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Q51404 (FUMC1_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fumarate hydratase class II 1
Short name=Fumarase C 1
EC=4.2.1.2
Gene names
Name:fumC1
Ordered Locus Names:PA4470
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity. HAMAP-Rule MF_00743

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Sequence caution

The sequence AAB17389.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Fumarate hydratase class II 1 HAMAP-Rule MF_00743
PRO_0000161299

Regions

Region98 – 1003Substrate binding By similarity
Region123 – 1264B site By similarity
Region133 – 1353Substrate binding By similarity
Region181 – 1822Substrate binding By similarity
Region318 – 3203Substrate binding By similarity

Sites

Active site1821Proton donor/acceptor By similarity
Active site3121 By similarity
Binding site3131Substrate By similarity
Site3251Important for catalytic activity By similarity

Experimental info

Sequence conflict1561P → S in AAB17389. Ref.2
Sequence conflict2221G → A in AAB17389. Ref.2
Sequence conflict3311A → G in AAB17389. Ref.2
Sequence conflict3401Missing in AAB17389. Ref.2
Sequence conflict3621N → T in AAB17389. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q51404 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 48D87C8B1C76B708

FASTA45848,696
        10         20         30         40         50         60 
MTDTRIERDS MGELAVPATA LYGAQTQRAV NNFPVSGQRM PQAFVRALLL AKAAAARANV 

        70         80         90        100        110        120 
SLQQLDAPMG EAIADTCLQL LQEDFMQHFP VDVFQTGSGT SSNMNANEVV ATLASRRLGG 

       130        140        150        160        170        180 
KVNPNDHVNC GQSSNDIIPS TIHISAALEI SERLLPALRH LEQTIQSKAG EVHAYVKTGR 

       190        200        210        220        230        240 
THLMDAMPVR MSQVLGGWAQ QVRQAGVHIE SVLPALQQLA QGGTAVGTGI NAHPRFAERF 

       250        260        270        280        290        300 
SQELNDLTGL AFRPGDDFFA LIGSQDTAVA ASGQLKTLAV TLMKLANDLR WMNSGPLAGL 

       310        320        330        340        350        360 
GEIELEALQP GSSIMPGKVN PVIPEATAMV AAQVIGNDAA IAVAGQSGNF ELNVMLPLVA 

       370        380        390        400        410        420 
DNLLHSIQLL ANVSRLLADK AIASFKVNQG KLSEALARNP ILVTALNPII GYQKAAEIAK 

       430        440        450 
QAYREGRPII DVALENTDLD RARLEVLLDP EKLTAGGL

« Hide

References

« Hide 'large scale' references
[1]Hassett D.J., Klotz M.G., Howell M.L.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FRD1.
[2]"The Pseudomonas aeruginosa fumC and sodA genes belong to an iron-responsive operon."
Polack B., Dacheux D., Delic-Attree I., Toussaint B., Vignais P.M.
Biochem. Biophys. Res. Commun. 226:555-560(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CHA.
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U59458 Genomic DNA. Translation: AAB02830.1.
U72494 Genomic DNA. Translation: AAB17389.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG07858.1.
PIRF83088.
JC4982.
RefSeqNP_253160.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ51404.
SMRQ51404. Positions 5-447.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA4470.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881033.
KEGGpae:PA4470.
PATRIC19843667. VBIPseAer58763_4680.

Organism-specific databases

PseudoCAPPA4470.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAIIPTTIH.
ProtClustDBPRK00485.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC1_PSEAE
AccessionPrimary (citable) accession number: Q51404
Secondary accession number(s): P72168
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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