HCDH1_CAEEL
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 03-AUG-2022, entry version 153.
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 + H(+) +
CC NADH; 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}.
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DR EMBL; Z22178; CAA80153.1; -; Genomic_DNA.
DR PIR; S40743; S40743.
DR RefSeq; NP_499075.1; NM_066674.1.
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 PDBsum; 4J0E; -.
DR PDBsum; 4J0F; -.
DR AlphaFoldDB; P34439; -.
DR SMR; P34439; -.
DR BioGRID; 50969; 2.
DR STRING; 6239.F54C8.1; -.
DR EPD; P34439; -.
DR PaxDb; P34439; -.
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 CTD; 186222; -.
DR WormBase; F54C8.1; CE00187; WBGene00010035; -.
DR eggNOG; KOG2304; Eukaryota.
DR GeneTree; ENSGT00940000166803; -.
DR HOGENOM; CLU_009834_2_0_1; -.
DR InParanoid; P34439; -.
DR OMA; CKLGFGH; -.
DR OrthoDB; 938257at2759; -.
DR PhylomeDB; P34439; -.
DR BRENDA; 1.1.1.35; 1045.
DR UniPathway; UPA00659; -.
DR PRO; PR:P34439; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010035; Expressed in adult organism and 3 other 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:3-hydroxyacyl-CoA dehydrogenase 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 Gene3D; 1.10.1040.10; -; 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; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00067; 3HCDH; 1.
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
