ID HCDH1_CAEEL Reviewed; 298 AA. AC P34439; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 10-JUN-2026, entry version 169. DE RecName: Full=Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1; DE EC=1.1.1.35; GN ORFNames=F54C8.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=7906398; DOI=10.1038/368032a0; RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A., RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., RA Wilkinson-Sproat J., Wohldman P.; RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. RT elegans."; RL Nature 368:32-38(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + CC H(+); Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z22178; CAA80153.1; -; Genomic_DNA. DR PIR; S40743; S40743. DR RefSeq; NP_499075.1; NM_066674.2. DR PDB; 4J0E; X-ray; 1.60 A; A/B=1-298. DR PDB; 4J0F; X-ray; 2.20 A; A/B=1-298. DR AlphaFoldDB; P34439; -. DR SMR; P34439; -. DR BioGRID; 50969; 2. DR FunCoup; P34439; 979. DR STRING; 6239.F54C8.1.1; -. DR PaxDb; 6239-F54C8.1.1; -. DR PeptideAtlas; P34439; -. DR EnsemblMetazoa; F54C8.1.1; F54C8.1.1; WBGene00010035. DR EnsemblMetazoa; F54C8.1.2; F54C8.1.2; WBGene00010035. DR GeneID; 186222; -. DR KEGG; cel:CELE_F54C8.1; -. DR UCSC; F54C8.1; c. elegans. DR AGR; WB:WBGene00010035; -. DR CTD; 186222; -. DR WormBase; F54C8.1; CE00187; WBGene00010035; -. DR eggNOG; KOG2304; Eukaryota. DR HOGENOM; CLU_009834_2_0_1; -. DR InParanoid; P34439; -. DR OMA; HFARHGH; -. DR OrthoDB; 5958943at2759; -. DR PhylomeDB; P34439; -. DR BRENDA; 1.1.1.35; 1045. DR UniPathway; UPA00659; -. DR EvolutionaryTrace; P34439; -. DR PRO; PR:P34439; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00010035; Expressed in adult organism and 3 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0003857; F:(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central. DR FunFam; 3.40.50.720:FF:000009; Fatty oxidation complex, alpha subunit; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR022694; 3-OHacyl-CoA_DH. 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; IPR013328; 6PGD_dom2. DR InterPro; IPR052242; Mito_3-hydroxyacyl-CoA_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43561; -; 1. DR PANTHER; PTHR43561:SF2; 3-HYDROXYACYL-COA DEHYDROGENASE F54C8.1-RELATED; 1. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR PIRSF; PIRSF000105; HCDH; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PDBsum; 4J0E; -. DR PDBsum; 4J0F; -. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid metabolism; Lipid metabolism; Mitochondrion; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1..298 FT /note="Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1" FT /id="PRO_0000109253" FT SITE 153 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250" FT HELIX 2..5 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 21..32 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 44..64 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 69..80 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 89..93 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 136..139 FT /evidence="ECO:0007829|PDB:4J0E" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:4J0F" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:4J0E" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 174..186 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:4J0E" FT TURN 198..201 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 202..219 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 224..235 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 241..248 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 250..263 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:4J0F" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 274..281 FT /evidence="ECO:0007829|PDB:4J0E" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:4J0E" FT STRAND 291..295 FT /evidence="ECO:0007829|PDB:4J0E" SQ SEQUENCE 298 AA; 32492 MW; D8C2BE57823445B4 CRC64; MFTAKCAMQN IRNVAIVGSG QMGSGIAQVT ASSGFNVMLA DVNKKALDRA MKAISQSVTH LSKKQKGTDK EKSDFVTLTM SRIKTCNNVS TAVADADLII EAAIENIDLK RGIFAQIEQS CKKDSILTTN TSSFLLEDVA KGLQDKTRFG GLHFFNPVPV MKLLEVIRSD DTSDETYATL IKFGTAVGKT TVACKDSPGF IVNRLLIPYF FEAARMYERG DASMTDIDEA MKLGAGHPMG PFELADYIGL DTVKFVMDGW AAKYPEVQLF EASPLVDKLV AEGKLGRKTG DGFYSYKK //