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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
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 sitei100SubstrateUniRule 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:BT_2246Imported
OrganismiBartonella tribocorum (strain CIP 105476 / IBS 506)Imported
Taxonomic identifieri382640 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000001592 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

STRINGi382640.Btr_2246.

Structurei

3D structure databases

ProteinModelPortaliA9IY14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 342Lyase_1InterPro annotationAdd BLAST331
Domaini408 – 459FumaraseC_CInterPro annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 132B siteUniRule annotation4
Regioni139 – 141Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

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

Sequencei

Sequence statusi: Complete.

A9IY14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVETRQETDS FGTISVRQDR YWGAQTERSL HNFNIGTEKQ PLTIIYALSL
60 70 80 90 100
IKKAAALVNM DKGKLSPKIG KAIVTAADEV LSGAFDTHFP LSVWQTGSGT
110 120 130 140 150
QSNMNVNEVI ANHASMLLGG KLGSKKPVHP NDHVNMSQSS NDSFPTALHI
160 170 180 190 200
ATTLQTRQHL FPILEALITT FKKKEEEFAD IIKIGRTHTQ DATPLTLAQE
210 220 230 240 250
FSGYRVALEA NLRRIETALA DVQMLAQGGT AVGTGLNAPK GFDVAFAQTI
260 270 280 290 300
STLTGISFKT AHNKFEALAH HGALAHFHGS LNALAADLFK IANDIRFLGS
310 320 330 340 350
GPRSGLGELN LPENEPGSSI MPGKINPTQC EAMTMVAAQV FGNHTSVTFA
360 370 380 390 400
ASQGHFELNV YKPVIGYNVL QSITLLGDCM RSFDMHCIQG LRANRVHIHA
410 420 430 440 450
LMERSLMLVT ALAPEIGYEK AAEIAKAAHK NDTTLRTEAL KAGVSGEDYD
460
RLVDPKKMIA PQ
Length:462
Mass (Da):50,063
Last modified:February 5, 2008 - v1
Checksum:i306C28F4D3D67E0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK02278.1.
RefSeqiWP_012232345.1. NC_010161.1.

Genome annotation databases

KEGGibtr:BT_2246.
PATRICi20552308. VBIBarTri113218_2272.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK02278.1.
RefSeqiWP_012232345.1. NC_010161.1.

3D structure databases

ProteinModelPortaliA9IY14.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382640.Btr_2246.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibtr:BT_2246.
PATRICi20552308. VBIBarTri113218_2272.

Phylogenomic databases

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

Entry informationi

Entry nameiA9IY14_BART1
AccessioniPrimary (citable) accession number: A9IY14
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: November 2, 2016
This is version 60 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.