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P0AC33

- FUMA_ECOLI

UniProt

P0AC33 - FUMA_ECOLI

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Protein
Fumarate hydratase class I, aerobic
Gene
fumA, b1612, JW1604
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

(S)-malate = fumarate + H2O.

Cofactori

Binds 1 4Fe-4S cluster.

Enzyme regulationi

Subject to aerobic respiratory control and catabolite 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. fumarate hydratase activity Source: EcoCyc
  3. identical protein binding Source: IntAct
  4. metal ion binding Source: UniProtKB-KW
  5. oxaloacetate tautomerase activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. 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:FUMA-MONOMER.
ECOL316407:JW1604-MONOMER.
MetaCyc:FUMA-MONOMER.
RETL1328306-WGS:GSTH-2399-MONOMER.
SABIO-RKP0AC33.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class I, aerobic (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:fumA
Ordered Locus Names:b1612, JW1604
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10356. fumA.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 548547Fumarate hydratase class I, aerobic
PRO_0000195656Add
BLAST

Proteomic databases

PaxDbiP0AC33.
PRIDEiP0AC33.

Expressioni

Gene expression databases

GenevestigatoriP0AC33.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-549075,EBI-549075

Protein-protein interaction databases

DIPiDIP-36200N.
IntActiP0AC33. 5 interactions.
MINTiMINT-1310290.
STRINGi511145.b1612.

Structurei

3D structure databases

ProteinModelPortaliP0AC33.
SMRiP0AC33. Positions 356-537.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.

Phylogenomic databases

eggNOGiCOG1838.
HOGENOMiHOG000009338.
KOiK01676.
OMAiTCVEYPE.
OrthoDBiEOG6TXR10.
PhylomeDBiP0AC33.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC33-1 [UniParc]FASTAAdd to Basket

« Hide

MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL    50
ARQAFHDASF MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG 100
VLPTCQDTGT AIIVGKKGQR VWTGGGDEAA LARGVYNTYI EDNLRYSQNA 150
PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF LCIAKGGGSA NKTYLYQETK 200
ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET NLKTVKLASA 250
KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV 300
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL 350
RKAGEGEAVR VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL 400
KERMDNGEGL PQYIKDHPIY YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ 450
LQAQGGSMIM LAKGNRSQQV TDACKKHGGF YLGSIGGPAA VLAQGSIKSL 500
ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL TQCTRCVK 548
Length:548
Mass (Da):60,299
Last modified:January 23, 2007 - v2
Checksum:i6082744088C64603
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00522 Genomic DNA. Translation: CAA25204.1.
AP009048 Genomic DNA. Translation: BAA15360.1.
U00096 Genomic DNA. Translation: AAC74684.1.
PIRiA03531. UFECAQ.
RefSeqiNP_416129.1. NC_000913.3.
YP_489875.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74684; AAC74684; b1612.
BAA15360; BAA15360; BAA15360.
GeneIDi12934128.
946826.
KEGGiecj:Y75_p1588.
eco:b1612.
PATRICi32118526. VBIEscCol129921_1683.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00522 Genomic DNA. Translation: CAA25204.1 .
AP009048 Genomic DNA. Translation: BAA15360.1 .
U00096 Genomic DNA. Translation: AAC74684.1 .
PIRi A03531. UFECAQ.
RefSeqi NP_416129.1. NC_000913.3.
YP_489875.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0AC33.
SMRi P0AC33. Positions 356-537.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-36200N.
IntActi P0AC33. 5 interactions.
MINTi MINT-1310290.
STRINGi 511145.b1612.

Proteomic databases

PaxDbi P0AC33.
PRIDEi P0AC33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74684 ; AAC74684 ; b1612 .
BAA15360 ; BAA15360 ; BAA15360 .
GeneIDi 12934128.
946826.
KEGGi ecj:Y75_p1588.
eco:b1612.
PATRICi 32118526. VBIEscCol129921_1683.

Organism-specific databases

EchoBASEi EB0351.
EcoGenei EG10356. fumA.

Phylogenomic databases

eggNOGi COG1838.
HOGENOMi HOG000009338.
KOi K01676.
OMAi TCVEYPE.
OrthoDBi EOG6TXR10.
PhylomeDBi P0AC33.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci EcoCyc:FUMA-MONOMER.
ECOL316407:JW1604-MONOMER.
MetaCyc:FUMA-MONOMER.
RETL1328306-WGS:GSTH-2399-MONOMER.
SABIO-RK P0AC33.

Miscellaneous databases

PROi P0AC33.

Gene expression databases

Genevestigatori P0AC33.

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. "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli."
    Miles J.S., Guest J.R.
    Nucleic Acids Res. 12:3631-3642(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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. "Purification and characterization of two types of fumarase from Escherichia coli."
    Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.
    J. Biochem. 109:728-733(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    Strain: W / ATCC 11105 / DSM 1900.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / EMG2.
  7. "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.
  8. "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: BIOCHEMICAL ANALYSIS OF FUMA AND FUMC.
  9. "Fumarase A from E. coli contains a [4Fe-4S] cluster."
    Flint D.H., Emptage M.H., Guest J.R.
    J. Inorg. Biochem. 36:306-306(1989)
    Cited for: IRON-SULFUR CLUSTER.

Entry informationi

Entry nameiFUMA_ECOLI
AccessioniPrimary (citable) accession number: P0AC33
Secondary accession number(s): P00923, P76889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 77 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, Direct protein sequencing, 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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