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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed-Annotation score: Annotation score: 3 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

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei190 – 1901Proton donor/acceptorBy similarity
Active sitei320 – 3201By similarity
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei333 – 3331Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:PMT_1485
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Fumarate hydratase class IIPRO_0000161297Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi74547.PMT1485.

Structurei

3D structure databases

ProteinModelPortaliQ7V5R2.
SMRiQ7V5R2. Positions 6-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023Substrate bindingUniRule annotation
Regioni131 – 1344B siteUniRule annotation
Regioni141 – 1433Substrate bindingUniRule annotation
Regioni189 – 1902Substrate bindingUniRule annotation
Regioni326 – 3283Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiIEKDTMG.
OrthoDBiEOG6V1M4M.

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.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7V5R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMADLMRIEH DSMGTIEVPA GVLWGAQTQR SLLNFAISTD RMPVELIHAL
60 70 80 90 100
ALIKQAAASV NCRLGVLDEV QRDQIIKAAS AVASGLHDDQ FPLRVWQTGS
110 120 130 140 150
GTHTNMNVNE VISNLASQAN DEPLGSHRPV HPNDHVNRSQ STNDAFPTAI
160 170 180 190 200
HIAAVQGITN NLLPELEQLI AAFARKSDAW SDIIKIGRTH LQDAVPLTLG
210 220 230 240 250
QEASAWRDQI ASAHSRIQSS LIELYPLPLG GTAVGTGLNA PARFGQETAA
260 270 280 290 300
QLASITGLPF SSAKNKFAVM ASHDGLVNAM AQLRMLAVAL FKISNDLRLL
310 320 330 340 350
ACGPRAGLAE LHLPENEPGS SIMPGKVNPS QCEAMAMVCL QVIGLDSAVT
360 370 380 390 400
MAGGSGHLQM NVYKPLIGFN LLHSIELLHD ACRKYRLAMV QGIEPNRIKI
410 420 430 440 450
QHDLEQSLML VTALAPEIGY DKASEIAHLA HEKGFSLREA ALKLGYVSKE
460
DFDRIVNPAL MTSARL
Length:466
Mass (Da):50,233
Last modified:October 1, 2003 - v1
Checksum:i395908D8DD84B12D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21660.1.

Genome annotation databases

EnsemblBacteriaiCAE21660; CAE21660; PMT_1485.
KEGGipmt:PMT1485.
PATRICi23011523. VBIProMar135351_1905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21660.1.

3D structure databases

ProteinModelPortaliQ7V5R2.
SMRiQ7V5R2. Positions 6-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74547.PMT1485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE21660; CAE21660; PMT_1485.
KEGGipmt:PMT1485.
PATRICi23011523. VBIProMar135351_1905.

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiIEKDTMG.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

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.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9313.

Entry informationi

Entry nameiFUMC_PROMM
AccessioniPrimary (citable) accession number: Q7V5R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 79 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

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.