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P14407

- FUMB_ECOLI

UniProt

P14407 - FUMB_ECOLI

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Protein

Fumarate hydratase class I, anaerobic

Gene
fumB, b4122, JW4083
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

It functions in the generation of fumarate for use as an anaerobic electron acceptor.

Catalytic activityi

(S)-malate = fumarate + H2O.

Cofactori

Binds 1 4Fe-4S cluster.

Enzyme regulationi

Subject to anaerobic repression.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi318 – 3181Iron-sulfur (4Fe-4S) By similarity
Active sitei397 – 3971 Reviewed prediction
Binding sitei463 – 4631Substrate Reviewed prediction

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 - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciEcoCyc:FUMB-MONOMER.
ECOL316407:JW4083-MONOMER.
MetaCyc:FUMB-MONOMER.
SABIO-RKP14407.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class I, anaerobic (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:fumB
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...

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

Gene expression databases

GenevestigatoriP14407.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP14407. 6 interactions.
STRINGi511145.b4122.

Structurei

3D structure databases

ProteinModelPortaliP14407.
SMRiP14407. Positions 356-537.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.

Phylogenomic databases

eggNOGiCOG1951.
HOGENOMiHOG000009338.
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

MSNKPFIYQA PFPMGKDNTE YYLLTSDYVS VADFDGETIL KVEPEALTLL    50
AQQAFHDASF MLRPAHQKQV AAILHDPEAS ENDKYVALQF LRNSEIAAKG 100
VLPTCQDTGT AIIVGKKGQR VWTGGGDEET LSKGVYNTYI EDNLRYSQNA 150
ALDMYKEVNT GTNLPAQIDL YAVDGDEYKF LCVAKGGGSA NKTYLYQETK 200
ALLTPGKLKN FLVEKMRTLG TAACPPYHIA FVIGGTSAET NLKTVKLASA 250
HYYDELPTEG NEHGQAFRDV QLEQELLEEA QKLGLGAQFG GKYFAHDIRV 300
IRLPRHGASC PVGMGVSCSA DRNIKAKINR EGIWIEKLEH NPGQYIPQEL 350
RQAGEGEAVK VDLNRPMKEI LAQLSQYPVS TRLSLTGTII VGRDIAHAKL 400
KELIDAGKEL PQYIKDHPIY YAGPAKTPAG YPSGSLGPTT AGRMDSYVDL 450
LQSHGGSMIM LAKGNRSQQV TDACHKHGGF YLGSIGGPAA VLAQQSIKHL 500
ECVAYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIVN KQCANCTK 548
Length:548
Mass (Da):60,105
Last modified:July 19, 2003 - v2
Checksum:i73685337862496B7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501L → V in AAA23827. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
KOi K01676.
OMAi DSEGVNA.
OrthoDBi EOG6TXR10.
PhylomeDBi P14407.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
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. "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.

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: July 9, 2014
This is version 133 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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