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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
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 sitei111SubstrateUniRule 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 annotationImported
Ordered Locus Names:CMM_2233Imported
OrganismiClavibacter michiganensis subsp. michiganensis (strain NCPPB 382)Imported
Taxonomic identifieri443906 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeClavibacter
Proteomesi
  • UP000001564 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

STRINGi443906.CMM_2233.

Structurei

3D structure databases

ProteinModelPortaliA5CT78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 347Lyase_1InterPro annotationAdd BLAST325
Domaini413 – 470FumaraseC_CInterPro annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 137B siteUniRule annotation4
Regioni144 – 146Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

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.

A5CT78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIAPGSPS SADEFRIEHD TMGEVRVPRD ALYAAQTQRA VENFPISGHG
60 70 80 90 100
LEPAQIQALA RIKRAAAIVN GEMGIIDADV SAAIVAAADE VAGGSHHEHF
110 120 130 140 150
PIDVYQTGSG TSSNMNMNEV LAALATASLG TPVHPNDHVN ASQSSNDVFP
160 170 180 190 200
TSVHVAVTGA LLAELIPALE HLAEALETKA EAWKGLVKAG RTHLMDATPV
210 220 230 240 250
TFGQEFAGYA RQTRLGIERV RTALPRVAEV PLGGTATGTG INTPLGFPQK
260 270 280 290 300
VITVLADDTG LPVTEALDHF EAQGARDGLV DASGALRTLA VSLTKICNDI
310 320 330 340 350
RWMGSGPNTG LGELHIPDLQ PGSSIMPGKI NPVIPEAVLM VCARVIGNDA
360 370 380 390 400
TVAWAGASGL FELNVAIPVM GSSLLESIRI LASSTRLLAD KTVDGLRVNE
410 420 430 440 450
EHARALAESS PSIVTPLNRI IGYEAAAKIA KHSVAQKMTV REAVVDLGYV
460 470
ERGEITEEQL DAGLDVLRMT APGL
Length:474
Mass (Da):49,629
Last modified:June 12, 2007 - v1
Checksum:iA7FB70C74BFB4186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM711867 Genomic DNA. Translation: CAN02303.1.

Genome annotation databases

EnsemblBacteriaiCAN02303; CAN02303; CMM_2233.
KEGGicmi:CMM_2233.
PATRICi21455301. VBIClaMic82482_2357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM711867 Genomic DNA. Translation: CAN02303.1.

3D structure databases

ProteinModelPortaliA5CT78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi443906.CMM_2233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAN02303; CAN02303; CMM_2233.
KEGGicmi:CMM_2233.
PATRICi21455301. VBIClaMic82482_2357.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

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 nameiA5CT78_CLAM3
AccessioniPrimary (citable) accession number: A5CT78
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 63 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 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.