Reviewed, UniProtKB/Swiss-Prot P40952 (KYE1_KLULA)

Names and origin

Protein names

Recommended name:
    Enoate reductase 1
Alternative name(s):
    2-enoate reductase
      Short name=ER
    EC=1.3.1.31
    Old yellow enzyme 1

Gene names

Name:	KYE1
Ordered Locus Names:	KLLA0A09075g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Enoate reductase with broad substrate specificity for different alpha,beta-unsaturated carbonyl compounds. Prefers NADPH over NADH as cofactor.
Catalytic activity	Butanoate + NAD+ = 2-butenoate + NADH. Ref.3
Cofactor	FMN.
Subunit structure	Homodimer or heterodimer.
Sequence similarities	Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Ontologies

Keywords
Ligand	FMN Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2-enoate reductase activity Inferred from electronic annotation. Source: EC FMN binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 398	398	Enoate reductase 1		PRO_0000194476
Sites
	Active site	196	1	Proton donor By similarity
	Binding site	37	1	FMN By similarity
	Binding site	191	1	FMN By similarity
	Binding site	191	1	Substrate By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	243	1	FMN By similarity
	Binding site	348	1	FMN By similarity
	Binding site	375	1	Substrate By similarity
Experimental info
	Sequence conflict	256	1	G → V in AAA98815. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40952-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: AA40CCC0C2BE6EC1	FASTA	398	44,780
	10 20 30 40 50 60 MSFMNFEPKP LADTDIFKPI KIGNTELKHR VVMPALTRMR ALHPGNVPNP DWAVEYYRQR 70 80 90 100 110 120 SQYPGTMIIT EGAFPSAQSG GYDNAPGVWS EEQLAQWRKI FKAIHDNKSF VWVQLWVLGR 130 140 150 160 170 180 QAFADNLARD GLRYDSASDE VYMGEDEKER AIRSNNPQHG ITKDEIKQYI RDYVDAAKKC 190 200 210 220 230 240 IDAGADGVEI HSANGYLLNQ FLDPISNKRT DEYGGSIENR ARFVLEVVDA VVDAVGAERT 250 260 270 280 290 300 SIRFSPYGVF GTMSGGSDPV LVAQFAYVLA ELEKRAKAGK RLAYVDLVEP RVTSPFQPEF 310 320 330 340 350 360 EGWYKGGTNE FVYSVWKGNV LRVGNYALDP DAAITDSKNP NTLIGYGRAF IANPDLVERL 370 380 390 EKGLPLNQYD RPSFYKMSAE GYIDYPTYEE AVAKGYKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and chromosomal localization of the gene encoding the Old Yellow Enzyme from Kluyveromyces lactis." Miranda M., Ramirez J., Guevara S., Ongay-Larios L., Pena A., Coria R. Yeast 11:459-465(1995) [PubMed: 7597850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.
[3]	"Comparison of three enoate reductases and their potential use for biotransformations." Chaparro-Riggers J.F., Rogers T.A., Vazquez-Figueroa E., Polizzi K.M., Bommarius A.S. Adv. Synth. Catal. 349:1521-1531(2007) Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37452 Genomic DNA. Translation: AAA98815.1. CR382121 Genomic DNA. Translation: CAH02985.1.
PIR	S55844.
RefSeq	XP_451397.1.
3D structure databases
HSSP	HSSP built from PDB template 1OYC based on UniProtKB Q02899.
SMR	P40952. Positions 5-398.
ModBase	Search...
Genome annotation databases
GeneID	2896828.
KEGG	kla:KLLA0A09075g.
Phylogenomic databases
HOGENOM	P40952.
Enzyme and pathway databases
BRENDA	1.6.99.1. 74088.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001155. OxRdtase_FMN_N. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00724. Oxidored_FMN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KYE1_KLULA

Accession

Primary (citable) accession number: P40952
Secondary accession number(s): Q6CXE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 27, 2004
Last modified:	June 16, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)