O94552 (FUMH_SCHPO) 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
ORF Names:	SPCC18.18c, SPCC290.01c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular location	Mitochondrion Potential.
Miscellaneous	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	Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from sequence or structural similarity. Source: PomBase tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase mitochondrial matrix Inferred from sequence or structural similarity. Source: PomBase tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion Potential
	Chain	40 – 520	481	Fumarate hydratase, mitochondrial		PRO_0000010332
Regions
	Region	184 – 187	4	B site By similarity
	Region	194 – 196	3	Substrate binding By similarity
Sites
	Binding site	155	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94552 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 4AF0DA8BF5E14AE8	FASTA	520	56,322
	10 20 30 40 50 60 MASVAHISTA KAIFRAGGLP CRRLITPTLT GLPLKTHRMN STTPTYHLIP KGGKHGEFRQ 70 80 90 100 110 120 ESDTFGPIQV PAEKYWGAQT QRSLQNFRIG GEKERLPLPL VRAFGVLKRA AASVNREFGL 130 140 150 160 170 180 DPKLADAIEQ AAQEVIDGRL DDNFPLVVFQ TGSGTQSNMN SNEVIANRAI EILGGTLGSK 190 200 210 220 230 240 KPVHPNDHVN MSQSSNDTFP TVMHIASVLQ IHTHLLPAMK HLHRALKGKE EEFKNIIKIG 250 260 270 280 290 300 RTHMQDATPL SLGQEFSGYV TQVGYGIERI NNALPRLCLL AQGGTAVGTG LNTFEGFDVK 310 320 330 340 350 360 VAEKVSKLTN IEFKTAPNKF EALAAHDAIV EMSGALNVIA CSLMKIANDI RQLGSGPRCG 370 380 390 400 410 420 LGELILPANE PGSSIMPGKV NPTQCEALTM VCAQVMGNHA TITVAGASGH CELNVFKPLL 430 440 450 460 470 480 AKNILSSIRL LGDACESFTD HCVVGIEPNY EGIARHLRDS LMLVTALNPH IGYDNCAKIA 490 500 510 520 KTALKNKSTL KHEFVTLGFG TPEQFDEWVR PELMISAKKV

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA21432.3.
PIR	T41265.
RefSeq	NP_588397.3. NM_001023388.3.
3D structure databases
ProteinModelPortal	O94552.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC18.18c-1.
Proteomic databases
PaxDb	O94552.
PRIDE	O94552.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC18.18c.1; SPCC18.18c.1:pep; SPCC18.18c.
GeneID	2539345.
KEGG	spo:SPCC18.18c.
Organism-specific databases
PomBase	SPCC18.18c.
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
OrthoDB	EOG44QX89.
Enzyme and pathway databases
UniPathway	UPA00223; UER01007.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
InterPro	IPR005677. Fum_hydII. IPR024083. Fumarase/histidase_N. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view]
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	20800510.

Entry information

Entry name

FUMH_SCHPO

Accession

Primary (citable) accession number: O94552
Secondary accession number(s): O74868

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program