HCNA_PSEPH
ID HCNA_PSEPH Reviewed; 105 AA.
AC O85226;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Hydrogen cyanide synthase subunit HcnA {ECO:0000312|EMBL:AAC38594.1};
DE Short=HcnA {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=hcnA {ECO:0000312|EMBL:AAC38594.1};
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:AAC38594.1}
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]
RP INDUCTION.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=10570200; DOI=10.1073/pnas.96.24.14073;
RA Blumer C., Heeb S., Pessi G., Haas D.;
RT "Global GacA-steered control of cyanide and exoprotease production in
RT Pseudomonas fluorescens involves specific ribosome binding sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14073-14078(1999).
RN [4]
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 (PubMed:16453871). {ECO:0000269|PubMed:16453871,
CC 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 (PubMed:10570200, PubMed:11021918). Post-
CC transcriptionally up-regulated by GacA (PubMed:10570200). Stimulated by
CC glycine. {ECO:0000269|PubMed:10570200, ECO:0000269|PubMed:11021918,
CC ECO:0000269|PubMed:16453871}.
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DR EMBL; AF053760; AAC38594.1; -; Genomic_DNA.
DR RefSeq; WP_011060873.1; NZ_LS999205.1.
DR AlphaFoldDB; O85226; -.
DR SMR; O85226; -.
DR STRING; 1124983.PFLCHA0_c26420; -.
DR GeneID; 57475633; -.
DR PATRIC; fig|1124983.3.peg.2664; -.
DR eggNOG; COG3383; Bacteria.
DR BioCyc; MetaCyc:MON-8123; -.
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 2: Evidence at transcript level;
KW 2Fe-2S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..105
FT /note="Hydrogen cyanide synthase subunit HcnA"
FT /id="PRO_0000419810"
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 105 AA; 11525 MW; F2DFF3A0C3773FA3 CRC64;
MRQIDRNFDI QPLQHADMTI SLNGQPVTAA LGETVLSVIQ ATGLRQVARN DHGQLVGAYC
GMGVCHCCLV QIDGRHKRRA CQTLVKPGMQ VQTLSNRITE TEPTL
