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Non-heme chloroperoxidase CPO-A1 (CPO-A1) (EC 1.11.1.-) (BPO1) (Bromide peroxidase) (Non-haem bromoperoxidase BPO-A1)

 CPOA1_KITAU             Reviewed;         275 AA.
P33912;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 82.
RecName: Full=Non-heme chloroperoxidase CPO-A1 {ECO:0000303|PubMed:9642069};
Short=CPO-A1;
EC=1.11.1.-;
AltName: Full=BPO1 {ECO:0000303|PubMed:1783900};
AltName: Full=Bromide peroxidase;
AltName: Full=Non-haem bromoperoxidase BPO-A1 {ECO:0000303|PubMed:8012573};
Name=bpoA1;
Kitasatospora aureofaciens (Streptomyces aureofaciens).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Kitasatospora.
NCBI_TaxID=1894;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
12843 / NCIMB 8234 / A-377;
PubMed=8012573; DOI=10.1099/00221287-140-3-509;
Pelletier I., Pfeifer O., Altenbuchner J., van Pee K.-P.;
"Cloning of a second non-haem bromoperoxidase gene from Streptomyces
aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces
lividans and enzyme purification.";
Microbiology 140:509-516(1994).
[2]
PROTEIN SEQUENCE OF 2-21, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
12843 / NCIMB 8234 / A-377;
PubMed=1783900; DOI=10.1099/00221287-137-11-2539;
Weng M., Pfeifer O., Krauss S., Lingens F., van Pee K.-H.;
"Purification, characterization and comparison of two non-haem
bromoperoxidases from Streptomyces aureofaciens ATCC 10762.";
J. Gen. Microbiol. 137:2539-2546(1991).
[3]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-275, AND PROBABLE
CATALYTIC ACTIVITY.
PubMed=9642069; DOI=10.1006/jmbi.1998.1802;
Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H.,
Hecht H.-J.;
"Structural investigation of the cofactor-free chloroperoxidases.";
J. Mol. Biol. 279:889-900(1998).
-!- FUNCTION: May be a chlorinating enzyme involved in 7-
chlorotetracycline biosynthesis. Able to brominate as well.
{ECO:0000269|PubMed:1783900}.
-!- ACTIVITY REGULATION: Brominating activity not inhibited by azide,
peroxidase activity stimulated by bromide.
{ECO:0000269|PubMed:1783900}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1783900}.
-!- SIMILARITY: Belongs to the bacterial non-heme bromo- and chloro-
peroxidases family. {ECO:0000305}.
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EMBL; U01096; AAC43253.1; -; Genomic_DNA.
PIR; S59929; S59929.
RefSeq; WP_030556552.1; NZ_LBHA01000051.1.
PDB; 1A8Q; X-ray; 1.75 A; A=2-275.
PDBsum; 1A8Q; -.
ProteinModelPortal; P33912; -.
SMR; P33912; -.
ESTHER; strau-brpa1; Haloperoxidase.
PeroxiBase; 5911; STaHalNPrx01.
PRIDE; P33912; -.
EvolutionaryTrace; P33912; -.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR000639; Epox_hydrolase-like.
Pfam; PF00561; Abhydrolase_1; 1.
PRINTS; PR00111; ABHYDROLASE.
PRINTS; PR00412; EPOXHYDRLASE.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
Oxidoreductase; Peroxidase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1783900}.
CHAIN 2 275 Non-heme chloroperoxidase CPO-A1.
/FTId=PRO_0000207066.
DOMAIN 22 255 AB hydrolase-1. {ECO:0000255}.
ACT_SITE 95 95 Charge relay system. {ECO:0000305}.
ACT_SITE 224 224 Charge relay system. {ECO:0000305}.
ACT_SITE 253 253 Charge relay system. {ECO:0000305}.
CONFLICT 4 4 C -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 17 17 W -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:1A8Q}.
STRAND 11 17 {ECO:0000244|PDB:1A8Q}.
STRAND 19 26 {ECO:0000244|PDB:1A8Q}.
HELIX 33 36 {ECO:0000244|PDB:1A8Q}.
HELIX 37 45 {ECO:0000244|PDB:1A8Q}.
STRAND 49 53 {ECO:0000244|PDB:1A8Q}.
HELIX 70 83 {ECO:0000244|PDB:1A8Q}.
STRAND 88 94 {ECO:0000244|PDB:1A8Q}.
HELIX 97 108 {ECO:0000244|PDB:1A8Q}.
STRAND 113 120 {ECO:0000244|PDB:1A8Q}.
HELIX 138 163 {ECO:0000244|PDB:1A8Q}.
TURN 164 167 {ECO:0000244|PDB:1A8Q}.
HELIX 175 185 {ECO:0000244|PDB:1A8Q}.
HELIX 190 202 {ECO:0000244|PDB:1A8Q}.
HELIX 206 209 {ECO:0000244|PDB:1A8Q}.
STRAND 216 221 {ECO:0000244|PDB:1A8Q}.
STRAND 225 227 {ECO:0000244|PDB:1A8Q}.
HELIX 229 231 {ECO:0000244|PDB:1A8Q}.
HELIX 233 239 {ECO:0000244|PDB:1A8Q}.
STRAND 244 248 {ECO:0000244|PDB:1A8Q}.
TURN 253 257 {ECO:0000244|PDB:1A8Q}.
HELIX 261 273 {ECO:0000244|PDB:1A8Q}.
SEQUENCE 275 AA; 30475 MW; AA2F6A958C58406E CRC64;
MPICTTRDGV EIFYKDWGQG RPVVFIHGWP LNGDAWQDQL KAVVDAGYRG IAHDRRGHGH
STPVWDGYDF DTFADDLNDL LTDLDLRDVT LVAHSMGGGE LARYVGRHGT GRLRSAVLLS
AIPPVMIKSD KNPDGVPDEV FDALKNGVLT ERSQFWKDTA EGFFSANRPG NKVTQGNKDA
FWYMAMAQTI EGGVRCVDAF GYTDFTEDLK KFDIPTLVVH GDDDQVVPID ATGRKSAQII
PNAELKVYEG SSHGIAMVPG DKEKFNRDLL EFLNK


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