BPOA2_KITAU
ID BPOA2_KITAU Reviewed; 278 AA.
AC P29715;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Non-haem bromoperoxidase BPO-A2;
DE EC=1.11.1.-;
DE AltName: Full=BPO2;
DE AltName: Full=Bromide peroxidase;
GN Name=bpoA2;
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
OG Plasmid pOP2621.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Kitasatospora.
OX NCBI_TaxID=1894;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC / NCIMB 8234 / A-377;
RX PubMed=1527491; DOI=10.1099/00221287-138-6-1123;
RA Pfeifer O., Pelletier I., Altenbuchner J., van Pee K.-H.;
RT "Molecular cloning and sequencing of a non-haem bromoperoxidase gene from
RT Streptomyces aureofaciens ATCC 10762.";
RL J. Gen. Microbiol. 138:1123-1131(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=1783900; DOI=10.1099/00221287-137-11-2539;
RA Weng M., Pfeifer O., Krauss S., Lingens F., van Pee K.-H.;
RT "Purification, characterization and comparison of two non-haem
RT bromoperoxidases from Streptomyces aureofaciens ATCC 10762.";
RL J. Gen. Microbiol. 137:2539-2546(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC / NCIMB 8234 / A-377;
RX PubMed=7664081; DOI=10.1038/nsb0894-532;
RA Hecht H.-J., Sobek H., Haag T., Pfeifer O., van Pee K.-H.;
RT "The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an
RT alpha/beta hydrolase fold.";
RL Nat. Struct. Biol. 1:532-537(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC / NCIMB 8234 / A-377;
RX PubMed=9642069; DOI=10.1006/jmbi.1998.1802;
RA Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H.,
RA Hecht H.-J.;
RT "Structural investigation of the cofactor-free chloroperoxidases.";
RL J. Mol. Biol. 279:889-900(1998).
CC -!- FUNCTION: May be a chlorinating enzyme involved in 7-chlorotetracycline
CC biosynthesis.
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC haloperoxidase / perhydrolase family. {ECO:0000305}.
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DR EMBL; M84990; AAB84315.1; -; Unassigned_DNA.
DR PIR; S27614; S27614.
DR RefSeq; WP_030279028.1; NZ_LBHA01000101.1.
DR PDB; 1BRO; X-ray; 2.05 A; A/B=2-278.
DR PDB; 1BRT; X-ray; 1.50 A; A=2-278.
DR PDB; 3VDX; X-ray; 3.00 A; A/B/C=1-278.
DR PDB; 4D9J; X-ray; 3.92 A; A/B/C/D/E/F/G/H/I/J/K/L=1-278.
DR PDB; 4IQ4; X-ray; 3.50 A; A/B/C/D/E/F=1-278.
DR PDB; 4ITV; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-278.
DR PDB; 4IVJ; X-ray; 7.35 A; A/B/C=1-278.
DR PDB; 4QES; X-ray; 4.19 A; A/B/C=1-278.
DR PDB; 4QF0; X-ray; 6.49 A; A/B/C/D/E/F=1-278.
DR PDB; 4QFF; X-ray; 7.81 A; A/B/C/D/E/F/G/H/I/J/K/L=1-278.
DR PDBsum; 1BRO; -.
DR PDBsum; 1BRT; -.
DR PDBsum; 3VDX; -.
DR PDBsum; 4D9J; -.
DR PDBsum; 4IQ4; -.
DR PDBsum; 4ITV; -.
DR PDBsum; 4IVJ; -.
DR PDBsum; 4QES; -.
DR PDBsum; 4QF0; -.
DR PDBsum; 4QFF; -.
DR AlphaFoldDB; P29715; -.
DR SMR; P29715; -.
DR STRING; 1894.JOER01000004_gene2579; -.
DR ESTHER; strau-brpa2; Haloperoxidase.
DR MEROPS; S33.991; -.
DR PeroxiBase; 5908; STaHalNPrx02.
DR eggNOG; COG2267; Bacteria.
DR OMA; DMWEYQM; -.
DR BRENDA; 1.11.1.18; 5978.
DR EvolutionaryTrace; P29715; -.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
KW Oxidoreductase; Peroxidase; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1783900"
FT CHAIN 2..278
FT /note="Non-haem bromoperoxidase BPO-A2"
FT /id="PRO_0000207067"
FT DOMAIN 26..264
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 99
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 229
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 258
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1BRT"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1BRT"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:1BRT"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1BRT"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1BRT"
SQ SEQUENCE 278 AA; 30385 MW; 955B5A7E20E71FE9 CRC64;
MPFITVGQEN STSIDLYYED HGTGQPVVLI HGFPLSGHSW ERQSAALLDA GYRVITYDRR
GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM GTGEVARYVS SYGTARIAKV
AFLASLEPFL LKTDDNPDGA APQEFFDGIV AAVKADRYAF YTGFFNDFYN LDENLGTRIS
EEAVRNSWNT AASGGFFAAA AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV
FHKALPSAEY VEVEGAPHGL LWTHAEEVNT ALLAFLAK
