CRT_CLOAB
ID CRT_CLOAB Reviewed; 261 AA.
AC P52046;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Short-chain-enoyl-CoA hydratase {ECO:0000305};
DE EC=4.2.1.150 {ECO:0000269|PubMed:5057466, ECO:0000269|PubMed:8655474};
DE AltName: Full=3-hydroxybutyryl-CoA dehydratase {ECO:0000305};
DE AltName: Full=Crotonase {ECO:0000303|PubMed:5057466, ECO:0000303|PubMed:8655474};
GN Name=crt; OrderedLocusNames=CA_C2712;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 1-10, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8655474; DOI=10.1128/jb.178.11.3015-3024.1996;
RA Boynton Z.L., Bennett G.N., Rudolph F.B.;
RT "Cloning, sequencing, and expression of clustered genes encoding beta-
RT hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA
RT dehydrogenase from Clostridium acetobutylicum ATCC 824.";
RL J. Bacteriol. 178:3015-3024(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=5057466; DOI=10.1016/s0021-9258(19)44966-1;
RA Waterson R.M., Castellino F.J., Hass G.M., Hill R.L.;
RT "Purification and characterization of crotonase from Clostridium
RT acetobutylicum.";
RL J. Biol. Chem. 247:5266-5271(1972).
CC -!- FUNCTION: Catalyzes the reversible hydration of crotonyl-CoA. Can also
CC use hexenoyl-CoA but not higher analogs. {ECO:0000269|PubMed:5057466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain (2E)-
CC enoyl-CoA + H2O; Xref=Rhea:RHEA:52664, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:87488, ChEBI:CHEBI:136760; EC=4.2.1.150;
CC Evidence={ECO:0000269|PubMed:5057466, ECO:0000269|PubMed:8655474};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for crotonyl-CoA {ECO:0000269|PubMed:5057466};
CC KM=0.13 mM for hexenoyl-CoA {ECO:0000269|PubMed:5057466};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:5057466}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; U17110; AAA95967.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK80658.1; -; Genomic_DNA.
DR PIR; G97233; G97233.
DR PIR; T47261; T47261.
DR RefSeq; NP_349318.1; NC_003030.1.
DR RefSeq; WP_010965999.1; NC_003030.1.
DR PDB; 5Z7R; X-ray; 2.20 A; A/B/C=1-261.
DR PDBsum; 5Z7R; -.
DR AlphaFoldDB; P52046; -.
DR SMR; P52046; -.
DR STRING; 272562.CA_C2712; -.
DR PRIDE; P52046; -.
DR EnsemblBacteria; AAK80658; AAK80658; CA_C2712.
DR GeneID; 44999201; -.
DR KEGG; cac:CA_C2712; -.
DR PATRIC; fig|272562.8.peg.2902; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_6_9; -.
DR OMA; ELSMSCD; -.
DR OrthoDB; 1498685at2; -.
DR BioCyc; MetaCyc:CRTCLOS-MON; -.
DR BRENDA; 4.2.1.150; 1452.
DR SABIO-RK; P52046; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
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; Direct protein sequencing; Fatty acid metabolism;
KW Lipid metabolism; Lyase; Reference proteome.
FT CHAIN 1..261
FT /note="Short-chain-enoyl-CoA hydratase"
FT /id="PRO_0000109317"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5Z7R"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5Z7R"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:5Z7R"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:5Z7R"
SQ SEQUENCE 261 AA; 28190 MW; C9D70D4D2FBF26D4 CRC64;
MELNNVILEK EGKVAVVTIN RPKALNALNS DTLKEMDYVI GEIENDSEVL AVILTGAGEK
SFVAGADISE MKEMNTIEGR KFGILGNKVF RRLELLEKPV IAAVNGFALG GGCEIAMSCD
IRIASSNARF GQPEVGLGIT PGFGGTQRLS RLVGMGMAKQ LIFTAQNIKA DEALRIGLVN
KVVEPSELMN TAKEIANKIV SNAPVAVKLS KQAINRGMQC DIDTALAFES EAFGECFSTE
DQKDAMTAFI EKRKIEGFKN R
