Reviewed, UniProtKB/Swiss-Prot Q92PB6 (FUMC_RHIME)

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:	R01859
ORF Names:	SMc00149

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O. HAMAP MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743
Subunit structure	Homotetramer By similarity. HAMAP MF_00743
Subcellular location	Cytoplasm By similarity HAMAP 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 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	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 – 463	463	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161305
Regions
	Region	129 – 132	4	B site By similarity
	Region	139 – 141	3	Substrate binding By similarity
Sites
	Binding site	100	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92PB6-1 [UniParc]. Last modified December 15, 2003. Version 2. Checksum: A500EDE8A6789C5F	FASTA	463	49,133
	10 20 30 40 50 60 MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI VKQAAARANM 70 80 90 100 110 120 ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT QSNMNANEVV SNRAIELLGG 130 140 150 160 170 180 VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI ACAERVIHDL LPALKHLHKA LEEKVKAFDH 190 200 210 220 230 240 IIKIGRTHTQ DATPLTLGQE FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV 250 260 270 280 290 300 GFAEKVAEEI AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS 310 320 330 340 350 360 GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA GSQGHFELNV 370 380 390 400 410 420 YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA ALDRSLMLVT ALAPKIGYDN 430 440 450 460 AAKIAKTAHK NGTTLREEAV GGGYVTDEEF DAVVRPETMI GPA

References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC46438.1. Different initiation.
RefSeq	NP_385965.3.
3D structure databases
SMR	Q92PB6. Positions 5-462.
ModBase	Search...
Genome annotation databases
GeneID	1233524.
GenomeReviews	Gene locus R01859 in contig AL591688_GR.
KEGG	sme:SMc00149.
NMPDR	fig|266834.1.peg.3153.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284369.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC00149-MONOMER.
BRENDA	4.2.1.2. 142.
Family and domain databases
HAMAP	MF_00743. FumaraseC. [Tree]
InterPro	IPR005677. Fum_hydII. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_RHIME

Accession

Primary (citable) accession number: Q92PB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	February 9, 2010
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)