HPCD_METS5
ID HPCD_METS5 Reviewed; 259 AA.
AC A4YI89;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=3-hydroxypropionyl-coenzyme A dehydratase {ECO:0000303|PubMed:19429610};
DE Short=3-hydroxypropionyl-CoA dehydratase {ECO:0000303|PubMed:19429610};
DE EC=4.2.1.116;
GN OrderedLocusNames=Msed_2001;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABP96141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=19429610; DOI=10.1128/jb.00068-09;
RA Teufel R., Kung J.W., Kockelkorn D., Alber B.E., Fuchs G.;
RT "3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A
RT reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate
RT cycle in the Sulfolobales.";
RL J. Bacteriol. 191:4572-4581(2009).
CC -!- FUNCTION: Plays a role in autotrophic carbon fixation via the 3-
CC hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible
CC dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the
CC reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-
CC CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.
CC {ECO:0000269|PubMed:19429610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O;
CC Xref=Rhea:RHEA:26518, ChEBI:CHEBI:15377, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:58528; EC=4.2.1.116;
CC Evidence={ECO:0000269|PubMed:19429610};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for 3-hydroxypropionyl-CoA {ECO:0000269|PubMed:19429610};
CC KM=75 uM for (S)-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:19429610};
CC pH dependence:
CC Optimum pH is 8.1 at room temperature. Retains half maximum activity
CC at pH 6.5 and pH 9.5 at room temperature.
CC {ECO:0000269|PubMed:19429610};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19429610}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255}.
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DR EMBL; CP000682; ABP96141.1; -; Genomic_DNA.
DR RefSeq; WP_012021928.1; NC_009440.1.
DR PDB; 5ZAI; X-ray; 1.80 A; A/B/C/D/E/F=1-259.
DR PDBsum; 5ZAI; -.
DR AlphaFoldDB; A4YI89; -.
DR SMR; A4YI89; -.
DR STRING; 399549.Msed_2001; -.
DR EnsemblBacteria; ABP96141; ABP96141; Msed_2001.
DR GeneID; 5103388; -.
DR GeneID; 59456864; -.
DR KEGG; mse:Msed_2001; -.
DR eggNOG; arCOG00249; Archaea.
DR HOGENOM; CLU_009834_7_6_2; -.
DR OMA; MDMCLSA; -.
DR BioCyc; MetaCyc:MON-13729; -.
DR BRENDA; 4.2.1.116; 7245.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0043956; F:3-hydroxypropionyl-CoA dehydratase activity; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT CHAIN 1..259
FT /note="3-hydroxypropionyl-coenzyme A dehydratase"
FT /id="PRO_0000404649"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:5ZAI"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:5ZAI"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:5ZAI"
SQ SEQUENCE 259 AA; 28316 MW; 5B58E3747F1410BE CRC64;
MEFETIETKK EGNLFWITLN RPDKLNALNA KLLEELDRAV SQAESDPEIR VIIITGKGKA
FCAGADITQF NQLTPAEAWK FSKKGREIMD KIEALSKPTI AMINGYALGG GLELALACDI
RIAAEEAQLG LPEINLGIYP GYGGTQRLTR VIGKGRALEM MMTGDRIPGK DAEKYGLVNR
VVPLANLEQE TRKLAEKIAK KSPISLALIK EVVNRGLDSP LLSGLALESV GWGVVFSTED
KKEGVSAFLE KREPTFKGK
