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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Acaryochloris marina (strain MBIC 11017)
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 sitei97SubstrateUniRule annotation1

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

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:AM1_1394Imported
OrganismiAcaryochloris marina (strain MBIC 11017)Imported
Taxonomic identifieri329726 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesAcaryochloridaceaeAcaryochloris
Proteomesi
  • UP000000268 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

STRINGi329726.AM1_1394.

Structurei

3D structure databases

ProteinModelPortaliB0C6K4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 339Lyase_1InterPro annotationAdd BLAST331
Domaini405 – 458FumaraseC_CInterPro annotationAdd BLAST54

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 129B siteUniRule annotation4
Regioni136 – 138Substrate 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.
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.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B0C6K4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIETDSMGS VEVPSDCYWG AQTQRSLKYF AIGDDKMPRA MIRALGLVKQ
60 70 80 90 100
AAAKVNLTLD RLSPEVANLI VEAATEVVNG RWDDQFPLRV WQTGSGTQSN
110 120 130 140 150
MNANEVIANR AIELANGQLG SKDPCHPNDH VNLSQSSNDV FPTAMHIAAL
160 170 180 190 200
EQLVHQLIPQ VTDLRDALGT KAGEFDGIVK IGRTHLMDAV PLTLGQEFSG
210 220 230 240 250
YVAQLEQNLT RLQHTLPHLY ELVLGGTAVG TGLNTHPEFA KRVADQIAEL
260 270 280 290 300
TGLPFVTAPN KFAGLAAHDA LVMTSGALKT LACSLVKIAN DLRWMASGPR
310 320 330 340 350
CGLGELSLPA NEPGSSIMPG KVNPTQCEAL TMVCAQVIGN DTAISFAGSQ
360 370 380 390 400
GNLELNVFKP VIIHNLLHSI RILSDACDAF KTYLVVGVQP NLSQIETYLN
410 420 430 440 450
QSLMLVTALT PQIGYDRAAQ VAKQAYQTGQ TLRETCVALG FLTAEEFDQS
460
VQPVQMTHPW DSNI
Length:464
Mass (Da):50,132
Last modified:February 26, 2008 - v1
Checksum:i9B596CA92AEA233A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000828 Genomic DNA. Translation: ABW26425.1.
RefSeqiWP_012161957.1. NC_009925.1.

Genome annotation databases

EnsemblBacteriaiABW26425; ABW26425; AM1_1394.
KEGGiamr:AM1_1394.
PATRICi20617196. VBIAcaMar40141_1243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000828 Genomic DNA. Translation: ABW26425.1.
RefSeqiWP_012161957.1. NC_009925.1.

3D structure databases

ProteinModelPortaliB0C6K4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi329726.AM1_1394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABW26425; ABW26425; AM1_1394.
KEGGiamr:AM1_1394.
PATRICi20617196. VBIAcaMar40141_1243.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
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.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiB0C6K4_ACAM1
AccessioniPrimary (citable) accession number: B0C6K4
Entry historyi
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 65 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.