Reviewed, UniProtKB/Swiss-Prot Q9FBN6 (FUMC_STRCO)

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:	SCO5042
ORF Names:	SCK7.15c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O. HAMAP MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743
Subunit structure	Homotetramer By similarity.
Subcellular location	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
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 461	461	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161322
Regions
	Region	123 – 126	4	B site By similarity
	Region	133 – 135	3	Substrate binding By similarity
Sites
	Binding site	100	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FBN6-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 0853F809C265A62D	FASTA	461	49,068
	10 20 30 40 50 60 MSEYRIEHDS MGEVRVPADA KWRAQTQRAV ENFPVSGQRI ERAHIEALAR IKSAAAKVNA 70 80 90 100 110 120 ELGVLDEDVA GAIQEAAGEV AEGKWDEHFP VDVFQTGSGT SSNMNTNEVV ATLATERLGR 130 140 150 160 170 180 DVHPNDHVNA SQSSNDVFPS SIHIAATAAV TRDLIPALDH LAGALERKAG EFADVVKSGR 190 200 210 220 230 240 THLMDATPVT LGQEFGGYAA QVRYGIERLQ ASLPRLAELP LGGTAVGTGI NTPPGFSAAV 250 260 270 280 290 300 IEEVARATGL PLTEARDHFE AQGARDGIVE TSGQLRTIGV GLTKIANDLR WMASGPRTGL 310 320 330 340 350 360 AEISLPDLQP GSSIMPGKVN PVIPEAVLMV AAQVTGNDAT VAAAGAAGNF ELNVMLPVIA 370 380 390 400 410 420 KNVLESVRLL ANVSRLLADR TVDGIVAHPE RAREYAESSP SVVTPLNKYL GYEEAAKVAK 430 440 450 460 RALAERKTIR QTVLEGGYVE RGDLTREQLD QALDVLRMTR P

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939122 Genomic DNA. Translation: CAC05887.1.
RefSeq	NP_629194.1.
3D structure databases
HSSP	HSSP built from PDB template 1FUQ based on UniProtKB P05042.
ModBase	Search...
Genome annotation databases
GeneID	1100483.
GenomeReviews	Gene locus SCO5042 in contig AL645882_GR.
KEGG	sco:SCO5042.
NMPDR	fig|100226.1.peg.4997.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9FBN6.
OMA	WMNSGPL.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO5042-MON.
BRENDA	4.2.1.2. 1084.
Family and domain databases
HAMAP	MF_00743. [Tree]
InterPro	IPR003031. D_crystallin. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_STRCO

Accession

Primary (citable) accession number: Q9FBN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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