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P14407

- FUMB_ECOLI

UniProt

P14407 - FUMB_ECOLI

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Protein

Fumarate hydratase class I, anaerobic

Gene

fumB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate.4 Publications

Catalytic activityi

(S)-malate = fumarate + H2O.1 Publication
(S,S)-tartrate = oxaloacetate + H2O.1 Publication

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Kineticsi

  1. KM=300 µM for (S)-malate1 Publication
  2. KM=320 µM for fumarate1 Publication
  3. KM=800 µM for D-tartrate1 Publication

Vmax=490 µmol/min/mg enzyme for (S)-malate dehydration1 Publication

Vmax=1430 µmol/min/mg enzyme for fumarate hydration1 Publication

Vmax=9.2 µmol/min/mg enzyme for D-tartrate dehydration1 Publication

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  2. D(-)-tartrate dehydratase activity Source: EcoCyc
  3. fumarate hydratase activity Source: EcoCyc
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. biofilm formation Source: EcoCyc
  2. cellular response to DNA damage stimulus Source: EcoliWiki
  3. tricarboxylic acid cycle Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FUMB-MONOMER.
ECOL316407:JW4083-MONOMER.
MetaCyc:FUMB-MONOMER.
SABIO-RKP14407.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class I, anaerobic1 Publication (EC:4.2.1.21 Publication)
Alternative name(s):
D-tartrate dehydratase1 Publication (EC:4.2.1.811 Publication)
Fumarase B1 Publication
Gene namesi
Name:fumB1 Publication
Ordered Locus Names:b4122, JW4083
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10357. fumB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Disruption of this gene seriously impairs growth under anaerobic conditions on D-tartrate when glycerol is supplied as an electron donor (D-tartrate fermentation). Cells lacking this gene also lose most (about 79%) of D-tartrate dehydratase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Fumarate hydratase class I, anaerobicPRO_0000195660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14407.
PRIDEiP14407.

Expressioni

Inductioni

Is mainly expressed during anaerobic growth. Is under the control of the Fnr transcriptional regulator.1 Publication

Gene expression databases

GenevestigatoriP14407.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiP14407. 6 interactions.
STRINGi511145.b4122.

Structurei

3D structure databases

ProteinModelPortaliP14407.
SMRiP14407. Positions 356-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.Curated

Phylogenomic databases

eggNOGiCOG1951.
HOGENOMiHOG000009338.
InParanoidiP14407.
KOiK01676.
OMAiDSEGVNA.
OrthoDBiEOG6TXR10.
PhylomeDBiP14407.

Family and domain databases

Gene3Di3.20.130.10. 1 hit.
InterProiIPR004646. 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]
PfamiPF05681. Fumerase. 1 hit.
PF05683. Fumerase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAMiSSF117457. SSF117457. 1 hit.
TIGRFAMsiTIGR00722. ttdA_fumA_fumB. 1 hit.
TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14407-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNKPFIYQA PFPMGKDNTE YYLLTSDYVS VADFDGETIL KVEPEALTLL
60 70 80 90 100
AQQAFHDASF MLRPAHQKQV AAILHDPEAS ENDKYVALQF LRNSEIAAKG
110 120 130 140 150
VLPTCQDTGT AIIVGKKGQR VWTGGGDEET LSKGVYNTYI EDNLRYSQNA
160 170 180 190 200
ALDMYKEVNT GTNLPAQIDL YAVDGDEYKF LCVAKGGGSA NKTYLYQETK
210 220 230 240 250
ALLTPGKLKN FLVEKMRTLG TAACPPYHIA FVIGGTSAET NLKTVKLASA
260 270 280 290 300
HYYDELPTEG NEHGQAFRDV QLEQELLEEA QKLGLGAQFG GKYFAHDIRV
310 320 330 340 350
IRLPRHGASC PVGMGVSCSA DRNIKAKINR EGIWIEKLEH NPGQYIPQEL
360 370 380 390 400
RQAGEGEAVK VDLNRPMKEI LAQLSQYPVS TRLSLTGTII VGRDIAHAKL
410 420 430 440 450
KELIDAGKEL PQYIKDHPIY YAGPAKTPAG YPSGSLGPTT AGRMDSYVDL
460 470 480 490 500
LQSHGGSMIM LAKGNRSQQV TDACHKHGGF YLGSIGGPAA VLAQQSIKHL
510 520 530 540
ECVAYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIVN KQCANCTK
Length:548
Mass (Da):60,105
Last modified:July 19, 2003 - v2
Checksum:i73685337862496B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501L → V in AAA23827. (PubMed:2656658)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27058 Genomic DNA. Translation: AAA23827.1.
U14003 Genomic DNA. Translation: AAA97022.1.
U00096 Genomic DNA. Translation: AAC77083.1.
AP009048 Genomic DNA. Translation: BAE78124.1.
PIRiA65222. B44511.
RefSeqiNP_418546.1. NC_000913.3.
YP_492265.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77083; AAC77083; b4122.
BAE78124; BAE78124; BAE78124.
GeneIDi12933156.
948642.
KEGGiecj:Y75_p4009.
eco:b4122.
PATRICi32123809. VBIEscCol129921_4253.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27058 Genomic DNA. Translation: AAA23827.1 .
U14003 Genomic DNA. Translation: AAA97022.1 .
U00096 Genomic DNA. Translation: AAC77083.1 .
AP009048 Genomic DNA. Translation: BAE78124.1 .
PIRi A65222. B44511.
RefSeqi NP_418546.1. NC_000913.3.
YP_492265.1. NC_007779.1.

3D structure databases

ProteinModelPortali P14407.
SMRi P14407. Positions 356-537.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P14407. 6 interactions.
STRINGi 511145.b4122.

Proteomic databases

PaxDbi P14407.
PRIDEi P14407.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77083 ; AAC77083 ; b4122 .
BAE78124 ; BAE78124 ; BAE78124 .
GeneIDi 12933156.
948642.
KEGGi ecj:Y75_p4009.
eco:b4122.
PATRICi 32123809. VBIEscCol129921_4253.

Organism-specific databases

EchoBASEi EB0352.
EcoGenei EG10357. fumB.

Phylogenomic databases

eggNOGi COG1951.
HOGENOMi HOG000009338.
InParanoidi P14407.
KOi K01676.
OMAi DSEGVNA.
OrthoDBi EOG6TXR10.
PhylomeDBi P14407.

Enzyme and pathway databases

BioCyci EcoCyc:FUMB-MONOMER.
ECOL316407:JW4083-MONOMER.
MetaCyc:FUMB-MONOMER.
SABIO-RK P14407.

Miscellaneous databases

PROi P14407.

Gene expression databases

Genevestigatori P14407.

Family and domain databases

Gene3Di 3.20.130.10. 1 hit.
InterProi 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 ]
Pfami PF05681. Fumerase. 1 hit.
PF05683. Fumerase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAMi SSF117457. SSF117457. 1 hit.
TIGRFAMsi TIGR00722. ttdA_fumA_fumB. 1 hit.
TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)."
    Guest J.R., Miles J.S., Roberts R.E., Woods S.A.
    J. Gen. Microbiol. 131:2971-2984(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF THE STRUCTURAL GENE.
  6. "Differential roles of the Escherichia coli fumarases and fnr-dependent expression of fumarase B and aspartase."
    Woods S.A., Guest J.R.
    FEMS Microbiol. Lett. 48:219-224(1987)
    Cited for: FUNCTION, INDUCTION.
  7. "Two biochemically distinct classes of fumarase in Escherichia coli."
    Woods S.A., Shwartzbach S.D., Guest J.R.
    Biochim. Biophys. Acta 954:14-26(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: K12.
  8. "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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  9. "Anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-tartrate dehydratase."
    Kim O.B., Lux S., Unden G.
    Arch. Microbiol. 188:583-589(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Biochemical similarities and differences between the catalytic [4Fe-4S] cluster containing fumarases FumA and FumB from Escherichia coli."
    van Vugt-Lussenburg B.M., van der Weel L., Hagen W.R., Hagedoorn P.L.
    PLoS ONE 8:E55549-E55549(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: K12.

Entry informationi

Entry nameiFUMB_ECOLI
AccessioniPrimary (citable) accession number: P14407
Secondary accession number(s): P78139, Q2M6I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 19, 2003
Last modified: November 26, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3