DB code: S00544

CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 1.11.1.-
CSA 1a8q
M-CSA 1a8q
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00344 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P33912 Non-haem bromoperoxidase BPO-A1
EC 1.11.1.-
Bromide peroxidase
BPO1
S33.992 (Serine)
[Graphical View]
P29715 Non-haem bromoperoxidase BPO-A2
EC 1.11.1.-
Bromide peroxidase
BPO2
PF00561 (Abhydrolase_1)
[Graphical View]

KEGG enzyme name

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P29715 BPOA2_STRAU Homotrimer.
P33912 BPA1_STRAU Homodimer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C01371 C01324 C00708 C00027 C00720 C01321 C00001
E.C.
Compound RH Br- I- H2O2 RBr RI H2O
Type lipid halide halide others halide halide H2O
ChEBI 15858
16382
16240
15377
PubChem 259
30165
784
22326046
962
22247451
1a8qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1broA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1broB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1brtA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:_CL Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1a7u, 1a88, 1a8q, 1a8s, 1a8u, 1brt & Swiss-prot;P33912, P29715, O31158, O31168, P49323

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1a8qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 94;ASP 223;HIS 252
1broA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 98;ASP 228;HIS 257
1broB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 98;ASP 228;HIS 257
1brtA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 98;ASP 228;HIS 257 mutant M99T

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.535-536
[3]
p.155-156
[4]
Fig.5, p.895-898
[5]
p.222

References
[1]
Resource
Comments
Medline ID
PubMed ID 786162
Journal Annu Rev Biochem
Year 1976
Volume 45
Pages 861-88
Authors Morrison M, Schonbaum GR
Title Peroxidase-catalyzed halogenation.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Medline ID 95393196
PubMed ID 7664081
Journal Nat Struct Biol
Year 1994
Volume 1
Pages 532-7
Authors Hecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH
Title The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
Related PDB 1bro
Related UniProtKB P29715
[3]
Resource
Comments
Medline ID
PubMed ID 7632719
Journal Biochim Biophys Acta
Year 1995
Volume 1250
Pages 149-57
Authors Pelletier I, Altenbuchner J, Mattes R
Title A catalytic triad is required by the non-heme haloperoxidases to perform halogenation.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
Medline ID 98307994
PubMed ID 9642069
Journal J Mol Biol
Year 1998
Volume 279
Pages 889-900
Authors Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
Title Structural investigation of the cofactor-free chloroperoxidases.
Related PDB 1a7u 1a88 1a8q 1a8s 1a8u 1brt
Related UniProtKB P33912 P29715 O31158 O31168 P49323
[5]
Resource
Comments
Medline ID
PubMed ID 12369917
Journal Curr Protein Pept Sci
Year 2000
Volume 1
Pages 209-35
Authors Holmquist M
Title Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12447906
Journal J Mol Recognit
Year 2002
Volume 15
Pages 291-6
Authors Littlechild J, Garcia-Rodriguez E, Dalby A, Isupov M
Title Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-07-13 2009-02-26