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Database: UniProt
Entry: A0A452Y149_AEGTS
LinkDB: A0A452Y149_AEGTS
Original site: A0A452Y149_AEGTS 
ID   A0A452Y149_AEGTS        Unreviewed;       454 AA.
AC   A0A452Y149;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET1Gv20252000.28, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET1Gv20252000.28}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023717};
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR   AlphaFoldDB; A0A452Y149; -.
DR   EnsemblPlants; AET1Gv20252000.28; AET1Gv20252000.28; AET1Gv20252000.
DR   Gramene; AET1Gv20252000.28; AET1Gv20252000.28; AET1Gv20252000.
DR   Proteomes; UP000015105; Chromosome 1D.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23309:SF47; 3-HYDROXYACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT   DOMAIN          150..328
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          331..424
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   REGION          423..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50401 MW;  DE6AB4E443BED395 CRC64;
     MMMLSKPIKA EEAHELGLVD AVVSPNDLLN DARRWALDIC ESKRPWVRAL YKTDKLESPE
     VAREILNSAR VQSRKQAANL QHPLVCIDAV EEGIVSGPRA GLRKEAMAFQ ELFFSGTCKS
     LIHVFFSQRA TSKQVPGVTD LGLMPRKVSK VAIVGGGPMG SGIATTLILS HYPVILKEIN
     EKFLNAGIGR IKENLQSRVR KGKMTKDNYD KTLSLLTGVL DYEKFKSVDL AIETVVENVK
     LKQQIFAELE QHCPSHCILA TNTSTIDLDL IGEKTNSQDR IVGTHFFAPA HIMPLLEIVR
     TPRASLQAVV TMLDVGKKIK KTPIVVGNCT GFAVNRMFFP YTQAALLLVD HGMDVDKIDQ
     ACIEFGMPIG PFRMTDLVGF DVALATGMQY LENFPERVYK SMLIPLMTED KRTGEASQKG
     FYKYEGKRKA SPDPEITSYV EESRRISGAT PDPE
//
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