P14407 (FUMB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	fumB
Ordered Locus Names:	b4122, JW4083

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	It functions in the generation of fumarate for use as an anaerobic electron acceptor.
Catalytic activity	(S)-malate = fumarate + H2O.
Cofactor	Binds 1 4Fe-4S cluster.
Enzyme regulation	Subject to anaerobic repression.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subunit structure	Homodimer.
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
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	biofilm formation Inferred from mutant phenotype PubMed 16385049. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki tricarboxylic acid cycle Inferred from genetic interaction PubMed 3005475. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW D(-)-tartrate dehydratase activity Inferred from mutant phenotype PubMed 17643228. Source: EcoCyc fumarate hydratase activity Inferred from direct assay PubMed 8226748. Source: EcoCyc 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
	Chain	1 – 548	548	Fumarate hydratase class I, anaerobic		PRO_0000195660
Sites
	Active site	397	1	Potential
	Metal binding	318	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	463	1	Substrate Potential
Amino acid modifications
	Modified residue	192	1	N6-acetyllysine Ref.5
Experimental info
	Sequence conflict	50	1	L → V in AAA23827. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14407 [UniParc]. Last modified July 19, 2003. Version 2. Checksum: 73685337862496B7	FASTA	548	60,105
	10 20 30 40 50 60 MSNKPFIYQA PFPMGKDNTE YYLLTSDYVS VADFDGETIL KVEPEALTLL AQQAFHDASF 70 80 90 100 110 120 MLRPAHQKQV AAILHDPEAS ENDKYVALQF LRNSEIAAKG VLPTCQDTGT AIIVGKKGQR 130 140 150 160 170 180 VWTGGGDEET LSKGVYNTYI EDNLRYSQNA ALDMYKEVNT GTNLPAQIDL YAVDGDEYKF 190 200 210 220 230 240 LCVAKGGGSA NKTYLYQETK ALLTPGKLKN FLVEKMRTLG TAACPPYHIA FVIGGTSAET 250 260 270 280 290 300 NLKTVKLASA HYYDELPTEG NEHGQAFRDV QLEQELLEEA QKLGLGAQFG GKYFAHDIRV 310 320 330 340 350 360 IRLPRHGASC PVGMGVSCSA DRNIKAKINR EGIWIEKLEH NPGQYIPQEL RQAGEGEAVK 370 380 390 400 410 420 VDLNRPMKEI LAQLSQYPVS TRLSLTGTII VGRDIAHAKL KELIDAGKEL PQYIKDHPIY 430 440 450 460 470 480 YAGPAKTPAG YPSGSLGPTT AGRMDSYVDL LQSHGGSMIM LAKGNRSQQV TDACHKHGGF 490 500 510 520 530 540 YLGSIGGPAA VLAQQSIKHL ECVAYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIVN KQCANCTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12." Bell P.J., Andrews S.C., Sivak M.N., Guest J.R. J. Bacteriol. 171:3494-3503(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 50. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27058 Genomic DNA. Translation: AAA23827.1. U14003 Genomic DNA. Translation: AAA97022.1. U00096 Genomic DNA. Translation: AAC77083.1. AP009048 Genomic DNA. Translation: BAE78124.1.
PIR	B44511. A65222.
RefSeq	NP_418546.1. NC_000913.2. YP_492265.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P14407.
SMR	P14407. Positions 356-537.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14407. 6 interactions.
STRING	511145.b4122.
Proteomic databases
PaxDb	P14407.
PRIDE	P14407.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC77083; AAC77083; b4122. BAE78124; BAE78124; BAE78124.
GeneID	12933156. 948642.
KEGG	ecj:Y75_p4009. eco:b4122.
PATRIC	32123809. VBIEscCol129921_4253.
Organism-specific databases
EchoBASE	EB0352.
EcoGene	EG10357. fumB.
Phylogenomic databases
eggNOG	COG1951.
HOGENOM	HOG000009338.
KO	K01676.
OMA	PFPLAHD.
ProtClustDB	PRK15391.
Enzyme and pathway databases
BioCyc	EcoCyc:FUMB-MONOMER. ECOL316407:JW4083-MONOMER. MetaCyc:FUMB-MONOMER.
SABIO-RK	P14407.
UniPathway	UPA00223; UER01007.
Gene expression databases
Genevestigator	P14407.
Family and domain databases
Gene3D	3.20.130.10. 1 hit.
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]
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

FUMB_ECOLI

Accession

Primary (citable) accession number: P14407
Secondary accession number(s): P78139, Q2M6I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 19, 2003
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program