ID   OXD_BACSX               Reviewed;         351 AA.
AC   P82604;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Phenylacetaldoxime dehydratase;
DE            EC=4.99.1.7;
GN   Name=oxd;
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13; 60-73; 89-98;
RP   246-259 AND 300-312, AND CHARACTERIZATION.
RX   PubMed=10651646; DOI=10.1021/bi991598u;
RA   Kato Y., Nakamura K., Sakiyama H., Mayhew S.G., Asano Y.;
RT   "Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus
RT   sp. strain OxB-1: purification, characterization, and molecular cloning of
RT   the gene.";
RL   Biochemistry 39:800-809(2000).
CC   -!- FUNCTION: Catalyzes the stoichiometric dehydration of Z-
CC       phenylacetaldoxime to phenylacetonitrile. Prefers the Z-form of
CC       phenylacetaldoxime over its E-isomer.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(Z)-phenylacetaldehyde oxime = H2O + phenylacetonitrile;
CC         Xref=Rhea:RHEA:20069, ChEBI:CHEBI:15377, ChEBI:CHEBI:25979,
CC         ChEBI:CHEBI:50723; EC=4.99.1.7;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
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DR   EMBL; AB028892; BAA90461.1; -; Genomic_DNA.
DR   RefSeq; WP_041072592.1; NZ_AP013294.1.
DR   AlphaFoldDB; P82604; -.
DR   SMR; P82604; -.
DR   STRING; 98228.OXB_1097; -.
DR   OrthoDB; 515450at2; -.
DR   BioCyc; MetaCyc:MON-15570; -.
DR   BRENDA; 4.99.1.7; 691.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018814; F:phenylacetaldoxime dehydratase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR025702; Haem-containing_dehydratase.
DR   Pfam; PF13816; Dehydratase_hem; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Heme; Iron; Lyase;
KW   Metal-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10651646"
FT   CHAIN           2..351
FT                   /note="Phenylacetaldoxime dehydratase"
FT                   /id="PRO_0000058108"
SQ   SEQUENCE   351 AA;  40151 MW;  B06B2C57890FD98A CRC64;
     MKNMPENHNP QANAWTAEFP PEMSYVVFAQ IGIQSKSLDH AAEHLGMMKK SFDLRTGPKH
     VDRALHQGAD GYQDSIFLAY WDEPETFKSW VADPEVQKWW SGKKIDENSP IGYWSEVTTI
     PIDHFETLHS GENYDNGVSH FVPIKHTEVH EYWGAMRDRM PVSASSDLES PLGLQLPEPI
     VRESFGKRLK VTAPDNICLI RTAQNWSKCG SGERETYIGL VEPTLIKANT FLRENASETG
     CISSKLVYEQ THDGEIVDKS CVIGYYLSMG HLERWTHDHP THKAIYGTFY EMLKRHDFKT
     ELALWHEVSV LQSKDIELIY VNCHPSTGFL PFFEVTEIQE PLLKSPSVRI Q