PRXC_PSEFL
ID PRXC_PSEFL Reviewed; 274 AA.
AC O31158;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Non-heme chloroperoxidase;
DE EC=1.11.1.-;
DE AltName: Full=Chloride peroxidase;
DE AltName: Full=Chloroperoxidase F;
DE Short=CPO-F;
GN Name=cpo; Synonyms=cpoF;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL914;
RX PubMed=8760926; DOI=10.1099/13500872-142-8-2129;
RA Kirner S., Krauss S., Sury G., Lam S.T., Ligon J.M., van Pee K.-H.;
RT "The non-haem chloroperoxidase from Pseudomonas fluorescens and its
RT relationship to pyrrolnitrin biosynthesis.";
RL Microbiology 142:2129-2135(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC STRAIN=BL914;
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 -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC haloperoxidase / perhydrolase family. {ECO:0000305}.
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DR EMBL; AF031153; AAB86577.1; -; Genomic_DNA.
DR PDB; 1A8S; X-ray; 1.80 A; A=2-274.
DR PDBsum; 1A8S; -.
DR AlphaFoldDB; O31158; -.
DR SMR; O31158; -.
DR ESTHER; psefl-cpoF; Haloperoxidase.
DR PeroxiBase; 5914; PfHalNPrx03_BL914.
DR KEGG; ag:AAB86577; -.
DR EvolutionaryTrace; O31158; -.
DR GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC.
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; Chloride; Oxidoreductase; Peroxidase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..274
FT /note="Non-heme chloroperoxidase"
FT /id="PRO_0000207060"
FT DOMAIN 22..254
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 95
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 225
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT ACT_SITE 254
FT /evidence="ECO:0000250|UniProtKB:P22862"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 138..161
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1A8S"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:1A8S"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1A8S"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:1A8S"
SQ SEQUENCE 274 AA; 29651 MW; 00E2CF31A99E460F CRC64;
MTTFTTRDGT QIYYKDWGSG QPIVFSHGWP LNADSWESQM IFLAAQGYRV IAHDRRGHGR
SSQPWSGNDM DTYADDLAQL IEHLDLRDAV LFGFSTGGGE VARYIGRHGT ARVAKAGLIS
AVPPLMLKTE ANPGGLPMEV FDGIRQASLA DRSQLYKDLA SGPFFGFNQP GAKSSAGMVD
WFWLQGMAAG HKNAYDCIKA FSETDFTEDL KKIDVPTLVV HGDADQVVPI EASGIASAAL
VKGSTLKIYS GAPHGLTDTH KDQLNADLLA FIKG
