HCNC_PSEAE
ID HCNC_PSEAE Reviewed; 417 AA.
AC G3XD12; Q7DCD2; Q9REV7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnC {ECO:0000312|EMBL:AAG05583.1};
DE Short=HcnC {ECO:0000303|PubMed:10763748};
DE EC=1.4.99.5 {ECO:0000269|PubMed:10763748, ECO:0000269|PubMed:233722};
DE AltName: Full=Glycine dehydrogenase (cyanide-forming) {ECO:0000303|PubMed:10763748};
DE Flags: Precursor;
GN Name=hcnC {ECO:0000312|EMBL:AAG05583.1}; OrderedLocusNames=PA2195;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF21030.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|EMBL:AAF21030.1};
RX PubMed=11092854; DOI=10.1128/jb.182.24.6940-6949.2000;
RA Pessi G., Haas D.;
RT "Transcriptional control of the hydrogen cyanide biosynthetic genes hcnABC
RT by the anaerobic regulator ANR and the quorum-sensing regulators LasR and
RT RhlR in Pseudomonas aeruginosa.";
RL J. Bacteriol. 182:6940-6949(2000).
RN [2] {ECO:0000312|EMBL:AAG05583.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3] {ECO:0000305}
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1111/j.1399-3054.1968.tb07283.x;
RA Wissing F.;
RT "Growth curves and pH optima for cyanide producing bacteria.";
RL Physiol. Plantarum 21:589-593(1968).
RN [4] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=C {ECO:0000269|PubMed:4813896};
RX PubMed=4813896; DOI=10.1128/jb.117.3.1289-1294.1974;
RA Wissing F.;
RT "Cyanide formation from oxidation of glycine of Pseudomonas species.";
RL J. Bacteriol. 117:1289-1294(1974).
RN [5] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=234422; DOI=10.1128/jb.121.2.695-699.1975;
RA Wissing F.;
RT "Cyanide production from glycine by a homogenate from a Pseudomonas
RT species.";
RL J. Bacteriol. 121:695-699(1975).
RN [6] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=9-D2 {ECO:0000269|PubMed:233722};
RX PubMed=233722; DOI=10.1128/jb.130.2.826-831.1977;
RA Castric P.A.;
RT "Glycine metabolism by Pseudomonas aeruginosa: hydrogen cyanide
RT biosynthesis.";
RL J. Bacteriol. 130:826-831(1977).
RN [7] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10763748; DOI=10.1007/s002039900127;
RA Blumer C., Haas D.;
RT "Mechanism, regulation, and ecological role of bacterial cyanide
RT biosynthesis.";
RL Arch. Microbiol. 173:170-177(2000).
RN [8] {ECO:0000305}
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:11591663};
RX PubMed=11591663; DOI=10.1128/jb.183.21.6207-6214.2001;
RA Gallagher L.A., Manoil C.;
RT "Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide
RT poisoning.";
RL J. Bacteriol. 183:6207-6214(2001).
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. {ECO:0000269|PubMed:10763748, ECO:0000269|PubMed:11092854,
CC ECO:0000269|PubMed:11591663, ECO:0000269|PubMed:233722,
CC ECO:0000269|PubMed:4813896}.
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:0000269|PubMed:10763748, ECO:0000269|PubMed:233722};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000303|PubMed:234422, ECO:0000305};
CC -!- ACTIVITY REGULATION: Oxygen is necessary for cyanogenesis. Activated by
CC succinate, glycine methyl ester, glucose and D,L-methionine in addition
CC to glycine. Phenazine methosulfate, methylene blue, 2,6-
CC dichlorophenolindophenol (DCIP) and ferricyanide can replace oxygen for
CC the reaction. Inhibited by pyrrolnitrin and acriflavine at 1 mM
CC concentration. {ECO:0000269|PubMed:4813896, ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 mM for glycine {ECO:0000269|PubMed:234422,
CC ECO:0000269|PubMed:4813896, ECO:0000269|Ref.3};
CC Note=Measured for the whole complex. {ECO:0000269|PubMed:4813896};
CC pH dependence:
CC Optimum pH is 8.3 (in the presence of Tris-HCl). Active from 7.3-7.8
CC in the presence of other buffers. {ECO:0000269|PubMed:234422,
CC ECO:0000269|PubMed:4813896, ECO:0000269|Ref.3};
CC Temperature dependence:
CC Not stable at 0 degrees Celsius. Decrease in activity up to 40%
CC immediately after freeze-drying procedure, with a further decrease up
CC to 10% when stored at -10 degrees Celsius.
CC {ECO:0000269|PubMed:234422, ECO:0000269|PubMed:4813896,
CC ECO:0000269|Ref.3};
CC -!- SUBUNIT: Heterotrimer of HcnA, HcnB and HcnC. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:234422}. 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: Reduced oxygen levels. {ECO:0000269|PubMed:11092854}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000255}.
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DR EMBL; AF208523; AAF21030.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05583.1; -; Genomic_DNA.
DR PIR; H83370; H83370.
DR RefSeq; NP_250885.1; NC_002516.2.
DR RefSeq; WP_003113686.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; G3XD12; -.
DR SMR; G3XD12; -.
DR STRING; 287.DR97_6235; -.
DR PaxDb; G3XD12; -.
DR PRIDE; G3XD12; -.
DR EnsemblBacteria; AAG05583; AAG05583; PA2195.
DR GeneID; 882196; -.
DR KEGG; pae:PA2195; -.
DR PATRIC; fig|208964.12.peg.2299; -.
DR PseudoCAP; PA2195; -.
DR HOGENOM; CLU_007884_4_5_6; -.
DR InParanoid; G3XD12; -.
DR OMA; WVQSKGL; -.
DR PhylomeDB; G3XD12; -.
DR BioCyc; PAER208964:G1FZ6-2235-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
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 1: Evidence at protein level;
KW Cell membrane; Flavoprotein; Lipoprotein; Membrane; Oxidoreductase;
KW Palmitate; Reference proteome; Signal; 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:11092854"
FT /id="PRO_0000419807"
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; 45282 MW; 63F5DB8A3118F318 CRC64;
MNRTYDIVIA GGGVIGASCA YQLSRRGNLR IAVVDDKRPG NATRASAGGL WAIGESVGLG
CGVIFFRMMS SRNRREAQGA AVAVDASTPH ILPPAFFDLA LQSNALYPEL HRELIERHGM
DFKFERTGLK YVIQDDEDRQ YAEHIVAQIP HLAEQVRWLD REELRRAEPA VSHAAHGALE
FLCDHQVSPF RLADAYLEAA RQNGVELLPG TNVTGVLRQG RRISGVRTDN AGVLHCRTLI
NAAGAWAAEL SEMATGRRIP VKPVKGQIVL TERMPRLLNG CLTTSDCYMA QKDNGEILIG
STTEDKGFDV SNTFPEIAGL VQGAVRCVPE LQQVNLKRTW AGLRPGSPDE LPILGPVAEV
EGYLNACGHF RTGILTSAIT GVLLDRLVHE ETLPLDIAPF LAARFQPEPA AVAVAAC
