Q983U5 (FUMC_RHILO) 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:	mll8172

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium › Rhizobium loti

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743
Catalytic activity	(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743
Subunit structure	Homotetramer By similarity. HAMAP-Rule MF_00743
Subcellular location	Cytoplasm By similarity 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Allosteric enzyme Complete 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 – 465	465	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161304
Regions
	Region	100 – 102	3	Substrate binding By similarity
	Region	131 – 134	4	B site By similarity
	Region	141 – 143	3	Substrate binding By similarity
	Region	189 – 190	2	Substrate binding By similarity
	Region	326 – 328	3	Substrate binding By similarity
Sites
	Active site	190	1	Proton donor/acceptor By similarity
	Active site	320	1	By similarity
	Binding site	321	1	Substrate By similarity
	Site	333	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q983U5 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 85407C084D9221F9	FASTA	465	49,592
	10 20 30 40 50 60 MTVAKTRTET DTFGPIEVAA DRYWGAQAQR SLGNFKIGWE KQPASIVRAL GVVKRAAAEV 70 80 90 100 110 120 NMEMKRLDPV VGKAIVDAAQ EVIDGKLNDH FPLVVWQTGS GTQSNMNANE VISNRAIEML 130 140 150 160 170 180 GGVMGSKKPV HPNDHVNMSQ SSNDTYPTAM HIACAEQVVH HLIPALHHLH KALDAKARAF 190 200 210 220 230 240 NHIIKIGRTH TQDATPLTLG QEFSGYAAQV ASSIKRIEMT LPGLQELAQG GTAVGTGLNA 250 260 270 280 290 300 PVGFAEKVAD RIAAITGIAF VTAPNKFEAL AAHDSMVFSH GAINAAAAAL FKIANDIRFL 310 320 330 340 350 360 GSGPRSGLGE LSLPENEPGS SIMPGKVNPT QCEAMTQVCV QVFGNNAALT FAGSQGHFEL 370 380 390 400 410 420 NVYNPLMAYN FLQSVQLLSD ASVSFTDNCV VGIEAREDNI KAALDRSLML VTALAPTIGY 430 440 450 460 DNAAKIAKTA HKNGTTLREE ALATGLVSEV DYDRLVRPED MTHPG

References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S. DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB53785.1.
RefSeq	NP_108324.1. NC_002678.2.
3D structure databases
ProteinModelPortal	Q983U5.
SMR	Q983U5. Positions 7-464.
ModBase	Search...
Protein-protein interaction databases
STRING	266835.mll8172.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB53785; BAB53785; BAB53785.
GeneID	1230976.
KEGG	mlo:mll8172.
PATRIC	22487309. VBIMesLot2464_6528.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	MLOT266835:GJ9L-6478-MONOMER.
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. [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.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_RHILO

Accession

Primary (citable) accession number: Q983U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program