HCNC_PSEPH
ID HCNC_PSEPH Reviewed; 417 AA.
AC O85228;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnC {ECO:0000312|EMBL:AAC38596.1};
DE Short=HcnC {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};
DE Flags: Precursor;
GN Name=hcnC {ECO:0000312|EMBL:AAC38596.1};
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:AAC38596.1}
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 ECO:0000255|PROSITE-ProRule:PRU00303}. Cell membrane
CC {ECO:0000255|PROSITE-ProRule:PRU00303}; Single-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303};
CC Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000255}.
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DR EMBL; AF053760; AAC38596.1; -; Genomic_DNA.
DR RefSeq; WP_015635308.1; NZ_LS999205.1.
DR AlphaFoldDB; O85228; -.
DR SMR; O85228; -.
DR STRING; 1124983.PFLCHA0_c26440; -.
DR GeneID; 57475635; -.
DR PATRIC; fig|1124983.3.peg.2666; -.
DR eggNOG; COG0665; Bacteria.
DR BioCyc; MetaCyc:MON-8125; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Lipoprotein; Membrane; Oxidoreductase; Palmitate; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..417
FT /note="Hydrogen cyanide synthase subunit HcnC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:9620970"
FT /id="PRO_0000419808"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 7..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 417 AA; 45334 MW; 313C546F36142415 CRC64;
MIKHYDVVIA GGGVIGASCA YQLSKRKDLK VALIDAKRPG NASRASAGGL WAIGESVGLG
CGVIFFRMMS ANRKREAQGS AVVVDSSTPH ILPQSFFDFA LQSNELYPRL HRELMGLHNM
DFKFEQTGLK FVIYDEEDRL YAEHIVGCIP HLSDQVRWLD QAALRASEPN VSHEAQGALE
FLCDHQVNPF RLTDAYTEGA RQNGVDVYFN TNVTGVLHQG NRVSGVKTDV AGLFRCTTLI
NAAGAWAAEL SLQATGIEIP VKPVKGQILL TERMPKLLNG CLTTSDCYMA QKDNGEILIG
STTEDKGFDV TTTYPEINGL VQGAVRCVPE LAHVNLKRCW AGLRPGSPDE LPILGPMDGV
EGYLNACGHF RTGILTSAIT GVLLDKLVNE EALPLDITPF LARRFATAPV KKQPEPA
