HACD_SCHPO
ID HACD_SCHPO Reviewed; 208 AA.
AC O14346; Q9UUC5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Probable very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:P40857};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase;
DE Short=HACD;
GN ORFNames=SPBC19C2.15c, SPBC2F12.16;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the third of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into
CC trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators.
CC {ECO:0000250|UniProtKB:P40857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain
CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134;
CC Evidence={ECO:0000250|UniProtKB:P40857};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P40857}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P40857}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40857}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52042.1; -; Genomic_DNA.
DR PIR; T39806; T39806.
DR RefSeq; NP_595700.1; NM_001021597.2.
DR AlphaFoldDB; O14346; -.
DR BioGRID; 277210; 3.
DR STRING; 4896.SPBC19C2.15c.1; -.
DR PaxDb; O14346; -.
DR EnsemblFungi; SPBC19C2.15c.1; SPBC19C2.15c.1:pep; SPBC19C2.15c.
DR GeneID; 2540685; -.
DR KEGG; spo:SPBC19C2.15c; -.
DR PomBase; SPBC19C2.15c; -.
DR VEuPathDB; FungiDB:SPBC19C2.15c; -.
DR eggNOG; KOG3187; Eukaryota.
DR HOGENOM; CLU_034302_6_1_1; -.
DR InParanoid; O14346; -.
DR OMA; TKLYLFA; -.
DR PhylomeDB; O14346; -.
DR Reactome; R-SPO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:O14346; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0102343; F:3-hydroxy-arachidoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102344; F:3-hydroxy-behenoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102345; F:3-hydroxy-lignoceroyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; ISO:PomBase.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; ISO:PomBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..208
FT /note="Probable very-long-chain (3R)-3-hydroxyacyl-CoA
FT dehydratase"
FT /id="PRO_0000116858"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..46
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..102
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..171
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 145
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 152
FT /evidence="ECO:0000250|UniProtKB:P40857"
SQ SEQUENCE 208 AA; 24037 MW; 6ED946280DAFDE1F CRC64;
MSKILKIQYL KLYNVISCFL WMSVLLRTGL IWGITKDTAV VFHETNTLVR WVQTLAIAEV
FHSIFGLVSS SPLTTIIQVA SRLYLVWGVC YPFSYVIEGS PIYLSMIIAW SITEIIRYAF
YAFNLNGDIP AFLTWLRYNT FLILYPIGAG SEFLLVLKSR IAAQYVWSLN KLLWPILMSI
YPPGLYIMYT HMLAQRRKIS KRAAARRT
