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Protein

Fumarate hydratase class I, aerobic

Gene

fumA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.By similarity

Catalytic activityi

(S)-malate = fumarate + H2O.By similarity
Keto-oxaloacetate = enol-oxaloacetate.By similarity

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. fumarate hydratase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. oxaloacetate tautomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciECOL386585:GJFA-2292-MONOMER.
ECOO157:FUMA-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class I, aerobicBy similarity (EC:4.2.1.2By similarity)
Alternative name(s):
Fumarase ABy similarity
Oxaloacetate keto--enol-isomeraseBy similarity
Short name:
OAAKE isomeraseBy similarity
Oxaloacetate tautomeraseBy similarity (EC:5.3.2.2By similarity)
Gene namesi
Name:fumABy similarity
Ordered Locus Names:Z2615, ECs2318
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558 Componenti: Chromosome UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 548547Fumarate hydratase class I, aerobicPRO_0000195657Add
BLAST

Expressioni

Inductioni

Is expressed under aerobic conditions. Is repressed by glucose and anaerobiosis.By similarity

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi155864.Z2615.

Structurei

3D structure databases

ProteinModelPortaliQ8X4P8.
SMRiQ8X4P8. Positions 356-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.Curated

Phylogenomic databases

eggNOGiCOG1951.
HOGENOMiHOG000009338.
KOiK01676.
OMAiQIQTSQC.
OrthoDBiEOG6TXR10.

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.

Q8X4P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS LSEFEGQEIL KVAPEALTLL
60 70 80 90 100
ARQAFHDASF MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG
110 120 130 140 150
VLPTCQDTGT AIIVGKKGQR VWTGGGDEAA LARGVYNTYI EDNLRYSQNA
160 170 180 190 200
PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF LCIAKGGGSA NKTYLYQETK
210 220 230 240 250
ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET NLKTVKLASA
260 270 280 290 300
KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV
310 320 330 340 350
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL
360 370 380 390 400
RKAGEGEAVR VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL
410 420 430 440 450
KERMDNGEGL PQYIKDHPIY YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ
460 470 480 490 500
LQALGGSMIM LAKGNRSQQV TDACKKHGGF YLGSIGGPAA VLAQGSIKSL
510 520 530 540
ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL TQCTRCVK
Length:548
Mass (Da):60,298
Last modified:January 23, 2007 - v3
Checksum:iF26C7AA07630563F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56599.1.
BA000007 Genomic DNA. Translation: BAB35741.1.
PIRiC85767.
F90918.
RefSeqiNP_288047.1. NC_002655.2.
NP_310345.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56599; AAG56599; Z2615.
BAB35741; BAB35741; BAB35741.
GeneIDi916929.
961562.
KEGGiece:Z2615.
ecs:ECs2318.
PATRICi18353964. VBIEscCol44059_2195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56599.1.
BA000007 Genomic DNA. Translation: BAB35741.1.
PIRiC85767.
F90918.
RefSeqiNP_288047.1. NC_002655.2.
NP_310345.1. NC_002695.1.

3D structure databases

ProteinModelPortaliQ8X4P8.
SMRiQ8X4P8. Positions 356-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z2615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56599; AAG56599; Z2615.
BAB35741; BAB35741; BAB35741.
GeneIDi916929.
961562.
KEGGiece:Z2615.
ecs:ECs2318.
PATRICi18353964. VBIEscCol44059_2195.

Phylogenomic databases

eggNOGiCOG1951.
HOGENOMiHOG000009338.
KOiK01676.
OMAiQIQTSQC.
OrthoDBiEOG6TXR10.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciECOL386585:GJFA-2292-MONOMER.
ECOO157:FUMA-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiFUMA_ECO57
AccessioniPrimary (citable) accession number: Q8X4P8
Secondary accession number(s): Q7ADM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.