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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Salinispora arenicola (strain CNS-205)
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

BioCyciSARE391037:GH66-4730-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:Sare_4674Imported
OrganismiSalinispora arenicola (strain CNS-205)Imported
Taxonomic identifieri391037 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeSalinispora
Proteomesi
  • UP000001153 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

STRINGi391037.Sare_4674.

Structurei

3D structure databases

ProteinModelPortaliA8M7R1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 341325Lyase_1InterPro annotationAdd
BLAST
Domaini407 – 46559FumaraseC_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni128 – 1314B siteUniRule annotation
Regioni138 – 1403Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8M7R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNPDATGYR IERDSMGEVE VPTEALWRAQ TQRAVQNFPI SGRGIEPAQI
60 70 80 90 100
RALAQIKGAA AEVNGELGVI DANVAAAIAA AAAHVADGGY DDQFPVDVFQ
110 120 130 140 150
TGSGTSSNMN TNEVIATLAS RELGADVHPN DDVNASQSSN DVFPSSIHLA
160 170 180 190 200
ATEFVARDLL PSFAHLAQAL EAKAVEFETV VKAGRTHLMD ATPVTLGQEF
210 220 230 240 250
GGYAAQVRYG IERLESALPR LAELPLGGTA VGTGINTPLG FAARVVERLR
260 270 280 290 300
DSTGLPLTEA RNHFEAQSAR DALVETSGQL RTVAVGLYKM ANDIRWMGSG
310 320 330 340 350
PRAGLRELRI PDLQPGSSIM PGKVNPVVCE AVRQVCAQVI GNDAAVTFAG
360 370 380 390 400
SQGDFELNVM LPVMARNVLE SIKLLAASGR LLADRCVVGL VADAEVCLAY
410 420 430 440 450
AEGSPSIVTP LNRHLGYDEA ASIAKEALAK QVSIREVVVA RGHLDSGRLT
460
ETQLDEALDL LRMTHP
Length:466
Mass (Da):49,300
Last modified:December 4, 2007 - v1
Checksum:iC75CB03EFC276F99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000850 Genomic DNA. Translation: ABW00428.1.
RefSeqiWP_012184652.1. NC_009953.1.

Genome annotation databases

EnsemblBacteriaiABW00428; ABW00428; Sare_4674.
GeneIDi5704853.
KEGGisaq:Sare_4674.
PATRICi23437964. VBISalAre38676_4723.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000850 Genomic DNA. Translation: ABW00428.1.
RefSeqiWP_012184652.1. NC_009953.1.

3D structure databases

ProteinModelPortaliA8M7R1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi391037.Sare_4674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABW00428; ABW00428; Sare_4674.
GeneIDi5704853.
KEGGisaq:Sare_4674.
PATRICi23437964. VBISalAre38676_4723.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061737.
KOiK01679.
OMAiFELNVYN.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciSARE391037:GH66-4730-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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CNS-205Imported.

Entry informationi

Entry nameiA8M7R1_SALAI
AccessioniPrimary (citable) accession number: A8M7R1
Entry historyi
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: July 6, 2016
This is version 51 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.