Q82ID7 (FUMC_STRAW) 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:	SAV_3221

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	467 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: UniProtKB-KW
Cellular component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	fumarate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161321
Regions
	Region	129 – 132	4	B site By similarity
	Region	139 – 141	3	Substrate binding By similarity
Sites
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82ID7 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 5D984D1060B87F36	FASTA	467	49,801
	10 20 30 40 50 60 MTDEDDKQNY RVEHDSMGEV RVPADAKWRA QTQRAVENFP ISGQRLERAH IEALARIKGA 70 80 90 100 110 120 AAKVNAELGV LDKDVAEAIQ EAAAEVAEGR WDEHFPVDVF QTGSGTSSNM NANEVIATLA 130 140 150 160 170 180 TERLGRDVHP NDHVNASQSS NDVFPSSIHI AATAAVTRDL VPALEHLAAA LGRKSEEFAD 190 200 210 220 230 240 VVKAGRTHLM DATPVTLGQE FGGYAAQVRY GVERLAASLP RLAELPLGGT AVGTGINTPP 250 260 270 280 290 300 GFSAAVIAEV ARVTGLPLTE ARDHFEAQGA RDGIVETSGQ LRTIAVGLTK IANDLRWMAS 310 320 330 340 350 360 GPRTGLSEIS LPDLQPGSSI MPGKVNPVIP EAVLMVAAQV TGNDATVAAA GAAGNFELNV 370 380 390 400 410 420 MLPVIAKNVL ESVRLLAHVS RLLADRTVDG IVAHRDRARE YAESSPSVVT PLNKYIGYEE 430 440 450 460 AAKVAKKALA ERQTIRQVVL ESGYVDRGDL TLEQLDEALD VLRMTHP

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC70932.1.
RefSeq	NP_824397.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q82ID7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1210693.
GenomeReviews	Gene locus SAV_3221 in contig BA000030_GR.
KEGG	sma:SAV_3221.
NMPDR	fig|227882.1.peg.3223.
PATRIC	23720069. VBIStrAve112782_3441.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284369.
OMA	QVIGHHT.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV3221-MONOMER.
Family and domain databases
HAMAP	MF_00743. FumaraseC. [Tree]
InterPro	IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR022761. Lyase1_N. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01679.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_STRAW

Accession

Primary (citable) accession number: Q82ID7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program