HCNA_PSEAE
ID HCNA_PSEAE Reviewed; 104 AA.
AC G3XD67; Q7DCD3; Q9REV9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnA {ECO:0000312|EMBL:AAG05581.1};
DE Short=HcnA {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};
GN Name=hcnA {ECO:0000312|EMBL:AAG05581.1}; OrderedLocusNames=PA2193;
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:AAF21028.1}
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:AAF21028.1};
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:AAG05581.1}
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).
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:233722, 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 -!- 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:0000269|PubMed:234422}.
CC -!- INDUCTION: Reduced oxygen levels. {ECO:0000269|PubMed:11092854}.
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DR EMBL; AF208523; AAF21028.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05581.1; -; Genomic_DNA.
DR PIR; F83370; F83370.
DR RefSeq; NP_250883.1; NC_002516.2.
DR RefSeq; WP_003113684.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; G3XD67; -.
DR SMR; G3XD67; -.
DR STRING; 287.DR97_6237; -.
DR PaxDb; G3XD67; -.
DR PRIDE; G3XD67; -.
DR DNASU; 882197; -.
DR EnsemblBacteria; AAG05581; AAG05581; PA2193.
DR GeneID; 882197; -.
DR KEGG; pae:PA2193; -.
DR PATRIC; fig|208964.12.peg.2297; -.
DR PseudoCAP; PA2193; -.
DR HOGENOM; CLU_153062_2_0_6; -.
DR InParanoid; G3XD67; -.
DR OMA; PRAPFCG; -.
DR PhylomeDB; G3XD67; -.
DR BioCyc; PAER208964:G1FZ6-2233-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050622; F:glycine dehydrogenase (cyanide-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.440; -; 1.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..104
FT /note="Hydrogen cyanide synthase subunit HcnA"
FT /id="PRO_0000419809"
FT DOMAIN 16..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 104 AA; 11427 MW; BB640066E8514682 CRC64;
MHLLERQHDI QPLSRADMTI HLNGQPVAAA AGETVLNVLN AVGLRRLARN DHGQASGAFC
GMGVCHCCLV AIDGRPKRRA CQTVVRPGMR VETESNRFDQ EERP
