HCNB_PSEPH
ID HCNB_PSEPH Reviewed; 469 AA.
AC O85227;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnB {ECO:0000312|EMBL:AAC38595.1};
DE Short=HcnB {ECO:0000303|PubMed:9620970};
DE EC=1.4.99.5 {ECO:0000250|UniProtKB:G3XD67};
DE AltName: Full=Glycine dehydrogenase (cyanide-forming) {ECO:0000303|PubMed:9620970};
GN Name=hcnB {ECO:0000312|EMBL:AAC38595.1};
OS Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1124983;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC38595.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=9620970; DOI=10.1128/jb.180.12.3187-3196.1998;
RA Laville J., Blumer C., Von Schroetter C., Gaia V., Defago G., Keel C.,
RA Haas D.;
RT "Characterization of the hcnABC gene cluster encoding hydrogen cyanide
RT synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol
RT agent Pseudomonas fluorescens CHA0.";
RL J. Bacteriol. 180:3187-3196(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=16453871; DOI=10.1002/j.1460-2075.1989.tb03384.x;
RA Voisard C., Keel C., Haas D., Defago G.;
RT "Cyanide production by Pseudomonas fluorescens helps suppress black root
RT rot of tobacco under gnotobiotic conditions.";
RL EMBO J. 8:351-358(1989).
RN [3] {ECO:0000305}
RP INDUCTION.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=11021918; DOI=10.1099/00221287-146-10-2417;
RA Blumer C., Haas D.;
RT "Iron regulation of the hcnABC genes encoding hydrogen cyanide synthase
RT depends on the anaerobic regulator ANR rather than on the global activator
RT GacA in Pseudomonas fluorescens CHA0.";
RL Microbiology 146:2417-2424(2000).
CC -!- FUNCTION: A three-component membrane-bound flavoenzyme that catalyzes
CC the formation of hydrogen cyanide, a secondary metabolite, by transfer
CC of electrons to a cyanide-resistant branch of the aerobic respiratory
CC chain. Contributes to suppression of black root rot of tobacco.
CC {ECO:0000269|PubMed:16453871, ECO:0000269|PubMed:9620970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + glycine = 2 AH2 + CO2 + hydrogen cyanide;
CC Xref=Rhea:RHEA:15821, ChEBI:CHEBI:13193, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:18407, ChEBI:CHEBI:57305; EC=1.4.99.5;
CC Evidence={ECO:0000250|UniProtKB:G3XD67};
CC -!- SUBUNIT: Heterotrimer of HcnA, HcnB and HcnC.
CC {ECO:0000250|UniProtKB:G3XD67}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:G3XD67}.
CC -!- INDUCTION: Transcriptionally up-regulated by Anr in response to Fe(3+)
CC in oxygen-limiting conditions. Stimulated by glycine.
CC {ECO:0000269|PubMed:11021918, ECO:0000269|PubMed:16453871}.
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DR EMBL; AF053760; AAC38595.1; -; Genomic_DNA.
DR RefSeq; WP_011060874.1; NZ_LS999205.1.
DR AlphaFoldDB; O85227; -.
DR SMR; O85227; -.
DR STRING; 1124983.PFLCHA0_c26430; -.
DR PRIDE; O85227; -.
DR GeneID; 57475634; -.
DR PATRIC; fig|1124983.3.peg.2665; -.
DR eggNOG; COG0446; Bacteria.
DR BioCyc; MetaCyc:MON-8124; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050622; F:glycine dehydrogenase (cyanide-forming) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Oxidoreductase.
FT CHAIN 1..469
FT /note="Hydrogen cyanide synthase subunit HcnB"
FT /id="PRO_0000419812"
SQ SEQUENCE 469 AA; 50647 MW; CE4538CA0AE19F50 CRC64;
MSLNPVIVGG GPAGMAAAIE LAEHGVRSTL IEEASRLGGV VYRGPLRDGV QLDYLGPRYC
EMLAKLHGDF ADHEQMIDVR LNSRVVGAEG TQSLVLLDGE EQVQQVSYEQ LILAAGCHER
SVPFPGWTLP GVKLLGGLQL QIKSGVVKPQ SPVVIAGTGP LLPLVACQLH ASGVRVAGVY
EACALGKIAK QSLAMLNKPQ LFLDGLSMLA YLKLHGIALR YGWGVVEAQG QDALSVVTVA
PYSSDWQPDM AKAQRIAAQT LAVGYGFIPR TQLSQQMGLE HNFSDDGYLR ASANAWQQSS
EPHVHLAGDM GGIRGGEAAM LSGRIAALSI LMQRGVLSNE AALQRRQGYE RKLASILRFR
GAVDRYTARG AGQVELPKGD TVICRCEHTT RNDIERALSQ GVQDMASLKM RTRVSMGDCQ
GRMCVGYCSD RLRQATGRKD VGWIRPRFPL DPIPFSAFPP SDQEVSQHD
