P0AC34 (FUMA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase class I, aerobic
Short name=Fumarase
EC=4.2.1.2

Gene names

Name:	fumA
Ordered Locus Names:	c2004

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	It functions as an aerobic enzyme in the citric acid cycle. It accounts for about 80% of the fumarase activity when the bacteria grows aerobically By similarity.
Catalytic activity	(S)-malate = fumarate + H2O.
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Enzyme regulation	Subject to aerobic respiratory control and catabolite repression.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class-I fumarase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW fumarate hydratase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 548	547	Fumarate hydratase class I, aerobic		PRO_0000195658
Sites
	Active site	397	1	Potential
	Metal binding	318	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	463	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	P0AC34 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6082744088C64603	FASTA	548	60,299
	10 20 30 40 50 60 MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL ARQAFHDASF 70 80 90 100 110 120 MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR 130 140 150 160 170 180 VWTGGGDEAA LARGVYNTYI EDNLRYSQNA PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF 190 200 210 220 230 240 LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET 250 260 270 280 290 300 NLKTVKLASA KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV 310 320 330 340 350 360 IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL RKAGEGEAVR 370 380 390 400 410 420 VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDNGEGL PQYIKDHPIY 430 440 450 460 470 480 YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQAQGGSMIM LAKGNRSQQV TDACKKHGGF 490 500 510 520 530 540 YLGSIGGPAA VLAQGSIKSL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL TQCTRCVK

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN80464.1.
RefSeq	NP_753899.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P0AC34.
SMR	P0AC34. Positions 356-537.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000045454; EBESCP00000043803; EBESCG00000044504.
GeneID	1036044.
GenomeReviews	Gene locus c2004 in contig AE014075_GR.
KEGG	ecc:c2004.
PATRIC	18281905. VBIEscCol75197_1871.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010386.
HOGENOM	HBG294102.
OMA	DKFVALD.
ProtClustDB	PRK15390.
Family and domain databases
InterPro	IPR004646. Fe-S_hydro-lyase_TtdA-typ_cat. IPR004647. Fe-S_hydro-lyase_TtdB-typ_cat. IPR011167. Fe_dep_fumarate_hydratase. IPR020557. Fumarate_lyase_CS. [Graphical view]
Gene3D	G3DSA:3.20.130.10. TtdB_fumA_fumB. 1 hit.
KO	K01676.
Pfam	PF05681. Fumerase. 1 hit. PF05683. Fumerase_C. 1 hit. [Graphical view]
PIRSF	PIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAM	SSF117457. SSF117457. 1 hit.
TIGRFAMs	TIGR00722. TtdA_fumA_fumB. 1 hit. TIGR00723. TtdB_fumA_fumB. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMA_ECOL6

Accession

Primary (citable) accession number: P0AC34
Secondary accession number(s): P00923, P76889

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program