HCNB_PSEAE
ID HCNB_PSEAE Reviewed; 464 AA.
AC Q9I1S2; Q9REV8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnB {ECO:0000312|EMBL:AAG05582.1};
DE Short=HcnB {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=hcnB {ECO:0000312|EMBL:AAG05582.1}; OrderedLocusNames=PA2194;
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:AAF21029.2}
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:AAF21029.2};
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:AAG05582.1}
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; AAF21029.2; -; Genomic_DNA.
DR EMBL; AE004091; AAG05582.1; -; Genomic_DNA.
DR PIR; G83370; G83370.
DR RefSeq; NP_250884.1; NC_002516.2.
DR RefSeq; WP_003113685.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1S2; -.
DR SMR; Q9I1S2; -.
DR STRING; 287.DR97_6236; -.
DR PaxDb; Q9I1S2; -.
DR PRIDE; Q9I1S2; -.
DR DNASU; 882182; -.
DR EnsemblBacteria; AAG05582; AAG05582; PA2194.
DR GeneID; 882182; -.
DR KEGG; pae:PA2194; -.
DR PATRIC; fig|208964.12.peg.2298; -.
DR PseudoCAP; PA2194; -.
DR HOGENOM; CLU_030705_1_0_6; -.
DR InParanoid; Q9I1S2; -.
DR OMA; DENRRDG; -.
DR PhylomeDB; Q9I1S2; -.
DR BioCyc; PAER208964:G1FZ6-2234-MON; -.
DR Proteomes; UP000002438; Chromosome.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Oxidoreductase; Reference proteome.
FT CHAIN 1..464
FT /note="Hydrogen cyanide synthase subunit HcnB"
FT /id="PRO_0000419811"
FT CONFLICT 371
FT /note="R -> A (in Ref. 1; AAF21029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50389 MW; 3E77853869B61ADD CRC64;
MNLRPVIVGG GSAGMAAAIE LARRGVPCVL FDEASRPGGV VYRGPLRAGV DPAYLGARYT
RMLEKLRRDF SACAGHIDLR LNSRVVGGDG QRLMVLDEAE RLHEVEYSHL LLATGCHERS
VPFPGWTLPG VMLLGGLQLQ IKSGVVKPLG DTLIAGSGPL LPLVACQLHA AGVRVAGVYE
ACAFGRMARE SLALLNKPQL FLDGLSMLGY LKLNGIPLHY GWGVVEASGD GELTEVTVAP
YDEEWRPDLE NARPVKASTL AVGYGFIPRT QLSQQLGLEH GFSDDGYLRA ECNVWQQSSQ
PHIHLAGDMA GIRGGEAAMI GGRIAALSIL LQREAIAPAE AIERRESHLA RLEAIKRFRA
GVERYTQRGA RQVELARADT VICRCEQVTR GDIERALEQG VQDIAGLKMR TRAGMGDCQG
RMCIGYCSDR LRRATGRHDV GWLRPRFPID PIPFSAFQNL GTEA
