ID   C7E716_9PSED            Unreviewed;       469 AA.
AC   C7E716;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Hydrogen cyanide synthase {ECO:0000313|EMBL:ACU30742.1};
GN   Name=hcnB {ECO:0000313|EMBL:ACU30742.1};
OS   Pseudomonas nunensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2961896 {ECO:0000313|EMBL:ACU30742.1};
RN   [1] {ECO:0000313|EMBL:ACU30742.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=In5 {ECO:0000313|EMBL:ACU30742.1};
RA   Jensen C., Stougaard P.;
RT   "A novel hydrogen cyanide gene cluster from a fungal-inhibiting Pseudomonas
RT   sp. isolate from Greenland.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACU30742.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=In5 {ECO:0000313|EMBL:ACU30742.1};
RX   PubMed=22417387; DOI=10.1139/w2012-004;
RA   Michelsen C.F., Stougaard P.;
RT   "Hydrogen cyanide synthesis and antifungal activity of the biocontrol
RT   strain Pseudomonas fluorescens In5 from Greenland is highly dependent on
RT   growth medium.";
RL   Can. J. Microbiol. 58:381-390(2012).
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DR   EMBL; GQ254718; ACU30742.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7E716; -.
DR   BRENDA; 1.4.99.5; 5121.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR017224; Opine_Oxase_asu/HCN_bsu.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..311
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          382..425
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   469 AA;  50910 MW;  DF7DCDE16CDD6CD2 CRC64;
     MSLHPVIVGG GPAGMAAAIE LARHGVRSTL LEEASRLGGV VYRGPLRDGV QLDYLGPRYS
     EILSRLHGEF QEQSGLIDVR LNHRVVGAEG TRALVVLDGD ERLHEFEYPQ LLLAAGCHER
     SVPFPGWTLP GVILLGGLQL QIKSGVVKPQ GPVVITGTGP LLPLVACQLH ASGVTVAGVY
     EACGFGKIAR ESLALLNKPQ LFLDGLSMLT FLKLHGIPMH YGWGVVAAQG EGELKSVTVA
     PYSRTWEPDL SRAETIAVQT LAVGYGFIPR TQLSQQMGLN HGFSDDGYLR ASANIWQQSN
     EPHVHLAGDM GGIRGGEAAM FAGRIAALSI LLQRDVLDKK LALVRRDRYL SKFKAIVRFR
     AAVDRYTERG AGQTALPAAD TVICRCEHAT RADIDRALEQ GVQDMASLKM RTRVSMGDCQ
     GRMCDGYCTD RLREATGRQD VGWLRPRFPI DPIPFSAFHN AATETANHE
//