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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
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 sitei119 – 1191SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciSMED366394:GJAL-1608-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:Smed_1576Imported
OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)Imported
Taxonomic identifieri366394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
Proteomesi
  • UP000001108 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

STRINGi366394.Smed_1576.

Structurei

3D structure databases

ProteinModelPortaliA6U9T7.
SMRiA6U9T7. Positions 22-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 361331Lyase_1InterPro annotationAdd
BLAST
Domaini427 – 48054FumaraseC_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1514B siteUniRule annotation
Regioni158 – 1603Substrate 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.

A6U9T7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAPRLGFM NRMMKAGITM TSTRTETDTF GPIEVASDRY WGAQAQRSLG
60 70 80 90 100
NFKIGWEKQP LAVVRALGIV KQAAARANMA LGRLDPTIGD AIVKAAQEVI
110 120 130 140 150
DGKLDDHFPL VVWQTGSGTQ SNMNANEVIS NRAIELLGGV MGSKKPVHPN
160 170 180 190 200
DHVNMSQSSN DTYPTAMHIA CAERVIHDLL PALKHLHKAL EEKVKAFQSI
210 220 230 240 250
IKIGRTHTQD ATPLTLGQEF SGYAAQVASS IKRIEMTLPG LCELAQGGTA
260 270 280 290 300
VGTGLNAPVG FAEKVAEQIA SITGIGFTSA PNKFEALAAH DSMVFSHGAI
310 320 330 340 350
NATAAALFKI ANDIRFLGSG PRSGLGELSL PENEPGSSIM PGKVNPTQCE
360 370 380 390 400
ALTQVCVQVF GNHASLTFAG SQGHFELNVY NPLMAYNYLQ SVQLLADAAV
410 420 430 440 450
SFTDNCVVGI EAREDNIKAA LDRSLMLVTA LAPKIGYDNA AKIAKTAHKN
460 470 480
GTTLRQEAVG GGYVTDEEFD AVVRPETMIG PA
Length:482
Mass (Da):51,277
Last modified:August 21, 2007 - v1
Checksum:i068F0496CCE62D1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000738 Genomic DNA. Translation: ABR60417.1.
RefSeqiWP_011975725.1. NC_009636.1.
YP_001327252.1. NC_009636.1.

Genome annotation databases

EnsemblBacteriaiABR60417; ABR60417; Smed_1576.
GeneIDi5322434.
KEGGismd:Smed_1576.
PATRICi23622151. VBISinMed134228_4714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000738 Genomic DNA. Translation: ABR60417.1.
RefSeqiWP_011975725.1. NC_009636.1.
YP_001327252.1. NC_009636.1.

3D structure databases

ProteinModelPortaliA6U9T7.
SMRiA6U9T7. Positions 22-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi366394.Smed_1576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR60417; ABR60417; Smed_1576.
GeneIDi5322434.
KEGGismd:Smed_1576.
PATRICi23622151. VBISinMed134228_4714.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciSMED366394:GJAL-1608-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. "Complete sequence of Sinorhizobium medicae WSM419 chromosome."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM419Imported.

Entry informationi

Entry nameiA6U9T7_SINMW
AccessioniPrimary (citable) accession number: A6U9T7
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: July 6, 2016
This is version 64 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.