P08417 (FUMH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase, mitochondrial
Short name=Fumarase
EC=4.2.1.2

Gene names

Name:	FUM1
Ordered Locus Names:	YPL262W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subunit structure	Homotetramer. Ref.7
Subcellular location	Mitochondrion matrix. Cytoplasm. Note: Both fumarases are encoded by a single nuclear gene. Ref.4
Miscellaneous	Present with 6920 molecules/cell in log phase SD medium. Ref.5 There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fumarate metabolic process Traceable author statement. Source: SGD tricarboxylic acid cycle Traceable author statement. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD mitochondrial matrix Inferred from direct assay. Source: SGD tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	fumarate hydratase activity Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 488

Fumarate hydratase, mitochondrial

PRO_0000010333

Regions

Region

164 – 166

3

Substrate binding By similarity

Sites

Binding site

126

1

Substrate By similarity

Amino acid modifications

Modified residue

428

1

Phosphothreonine Ref.6

Experimental info

Sequence conflict

173

1

M → V in AAA66909. Ref.1

Sequence conflict

289

1

K → R in AAA66909. Ref.1

Sequence conflict

392

1

A → V in AAA66909. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

488

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Beta strand

33 – 35

3

Beta strand

38 – 43

6

Helix

48 – 54

7

Helix

61 – 64

4

Helix

68 – 87

20

Helix

93 – 107

15

Helix

112 – 114

3

Beta strand

118 – 121

4

Helix

126 – 142

17

Helix

155 – 159

5

Turn

160 – 162

3

Helix

165 – 182

18

Helix

185 – 202

18

Turn

203 – 205

3

Beta strand

207 – 212

6

Beta strand

215 – 221

7

Helix

222 – 247

26

Turn

255 – 257

3

Helix

267 – 279

13

Helix

289 – 294

6

Helix

297 – 323

27

Beta strand

327 – 330

4

Helix

353 – 377

25

Helix

387 – 411

25

Helix

413 – 415

3

Helix

420 – 429

10

Helix

432 – 434

3

Turn

435 – 437

3

Helix

438 – 440

3

Helix

443 – 456

14

Helix

460 – 466

7

Helix

472 – 478

7

Helix

481 – 483

3

Sequences

	Sequence		Length	Mass (Da)
	P08417 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: C099A02409A210E6	FASTA	488	53,152
	10 20 30 40 50 60 MLRFTNCSCK TFVKSSYKLN IRRMNSSFRT ETDAFGEIHV PADKYWGAQT QRSFQNFKIG 70 80 90 100 110 120 GARERMPLPL VHAFGVLKKS AAIVNESLGG LDPKISKAIQ QAADEVASGK LDDHFPLVVF 130 140 150 160 170 180 QTGSGTQSNM NANEVISNRA IEILGGKIGS KQVHPNNHCN QSQSSNDTFP TVMHIAASLQ 190 200 210 220 230 240 IQNELIPELT NLKNALEAKS KEFDHIVKIG RTHLQDATPL TLGQEFSGYV QQVENGIQRV 250 260 270 280 290 300 AHSLKTLSFL AQGGTAVGTG LNTKPGFDVK IAEQISKETG LKFQTAPNKF EALAAHDAIV 310 320 330 340 350 360 ECSGALNTLA CSLFKIAQDI RYLGSGPRCG YHELMLPENE PGSSIMPGKV NPTQNEALTQ 370 380 390 400 410 420 VCVQVMGNNA AITFAGSQGQ FELNVFKPVM IANLLNSIRL ITDAAYSFRV HCVEGIKANE 430 440 450 460 470 480 PRIHELLTKS LMLVTALNPK IGYDAASKVA KNAHKKGITL KESALELGVL TEKEFDEWVV PEHMLGPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1." Wu M., Tzagoloff A. J. Biol. Chem. 262:12275-12282(1987) [PubMed: 3040736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M. Biochemistry 40:9758-9769(2001) [PubMed: 11502169] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-52, SUBCELLULAR LOCATION. Strain: ATCC 201238 / W303-1B.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C. Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[7]	"Crystal structures of native and recombinant yeast fumarase." Weaver T., Lees M., Zaitsev V., Zaitseva I., Duke E., Lindley P., McSweeny S., Svensson A., Keruchenko J., Keruchenko I., Gladilin K., Banaszak L. J. Mol. Biol. 280:431-442(1998) [PubMed: 9665847] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02802 Genomic DNA. Translation: AAA66909.1.
Z73618 Genomic DNA. Translation: CAA97997.1.
BK006949 Genomic DNA. Translation: DAA11174.1.

PIR

UFBYM. S65295.

RefSeq

NP_015061.1. NM_001184076.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YFM	X-ray	2.60	A	1-488	[»]

ProteinModelPortal

P08417.

SMR

P08417. Positions 27-485.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6451N.

IntAct

P08417. 5 interactions.

MINT

MINT-606236.

STRING

P08417.

Proteomic databases

PeptideAtlas

P08417.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL262W; YPL262W; YPL262W.

GeneID

855866.

KEGG

sce:YPL262W.

NMPDR

fig|4932.3.peg.6185.

Organism-specific databases

CYGD

YPL262w.

SGD

S000006183. FUM1.

Phylogenomic databases

eggNOG

fuNOG07385.

GeneTree

EFGT00050000004718.

HOGENOM

HBG284369.

OMA

AGHEPLT.

OrthoDB

EOG44QX89.

Enzyme and pathway databases

BRENDA

4.2.1.2. 984.

Gene expression databases

ArrayExpress

P08417.

Genevestigator

P08417.

GermOnline

YPL262W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]

Gene3D

G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.

KO

K01679.

Pfam

PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR00979. FumC_II. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

980493.

Entry information

Entry name

FUMH_YEAST

Accession

Primary (citable) accession number: P08417
Secondary accession number(s): D6W3A8, Q08978

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program