CPOA1_KITAU
ID CPOA1_KITAU Reviewed; 275 AA.
AC P33912;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Non-heme chloroperoxidase CPO-A1 {ECO:0000303|PubMed:9642069};
DE Short=CPO-A1;
DE EC=1.11.1.-;
DE AltName: Full=BPO1 {ECO:0000303|PubMed:1783900};
DE AltName: Full=Bromide peroxidase;
DE AltName: Full=Non-haem bromoperoxidase BPO-A1 {ECO:0000303|PubMed:8012573};
GN Name=bpoA1;
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
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=8012573; DOI=10.1099/00221287-140-3-509;
RA Pelletier I., Pfeifer O., Altenbuchner J., van Pee K.-P.;
RT "Cloning of a second non-haem bromoperoxidase gene from Streptomyces
RT aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces
RT lividans and enzyme purification.";
RL Microbiology 140:509-516(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC / NCIMB 8234 / A-377;
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 (1.75 ANGSTROMS) OF 2-275, AND PROBABLE CATALYTIC
RP ACTIVITY.
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. Able to brominate as well. {ECO:0000269|PubMed:1783900}.
CC -!- ACTIVITY REGULATION: Brominating activity not inhibited by azide,
CC peroxidase activity stimulated by bromide.
CC {ECO:0000269|PubMed:1783900}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1783900}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC haloperoxidase / perhydrolase family. {ECO:0000305}.
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DR EMBL; U01096; AAC43253.1; -; Genomic_DNA.
DR PIR; S59929; S59929.
DR RefSeq; WP_030556552.1; NZ_LBHA01000051.1.
DR PDB; 1A8Q; X-ray; 1.75 A; A=2-275.
DR PDBsum; 1A8Q; -.
DR AlphaFoldDB; P33912; -.
DR SMR; P33912; -.
DR STRING; 1894.JOER01000052_gene6160; -.
DR ESTHER; strau-brpa1; Haloperoxidase.
DR PeroxiBase; 5911; STaHalNPrx01.
DR eggNOG; COG2267; Bacteria.
DR OMA; EGQIRSW; -.
DR EvolutionaryTrace; P33912; -.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1783900"
FT CHAIN 2..275
FT /note="Non-heme chloroperoxidase CPO-A1"
FT /id="PRO_0000207066"
FT DOMAIN 22..255
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="W -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 138..163
FT /evidence="ECO:0007829|PDB:1A8Q"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:1A8Q"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1A8Q"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:1A8Q"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:1A8Q"
SQ 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
