Q39659 (MFPA_CUCSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a Including the following 2 domains: Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase EC=4.2.1.17 EC=5.1.2.3 EC=5.3.3.8 3-hydroxyacyl-CoA dehydrogenase EC=1.1.1.35
Organism	Cucumis sativus (Cucumber)
Taxonomic identifier	3659 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Benincaseae › Cucumis

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. Ref.1 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Ref.1 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Ref.1 (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. Ref.1
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subcellular location	Glyoxysome Ref.1.
Domain	The epimerase and isomerase activities are contained in the N-terminal region while the dehydrogenase activity is in the C-terminal region. Ref.1
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Glyoxysome Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	glyoxysome Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	3-hydroxyacyl-CoA dehydratase activity Inferred from direct assay Ref.1. Source: UniProtKB 3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 3-hydroxybutyryl-CoA epimerase activity Inferred from direct assay Ref.1. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from direct assay Ref.1. Source: UniProtKB enoyl-CoA hydratase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 725	725	Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a		PRO_0000109251

Sequences

	Sequence		Length	Mass (Da)
	Q39659 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D7C7943A51AFE7DB	FASTA	725	79,170
	10 20 30 40 50 60 MGSNAKGRTV MEVGTDGVAI ITIINPPVNS LSFDVLFSLR DSYEQALRRD DVKAIVVTGA 70 80 90 100 110 120 KGKFSGGFDI TAFGVLQGGK GEQPNVRNIS IEMITDIFEA ARKPAVAAID GLALGGGLEV 130 140 150 160 170 180 AMACHARIST PTAQLGLPEL QLGIIPGFGG TQRLPRLVGL SKALEMMLTS KPIKGQEAHS 190 200 210 220 230 240 LGLVDAIVPP EELINTARRW ALEILERRRP WVHSLHRTDK LESLAEARKI FNLARAQAKK 250 260 270 280 290 300 QYPNLKHTIA CIDAVETGVV SGPRAGLWKE AEEFQGLLHS DTCKSLIHIF FAQRSTTKVP 310 320 330 340 350 360 GVTDLGLVPR QIKKVAIVGG GLMGSGIATA LILSNYHVVL KEVNDKFLQA GIDRVRANLQ 370 380 390 400 410 420 SRVKKGNMTN EKFEKSISLL KGVLNYESFK DVDMVIEAVI ENVSLKQQIF SDLEKYCPPH 430 440 450 460 470 480 CMLATNTSTI DLELIGERIK SRDRIIGAHF FSPAHIMPLL EIVRTKHTAA QVIVDLLDVG 490 500 510 520 530 540 KNIKKTPVVV GNCTGFAVNR MFFPYSQAAI LLAEHGVDPY QIDRAISKFG MPMGPFRLCD 550 560 570 580 590 600 LVGFGVAAAT ASQFVQAFPE RTYKSMLIPL MQEDKNAGES TRKGFYVYDK NRKAGPNPEL 610 620 630 640 650 660 KKYIEKARNS SGVSVDPKLT KLPEKDIVEM IFFPVVNEAC RVLAEGIAVK AADLDIAGVM 670 680 690 700 710 720 GMGFPSYRGG LMFWADSLGS NYIYSRLEEW SKQYGGFFKP CGYLAERAVQ GATLSAPGGH AKPRM

References

[1]

"Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity." Preisig-Mueller R., Guehnemann-Schaefer K., Kindl H. J. Biol. Chem. 269:20475-20481(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Tissue: Seedling cotyledon.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X78996 mRNA. Translation: CAA55630.1.
PIR	T10464.
RefSeq	XP_004168411.1. XM_004168363.1.
3D structure databases
ProteinModelPortal	Q39659.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	101210295.
Enzyme and pathway databases
UniPathway	UPA00659.
Family and domain databases
Gene3D	1.10.1040.10. 2 hits. 3.40.50.720. 1 hit.
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core_superfam. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 2 hits.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MFPA_CUCSA

Accession

Primary (citable) accession number: Q39659

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program