P39461 (FUMC_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase class II
Short name=Fumarase C
EC=4.2.1.2

Gene names

Name:	fumC
Ordered Locus Names:	SSO1077

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › Sulfolobus solfataricus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as an auxiliary aerobic enzyme in the citric acid cycle. Ref.4
Catalytic activity	(S)-malate = fumarate + H2O. Ref.4
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743
Subunit structure	Homotetramer. Ref.4
Subcellular location	Cytoplasm HAMAP-Rule MF_00743.
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. HAMAP-Rule MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.125 mM for malate (at pH 7.5 and at 70 degrees Celsius) Ref.4 KM=0.3 mM for malate (at pH 7.5 and at 70 degrees Celsius) pH dependence: Optimum pH is 8.0. Temperature dependence: Optimum temperature is 85 degrees Celsius. Active from 40 to 90 degrees Celsius.
Sequence caution	The sequence AAK41339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161334
Regions
	Region	76 – 78	3	Substrate binding By similarity
	Region	101 – 104	4	B site By similarity
	Region	111 – 113	3	Substrate binding By similarity
	Region	159 – 160	2	Substrate binding By similarity
	Region	297 – 299	3	Substrate binding By similarity
Sites
	Active site	160	1	Proton donor/acceptor By similarity
	Active site	291	1	By similarity
	Binding site	292	1	Substrate By similarity
	Site	304	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39461 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 8D2A9CF37817EA6C	FASTA	438	47,911
	10 20 30 40 50 60 MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS IIKASDDLID 70 80 90 100 110 120 GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV HPNDHVNFGQ SSNDTVPTAI 130 140 150 160 170 180 RIAAVAEVTN RLLPALQQII SSLNKKAEEY KDVIKAGRTH LRDALPVTLG QELSAYADAF 190 200 210 220 230 240 QHEHEQVMNI LEYVKELPIG GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR 250 260 270 280 290 300 LLTDLLLLSG ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP 310 320 330 340 350 360 VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS EALEKMSRLV 370 380 390 400 410 420 IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK LNKGMSIREA LRELGYSDNE 430 INKILDLSKL VKPGFTAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase." Colombo S., Grisa M., Tortora P., Vanoni M. FEBS Lett. 337:93-98(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14. Strain: DSM 5833 / MT-4.
[2]	Erratum Colombo S., Grisa M., Tortora P., Vanoni M. FEBS Lett. 340:151-153(1994) [PubMed] [Europe PMC] [Abstract]
[3]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[4]	"Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus." Puchegger S., Redl B., Stoeffler G. J. Gen. Microbiol. 136:1537-1541(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75402 Genomic DNA. Translation: CAA53156.1. AE006641 Genomic DNA. Translation: AAK41339.1. Different initiation.
PIR	D90260. S40448.
RefSeq	NP_342549.1. NC_002754.1.
3D structure databases
ProteinModelPortal	P39461.
ModBase	Search...
Protein-protein interaction databases
STRING	273057.SSO1077.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK41339; AAK41339; SSO1077.
GeneID	1454118.
KEGG	sso:SSO1077.
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BRENDA	4.2.1.2. 6163.
UniPathway	UPA00223; UER01007.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
HAMAP	MF_00743. FumaraseC.
InterPro	IPR003031. D_crystallin. 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. IPR001611. Leu-rich_rpt. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. PS51450. LRR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_SULSO

Accession

Primary (citable) accession number: P39461

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program