FLUDE_STREN
ID FLUDE_STREN Reviewed; 507 AA.
AC F8JX40; G8WN34;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Fluoroacetaldehyde dehydrogenase;
DE EC=1.2.1.69;
GN OrderedLocusNames=SCAT_0945, SCATT_09460;
OS Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC
OS 14057 / NRRL 8057).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1003195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057;
RX PubMed=21868806; DOI=10.1128/jb.05583-11;
RA Barbe V., Bouzon M., Mangenot S., Badet B., Poulain J., Segurens B.,
RA Vallenet D., Marliere P., Weissenbach J.;
RT "Complete genome sequence of Streptomyces cattleya NRRL 8057, a producer of
RT antibiotics and fluorometabolites.";
RL J. Bacteriol. 193:5055-5056(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057;
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057;
RX PubMed=11571203; DOI=10.1128/aem.67.10.4919-4921;
RA Murphy C.D., Moss S.J., O'Hagan D.;
RT "Isolation of an aldehyde dehydrogenase involved in the oxidation of
RT fluoroacetaldehyde to fluoroacetate in Streptomyces cattleya.";
RL Appl. Environ. Microbiol. 67:4919-4921(2001).
RN [4]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Catalyzes the oxidation of fluoroacetaldehyde to
CC fluoroacetate. Has high affinity for fluoroacetate and glycolaldehyde
CC but not for acetaldehyde. {ECO:0000269|PubMed:11571203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fluoroacetaldehyde + H2O + NAD(+) = fluoroacetate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:16677, ChEBI:CHEBI:14272, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18172, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.69;
CC Evidence={ECO:0000269|PubMed:11571203};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for fluoroacetaldehyde {ECO:0000269|PubMed:11571203};
CC KM=150 uM for glycoaldehyde {ECO:0000269|PubMed:11571203};
CC KM=810 uM for acetaldehyde {ECO:0000269|PubMed:11571203};
CC KM=320 uM for benzaldehyde {ECO:0000269|PubMed:11571203};
CC Vmax=0.143 umol/min/mg enzyme with fluoroacetaldehyde as substrate
CC {ECO:0000269|PubMed:11571203};
CC Vmax=0.206 umol/min/mg enzyme with glycoaldehyde as substrate
CC {ECO:0000269|PubMed:11571203};
CC Vmax=0.129 umol/min/mg enzyme with acetaldehyde as substrate
CC {ECO:0000269|PubMed:11571203};
CC Vmax=0.099 umol/min/mg enzyme with benzaldehyde as substrate
CC {ECO:0000269|PubMed:11571203};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11571203}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP003219; AEW93317.1; -; Genomic_DNA.
DR EMBL; FQ859185; CCB73675.1; -; Genomic_DNA.
DR RefSeq; WP_014141713.1; NC_017586.1.
DR AlphaFoldDB; F8JX40; -.
DR SMR; F8JX40; -.
DR STRING; 1003195.SCAT_0945; -.
DR PRIDE; F8JX40; -.
DR EnsemblBacteria; AEW93317; AEW93317; SCATT_09460.
DR KEGG; sct:SCAT_0945; -.
DR KEGG; scy:SCATT_09460; -.
DR PATRIC; fig|1003195.11.peg.2533; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_11; -.
DR OMA; HGIGYYP; -.
DR OrthoDB; 744602at2; -.
DR SABIO-RK; F8JX40; -.
DR Proteomes; UP000007842; Chromosome.
DR GO; GO:0033723; F:fluoroacetaldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11571203"
FT CHAIN 2..507
FT /note="Fluoroacetaldehyde dehydrogenase"
FT /id="PRO_0000430453"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /evidence="ECO:0000250"
FT BINDING 219..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 7..9
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="R -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 54570 MW; 29EB34AAE87B682F CRC64;
MTVHQAPGTP GSVISLRPRY DNWIGGDWKA PAEGRYFANP TPVTGEEYTE IARSTAADID
LALDAAHAAA PAWGRTAPAE RAAVLGRIAD RIEQHLTELA VAEVWDNGKP IREALAADLP
LAVDHFRYFA GVLRAQEGSI SQLDEDTVAY HFHEPLGVVG QIIPWNFPLL MAVWKLAPAL
AAGNAVVLKP AEQTPVSILV LMELIADILP PGVINVVNGF GIEAGKPLAI NPRIAKVAFT
GETTTGRLIM QYASQNLIPV TLELGGKSPN LFFEDVAAAR DDFYDKALEG FTMFALNQGE
VCTCPSRALI AGGIYDGFLG DALERTRAVK QGNPLDTETM IGAQASNDQL EKILSYIDIG
TAEGAKVLTG GERVDLGGSL SGGYYVAPTI FEGDNRMRIF QEEIFGPVVS VTRFDGYDDA
ISIANDTLYG LGAGVWTRDL STAYRAGRAI QAGRVWTNCY HAYPAHAAFG GYKNSGIGRE
THKMMLDHYQ QTKNLLISYS AKGPGLF
