P29715 (BPOA2_STRAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-haem bromoperoxidase BPO-A2
EC=1.11.1.-

Alternative name(s):
BPO2
Bromide peroxidase

Gene names

Name:

bpoA2

Encoded on

Plasmid pOP2621

Organism

Streptomyces aureofaciens

Taxonomic identifier

1894 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.
Subunit structure	Homotrimer.
Sequence similarities	Belongs to the bacterial non-heme bromo- and chloro-peroxidases family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peroxidase 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 278

277

Non-haem bromoperoxidase BPO-A2

PRO_0000207067

Sites

Active site

99

1

By similarity

Active site

229

1

By similarity

Active site

258

1

By similarity

Secondary structure

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278

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Beta strand

12 – 21

10

Beta strand

23 – 30

8

Helix

37 – 40

4

Helix

41 – 49

9

Beta strand

53 – 57

5

Helix

74 – 88

15

Beta strand

92 – 98

7

Helix

101 – 112

12

Beta strand

117 – 124

8

Helix

143 – 155

13

Helix

157 – 169

13

Helix

171 – 174

4

Turn

176 – 178

3

Helix

181 – 192

12

Helix

196 – 205

10

Turn

211 – 213

3

Helix

214 – 216

3

Beta strand

221 – 226

6

Beta strand

230 – 232

3

Turn

234 – 237

4

Helix

238 – 244

7

Beta strand

248 – 253

6

Helix

260 – 263

4

Helix

265 – 277

13

Sequences

	Sequence		Length	Mass (Da)
	P29715 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 955B5A7E20E71FE9	FASTA	278	30,385
	10 20 30 40 50 60 MPFITVGQEN STSIDLYYED HGTGQPVVLI HGFPLSGHSW ERQSAALLDA GYRVITYDRR 70 80 90 100 110 120 GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM GTGEVARYVS SYGTARIAKV 130 140 150 160 170 180 AFLASLEPFL LKTDDNPDGA APQEFFDGIV AAVKADRYAF YTGFFNDFYN LDENLGTRIS 190 200 210 220 230 240 EEAVRNSWNT AASGGFFAAA AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV 250 260 270 FHKALPSAEY VEVEGAPHGL LWTHAEEVNT ALLAFLAK

References

[1]	"Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762." Pfeifer O., Pelletier I., Altenbuchner J., van Pee K.-H. J. Gen. Microbiol. 138:1123-1131(1992) [PubMed: 1527491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.
[2]	"Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762." Weng M., Pfeifer O., Krauss S., Lingens F., van Pee K.-H. J. Gen. Microbiol. 137:2539-2546(1991) [PubMed: 1783900] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[3]	"The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold." Hecht H.-J., Sobek H., Haag T., Pfeifer O., van Pee K.-H. Nat. Struct. Biol. 1:532-537(1994) [PubMed: 7664081] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.
[4]	"Structural investigation of the cofactor-free chloroperoxidases." Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H., Hecht H.-J. J. Mol. Biol. 279:889-900(1998) [PubMed: 9642069] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M84990 Unassigned DNA. Translation: AAB84315.1.

PIR

S27614.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BRO	X-ray	2.05	A/B	2-278	[»]
1BRT	X-ray	1.50	A	2-278	[»]

ProteinModelPortal

P29715.

SMR

P29715. Positions 2-278.

ModBase

Search...

Protein family/group databases

PeroxiBase

5908. STaHalNPrx02.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

PRINTS

PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.

ProtoNet

Search...

Entry information

Entry name

BPOA2_STRAU

Accession

Primary (citable) accession number: P29715

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 28, 2011
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program