Q54VA2 (FUMH_DICDI) 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:	fumH
ORF Names:	DDB_G0280495

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	485 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	Isoform 1: Mitochondrion By similarity. Isoform 2: Cytoplasm By similarity.
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	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing
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: dictyBase response to bacterium Inferred from expression pattern PubMed 19482547. Source: dictyBase tricarboxylic acid cycle Inferred by curator. Source: dictyBase
Cellular_component	extracellular space Inferred from direct assay PubMed 20422638. Source: dictyBase mitochondrion Inferred from sequence or structural similarity. Source: dictyBase phagocytic vesicle Inferred from direct assay PubMed 19482547. Source: dictyBase tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q54VA2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q54VA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 19	19	Mitochondrion Potential
	Chain	20 – 485	466	Fumarate hydratase, mitochondrial		PRO_0000331360
Regions
	Region	150 – 153	4	B site By similarity
	Region	160 – 162	3	Substrate binding By similarity
Sites
	Binding site	120	1	Substrate By similarity
Natural variations
	Alternative sequence	1 – 19	19	Missing in isoform 2.		VSP_033185

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A70941925A48FBBE	FASTA	485	52,963
	10 20 30 40 50 60 MLSASRKLNN QQFLKTIRNM TTFRSEFDTF GEVKVNDEKY WGAQTQRSLE NFDIGGESEK 70 80 90 100 110 120 MPLMVVRSFG ILKRCAAIVN KKYGLDATIA DNIAKAATEV VEGKLDDQFP LVVFQTGSGT 130 140 150 160 170 180 QSNMNANEVI SNRAIELMTG KRDFSKKLVH PNDHVNKSQS SNDTFPTCMH IAAAISINEK 190 200 210 220 230 240 LVPALEMLLA AMRTKQNEFN HIIKIGRTHL QDATPLTLGQ EFSGYCTQIE YGIQRIKDTL 250 260 270 280 290 300 PRLYNLAQGG TAVGTGLNTP VGFDVDIASE VAKFTGLPFK TAPNKFEALA AHDAMVEVSG 310 320 330 340 350 360 ALNTVAVSLM KIANDIRFLG SGPRCGLGEL ILPENEPGSS IMPGKVNPTQ CEAMTMVCAQ 370 380 390 400 410 420 VMGNNTTVSI AGSNGHFELN VFKPVIIKNV LSSIRLIADA SVSFTKHCVV GIKADEKRID 430 440 450 460 470 480 QLLHESLMLV TALNPYIGYD KAAKAAKKAH KEKTTLKEAC LSLGFTTSEE FDKWVDPSKM IGSMK
	Isoform 2 [UniParc]. Checksum: F428A15A5F9FB22B	FASTA	466	50,718
	10 20 30 40 50 60 MTTFRSEFDT FGEVKVNDEK YWGAQTQRSL ENFDIGGESE KMPLMVVRSF GILKRCAAIV 70 80 90 100 110 120 NKKYGLDATI ADNIAKAATE VVEGKLDDQF PLVVFQTGSG TQSNMNANEV ISNRAIELMT 130 140 150 160 170 180 GKRDFSKKLV HPNDHVNKSQ SSNDTFPTCM HIAAAISINE KLVPALEMLL AAMRTKQNEF 190 200 210 220 230 240 NHIIKIGRTH LQDATPLTLG QEFSGYCTQI EYGIQRIKDT LPRLYNLAQG GTAVGTGLNT 250 260 270 280 290 300 PVGFDVDIAS EVAKFTGLPF KTAPNKFEAL AAHDAMVEVS GALNTVAVSL MKIANDIRFL 310 320 330 340 350 360 GSGPRCGLGE LILPENEPGS SIMPGKVNPT QCEAMTMVCA QVMGNNTTVS IAGSNGHFEL 370 380 390 400 410 420 NVFKPVIIKN VLSSIRLIAD ASVSFTKHCV VGIKADEKRI DQLLHESLML VTALNPYIGY 430 440 450 460 DKAAKAAKKA HKEKTTLKEA CLSLGFTTSE EFDKWVDPSK MIGSMK

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000036 Genomic DNA. Translation: EAL67226.1. AAFI02000036 Genomic DNA. Translation: EAL67227.1.
RefSeq	XP_001134561.1. XM_001134561.1. XP_641207.1. XM_636115.1.
3D structure databases
ProteinModelPortal	Q54VA2.
SMR	Q54VA2. Positions 23-482.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0231397.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231397; DDB0231397; DDB_G0280495.
GeneID	8622588.
KEGG	ddi:DDB_G0280495.
Organism-specific databases
dictyBase	DDB_G0280495. fumH.
Phylogenomic databases
eggNOG	COG0114.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	CLSZ2430620.
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...

Entry information

Entry name

FUMH_DICDI

Accession

Primary (citable) accession number: Q54VA2
Secondary accession number(s): Q54VA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	May 29, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)