89

3

Helix

90 – 92

3

Helix

97 – 106

10

Helix

111 – 116

6

Helix

118 – 130

13

Beta strand

134 – 139

6

Helix

140 – 143

4

Turn

144 – 146

3

Helix

147 – 156

10

Helix

161 – 163

3

Turn

164 – 166

3

Helix

167 – 175

9

Helix

179 – 181

3

Helix

182 – 205

24

Helix

211 – 217

7

Turn

221 – 223

3

Helix

228 – 259

32

Helix

261 – 269

9

Helix

271 – 273

3

Helix

274 – 284

11

Beta strand

291 – 297

7

Beta strand

299 – 301

3

Beta strand

304 – 306

3

Beta strand

311 – 314

4

Helix

316 – 319

4

Turn

323 – 325

3

Beta strand

326 – 328

3

Beta strand

334 – 336

3

Beta strand

342 – 344

3

Helix

347 – 349

3

Helix

354 – 371

18

Beta strand

376 – 379

4

Helix

381 – 383

3

Beta strand

390 – 392

3

Beta strand

399 – 401

3

Sequences

	Sequence		Length	Mass (Da)
	Q00441 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 257ABEFC2D88B3FE	FASTA	404	45,099
	10 20 30 40 50 60 MTTVPDLESD SFHVDWYRTY AELRETAPVT PVRFLGQDAW LVTGYDEAKA ALSDLRLSSD 70 80 90 100 110 120 PKKKYPGVEV EFPAYLGFPE DVRNYFATNM GTSDPPTHTR LRKLVSQEFT VRRVEAMRPR 130 140 150 160 170 180 VEQITAELLD EVGDSGVVDI VDRFAHPLPI KVICELLGVD EKYRGEFGRW SSEILVMDPE 190 200 210 220 230 240 RAEQRGQAAR EVVNFILDLV ERRRTEPGDD LLSALIRVQD DDDGRLSADE LTSIALVLLL 250 260 270 280 290 300 AGFEASVSLI GIGTYLLLTH PDQLALVRRD PSALPNAVEE ILRYIAPPET TTRFAAEEVE 310 320 330 340 350 360 IGGVAIPQYS TVLVANGAAN RDPKQFPDPH RFDVTRDTRG HLSFGQGIHF CMGRPLAKLE 370 380 390 400 GEVALRALFG RFPALSLGID ADDVVWRRSL LLRGIDHLPV RLDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases." Haydock S.F., Dowson J.A., Dhillon N., Roberts G.A., Cortes J., Leadlay P.F. Mol. Gen. Genet. 230:120-128(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea." Weber J.M., Leung J.O., Swanson S.J., Idler K.B., McAlpine J.B. Science 252:114-117(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338." Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F. Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NRRL 23338.
[4]	"Structure of cytochrome P450eryF involved in erythromycin biosynthesis." Cupp-Vickery J.L., Poulos T.L. Nat. Struct. Biol. 2:144-153(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]	"Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity." Cupp-Vickery J., Anderson R., Hatziris Z. Proc. Natl. Acad. Sci. U.S.A. 97:3050-3055(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]	"Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF." Cupp-Vickery J., Garcia C., Hofacre A., McGee-Estrada K. J. Mol. Biol. 311:101-110(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X60379 Genomic DNA. Translation: CAA42927.1.
M54983 Genomic DNA. Translation: AAA26496.1.
AM420293 Genomic DNA. Translation: CAM00071.1.

PIR

S18531.

RefSeq

YP_001102997.1. NC_009142.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EGY	X-ray	2.35	A	3-404	[»]
1EUP	X-ray	2.10	A	3-404	[»]
1JIN	X-ray	2.30	A	3-404	[»]
1JIO	X-ray	2.10	A	2-404	[»]
1JIP	X-ray	2.00	A	2-404	[»]
1OXA	X-ray	2.10	A	3-404	[»]
1Z8O	X-ray	1.70	A	1-404	[»]
1Z8P	X-ray	1.85	A	1-404	[»]
1Z8Q	X-ray	2.00	A	1-404	[»]

ProteinModelPortal

Q00441.

SMR

Q00441. Positions 2-404.

ModBase

Search...

Protein-protein interaction databases

STRING

405948.SACE_0730.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAM00071; CAM00071; SACE_0730.

GeneID

4940591.

KEGG

sen:SACE_0730.

PATRIC

23408848. VBISacEry28377_0744.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000243678.

KO

K14366.

OMA

TWLVTRY.

ProtClustDB

CLSK644214.

Enzyme and pathway databases

UniPathway

UPA00240.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00359. BP450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q00441.

Entry information

Entry name

CPXJ_SACEN

Accession

Primary (citable) accession number: Q00441
Secondary accession number(s): A4F7P7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program