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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
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 sitei101SubstrateUniRule 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:Bamb_0966Imported
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))Imported
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000000662 Componenti: Chromosome 1

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

STRINGi339670.Bamb_0966.

Structurei

3D structure databases

ProteinModelPortaliQ0BH48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 343Lyase_1InterPro annotationAdd BLAST331
Domaini409 – 462FumaraseC_CInterPro annotationAdd BLAST54

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni130 – 133B siteUniRule annotation4
Regioni140 – 142Substrate 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.

Q0BH48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEAVRMERD TFGEIAVPAD RLWGAQTERS LQNFRISTEK QSPELIHALA
60 70 80 90 100
IVKRAAAAVN QSLGVLADDK ARAIIDAADE IIAGKHPREF PLAVWQTGSG
110 120 130 140 150
TQTNMNLNEV IANRASELLG GERGEARKVH PNDDVNRGQS SNDVFPTAMH
160 170 180 190 200
IAAAYAIVNH LLPALRTLRT TLDAKSKAFA DIVKIGRTHL QDATPLTLGQ
210 220 230 240 250
EFSGYVAQLD QSVRHVESAL PHLYELALGG TAVGTGLNAH PEFAVRVADE
260 270 280 290 300
IGRLTKLPFV TAPSKFEVMA AADALVFAHG ALKTVAAGLM KIANDVRWLA
310 320 330 340 350
SGPRCGLGEL SIPENEPGSS IMPGKVNPTQ SEAVTMLCCQ VFGNDVAVNV
360 370 380 390 400
GGASGNFELN VFRPMIAHNV LQSVRLLADG AQSFNDHCAA GIEPNRARID
410 420 430 440 450
LLLNESLMLV TALNPHIGYD KAAQIAKKAH KEGTTLKAAA LALGYLTEAE
460
FDAWVRPEEM IGSR
Length:464
Mass (Da):49,715
Last modified:October 17, 2006 - v1
Checksum:iE8CB581C756DEA10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI86525.1.
RefSeqiWP_011656316.1. NZ_CP009798.1.

Genome annotation databases

EnsemblBacteriaiABI86525; ABI86525; Bamb_0966.
KEGGibam:Bamb_0966.
PATRICi19017480. VBIBurAmb61564_1042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI86525.1.
RefSeqiWP_011656316.1. NZ_CP009798.1.

3D structure databases

ProteinModelPortaliQ0BH48.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_0966.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI86525; ABI86525; Bamb_0966.
KEGGibam:Bamb_0966.
PATRICi19017480. VBIBurAmb61564_1042.

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 nameiQ0BH48_BURCM
AccessioniPrimary (citable) accession number: Q0BH48
Entry historyi
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 75 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.