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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Trichodesmium erythraeum (strain IMS101)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi: tricarboxylic 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
Binding sitei105 – 1051SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciTERY203124:GJDR-1336-MONOMER.
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:Tery_1328Imported
OrganismiTrichodesmium erythraeum (strain IMS101)Imported
Taxonomic identifieri203124 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium
Proteomesi
  • UP000008878 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi203124.Tery_1328.

Structurei

3D structure databases

ProteinModelPortaliQ116C7.
SMRiQ116C7. Positions 8-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 347331Lyase_1InterPro annotationAdd
BLAST
Domaini413 – 46654FumaraseC_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1374B siteUniRule annotation
Regioni144 – 1463Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFELNVYN.
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.

Q116C7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTESKHPKMR LERDSMGNIE VPADRYWGAQ TQRSLIYFSI GQDYIPLEVI
60 70 80 90 100
KAFAILKKAV AQTNQEFGKL PEYKTKLIIQ AAEEIIAGKL DRNFPLRVWM
110 120 130 140 150
TGSGTQCNMN INEVIANRAI EIAGGKMGSK NPIHPNDHVN MSQSSNDTFP
160 170 180 190 200
TAMHISSAVA LHKQLLPKVK KIRDALQEKS VEFDEIVKIG RTHLQDAVPL
210 220 230 240 250
TLGQEFSGYV AQLDANLQRI THTLPDLYEL AIGGTAVGTG LNTVKGFAEL
260 270 280 290 300
AAKHISEITG LPFVSAPNKF AALAAHDGIV MASGALKTLA CSLLKIANDI
310 320 330 340 350
RWLGSGPRCG FGELILPANE PGSSIMPGKV NPTQCEAMTM VATQVMGYDA
360 370 380 390 400
AITLAGAQGN FELNTYKPMM IFNLIQSINL IADSCNNFTD FLLVDLKPNR
410 420 430 440 450
KKIEFYLENS LMLVTALSPK IGYDRAAEVA HFAHEKDLTL KQACLELGYV
460
SGKEFDEIVI PENMTHPST
Length:469
Mass (Da):51,345
Last modified:August 22, 2006 - v1
Checksum:iBC870249C6AADAA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA. Translation: ABG50647.1.
RefSeqiWP_011611026.1. NC_008312.1.

Genome annotation databases

EnsemblBacteriaiABG50647; ABG50647; Tery_1328.
KEGGiter:Tery_1328.
PATRICi23986459. VBITriEry99848_1667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA. Translation: ABG50647.1.
RefSeqiWP_011611026.1. NC_008312.1.

3D structure databases

ProteinModelPortaliQ116C7.
SMRiQ116C7. Positions 8-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203124.Tery_1328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG50647; ABG50647; Tery_1328.
KEGGiter:Tery_1328.
PATRICi23986459. VBITriEry99848_1667.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFELNVYN.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciTERY203124:GJDR-1336-MONOMER.

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: IMS101Imported.

Entry informationi

Entry nameiQ116C7_TRIEI
AccessioniPrimary (citable) accession number: Q116C7
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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 one 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.