{PDOC00065}
{PS00067; 3HCDH}
{BEGIN}
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* 3-hydroxyacyl-CoA dehydrogenase signature *
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3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) (HCDH) [1] is an enzyme involved
in fatty acid metabolism,  it catalyzes the reduction  of 3-hydroxyacyl-CoA to
3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems,
one located in  mitochondria and  the  other in peroxisomes.   In  peroxisomes
3-hydroxyacyl-CoA  dehydrogenase  forms,  with  enoyl-CoA  hydratase (ECH) and
3,2-trans-enoyl-CoA isomerase (ECI)  a  multifunctional  enzyme  where  the N-
terminal domain bears the hydratase/isomerase  activities  and  the C-terminal
domain the  dehydrogenase  activity.  There are two mitochondrial enzymes: one
which is   monofunctional   and  the  other  which is,  like  its  peroxisomal
counterpart, multifunctional.

In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA) HCDH is part
of a multifunctional enzyme which also contains an ECH/ECI domain as well as a
3-hydroxybutyryl-CoA epimerase domain [2].

The other proteins structurally related to HCDH are:

 - Bacterial  3-hydroxybutyryl-CoA  dehydrogenase (EC 1.1.1.157) which reduces
   3-hydroxybutanoyl-CoA to acetoacetyl-CoA [3].
 - Eye  lens  protein  lambda-crystallin [4], which is specific to lagomorphes
   (such as rabbit).

There are two major region of similarities in the sequences of proteins of the
HCDH family, the  first one located in the N-terminal, corresponds to the NAD-
binding site, the second one is located in the center of the sequence. We have
chosen to derive a signature pattern from this central region.

-Consensus pattern: [DNES]-x(2)-[GA]-F-[LIVMFYA]-x-[NT]-R-x(3)-[PA]-[LIVMFY]-
                    [LIVMFYST]-x(5,6)-[LIVMFYCT]-[LIVMFYEAH]-x(2)-[GVE]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2004 / Pattern and text revised.

[ 1] Birktoff J.J., Holden H.M., Hamlin R., Xuong N.-H., Banaszak L.J.
     Proc. Natl. Acad. Sci. U.S.A. 84:8262-8266(1987).
[ 2] Nakahigashi K., Inokuchi H.
     "Nucleotide sequence of the fadA and fadB genes from Escherichia
     coli."
     Nucleic Acids Res. 18:4937-4937(1990).
     PubMed=2204034
[ 3] Mullany P., Clayton C.L., Pallen M.J., Slone R., al-Saleh A.,
     Tabaqchali S.
     "Genes encoding homologues of three consecutive enzymes in the
     butyrate/butanol-producing pathway of Clostridium acetobutylicum are
     clustered on the Clostridium difficile chromosome."
     FEMS Microbiol. Lett. 124:61-67(1994).
     PubMed=8001771
[ 4] Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H.,
     de Jong W.W.
     "Lambda-crystallin, a major rabbit lens protein, is related to
     hydroxyacyl-coenzyme A dehydrogenases."
     J. Biol. Chem. 263:15462-15466(1988).
     PubMed=3170592

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