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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
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)DescriptionActionsGraphical viewLength
Binding sitei110SubstrateUniRule annotation1

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

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:Krad_1112Imported
OrganismiKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)Imported
Taxonomic identifieri266940 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaKineosporialesKineosporiaceaeKineococcus
Proteomesi
  • UP000001116 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi266940.Krad_1112.

Structurei

3D structure databases

ProteinModelPortaliA6W711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 346Lyase_1InterPro annotationAdd BLAST325
Domaini412 – 470FumaraseC_CInterPro annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni133 – 136B siteUniRule annotation4
Regioni143 – 145Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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.

A6W711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTDAPAPDP RAEFRIEHDT MGEVRVPAAA KYRAQTQRAV ENFPLSGTGL
60 70 80 90 100
ERAHIEALAR IKKAAALANA ELGVLAEDLA RAVADAAEEV ATGRWDAEFP
110 120 130 140 150
VDIFQTGSGT SSNMNANEVI ATLATERFGS PVHPNDHVNA SQSSNDVFPT
160 170 180 190 200
SVHVAATSAV VNELVPALRH LEASLRRKAV EWAEVVKSGR THLMDATPVT
210 220 230 240 250
LGQEFAGYAA QVKRGIERVE ATVVRVAEVP LGGTAVGTGI NTPPGFPQRV
260 270 280 290 300
IELLAADTGL PLTEAEDHFE AQGARDALVE LSGALKVVAV SVTKICNDLR
310 320 330 340 350
WMGSGPRTGL GELRLPDLQP GSSIMPGKVN PVVPEAALMV CAQVVGNDAA
360 370 380 390 400
VTWAGASGAF ELNVQIPVMA RNVLESARLL GNAAKLLADR TVDGLEADVE
410 420 430 440 450
ACRRFAESSP SIVTPLNRVI GYEAAAKVAK HAVATGSTVR EAVVALGFVE
460 470
RGEVSEEQLD TALDVMSMTH P
Length:471
Mass (Da):49,562
Last modified:August 21, 2007 - v1
Checksum:iBFC6BFF15F519CCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000750 Genomic DNA. Translation: ABS02600.1.
RefSeqiWP_012084548.1. NC_009664.2.

Genome annotation databases

EnsemblBacteriaiABS02600; ABS02600; Krad_1112.
KEGGikra:Krad_1112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000750 Genomic DNA. Translation: ABS02600.1.
RefSeqiWP_012084548.1. NC_009664.2.

3D structure databases

ProteinModelPortaliA6W711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266940.Krad_1112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS02600; ABS02600; Krad_1112.
KEGGikra:Krad_1112.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiA6W711_KINRD
AccessioniPrimary (citable) accession number: A6W711
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 66 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.