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Q51404

- FUMC1_PSEAE

UniProt

Q51404 - FUMC1_PSEAE

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Protein

Fumarate hydratase class II 1

Gene

fumC1

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei182 – 1821Proton donor/acceptorBy similarity
Active sitei312 – 3121By similarity
Binding sitei313 – 3131SubstrateUniRule annotation
Sitei325 – 3251Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: PseudoCAP

GO - Biological processi

  1. cellular response to iron ion starvation Source: PseudoCAP
  2. fumarate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II 1UniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase C 1UniRule annotation
Gene namesi
Name:fumC1UniRule annotation
Ordered Locus Names:PA4470
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA4470.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Fumarate hydratase class II 1PRO_0000161299Add
BLAST

Proteomic databases

PRIDEiQ51404.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA4470.

Structurei

3D structure databases

ProteinModelPortaliQ51404.
SMRiQ51404. Positions 5-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni123 – 1264B siteUniRule annotation
Regioni133 – 1353Substrate bindingUniRule annotation
Regioni181 – 1822Substrate bindingUniRule annotation
Regioni318 – 3203Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiQ51404.
KOiK01679.
OMAiLNVMLPI.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ51404.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q51404-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDTRIERDS MGELAVPATA LYGAQTQRAV NNFPVSGQRM PQAFVRALLL
60 70 80 90 100
AKAAAARANV SLQQLDAPMG EAIADTCLQL LQEDFMQHFP VDVFQTGSGT
110 120 130 140 150
SSNMNANEVV ATLASRRLGG KVNPNDHVNC GQSSNDIIPS TIHISAALEI
160 170 180 190 200
SERLLPALRH LEQTIQSKAG EVHAYVKTGR THLMDAMPVR MSQVLGGWAQ
210 220 230 240 250
QVRQAGVHIE SVLPALQQLA QGGTAVGTGI NAHPRFAERF SQELNDLTGL
260 270 280 290 300
AFRPGDDFFA LIGSQDTAVA ASGQLKTLAV TLMKLANDLR WMNSGPLAGL
310 320 330 340 350
GEIELEALQP GSSIMPGKVN PVIPEATAMV AAQVIGNDAA IAVAGQSGNF
360 370 380 390 400
ELNVMLPLVA DNLLHSIQLL ANVSRLLADK AIASFKVNQG KLSEALARNP
410 420 430 440 450
ILVTALNPII GYQKAAEIAK QAYREGRPII DVALENTDLD RARLEVLLDP

EKLTAGGL
Length:458
Mass (Da):48,696
Last modified:November 1, 1996 - v1
Checksum:i48D87C8B1C76B708
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561P → S in AAB17389. (PubMed:8806672)Curated
Sequence conflicti222 – 2221G → A in AAB17389. (PubMed:8806672)Curated
Sequence conflicti331 – 3311A → G in AAB17389. (PubMed:8806672)Curated
Sequence conflicti340 – 3401Missing in AAB17389. (PubMed:8806672)Curated
Sequence conflicti362 – 3621N → T in AAB17389. (PubMed:8806672)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59458 Genomic DNA. Translation: AAB02830.1.
U72494 Genomic DNA. Translation: AAB17389.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG07858.1.
PIRiF83088.
JC4982.
RefSeqiNP_253160.1. NC_002516.2.
WP_003112741.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG07858; AAG07858; PA4470.
GeneIDi881033.
KEGGipae:PA4470.
PATRICi19843667. VBIPseAer58763_4680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59458 Genomic DNA. Translation: AAB02830.1 .
U72494 Genomic DNA. Translation: AAB17389.1 . Different initiation.
AE004091 Genomic DNA. Translation: AAG07858.1 .
PIRi F83088.
JC4982.
RefSeqi NP_253160.1. NC_002516.2.
WP_003112741.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q51404.
SMRi Q51404. Positions 5-447.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA4470.

Proteomic databases

PRIDEi Q51404.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG07858 ; AAG07858 ; PA4470 .
GeneIDi 881033.
KEGGi pae:PA4470.
PATRICi 19843667. VBIPseAer58763_4680.

Organism-specific databases

PseudoCAPi PA4470.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi Q51404.
KOi K01679.
OMAi LNVMLPI.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q51404.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFUMC1_PSEAE
AccessioniPrimary (citable) accession number: Q51404
Secondary accession number(s): P72168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3