Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate hydratase class II

Gene

fumC

Organism
Salinispora arenicola (strain CNS-205)
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.UniRule annotation

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

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 sitei186SubstrateUniRule annotation1
Active sitei187Proton donor/acceptorUniRule annotation1
Active sitei317UniRule annotation1
Binding sitei318SubstrateUniRule annotation1
Sitei330Important for catalytic activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationSAAS annotationImported
Biological processTricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciSARE391037:G1GA7-4733-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
Alternative name(s):
Aerobic fumaraseUniRule annotation
Iron-independent fumaraseUniRule 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 annotation

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Domaini17 – 341Lyase_1InterPro annotationAdd BLAST325
Domaini407 – 465FumaraseC_CInterPro annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 105Substrate bindingUniRule annotation3
Regioni128 – 131Substrate binding (B site)UniRule annotation4
Regioni138 – 140Substrate bindingUniRule annotation3
Regioni323 – 325Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q Bacteria
COG0114 LUCA
HOGENOMiHOG000061737
KOiK01679
OMAiVSFTDNC
OrthoDBiPOG091H01XG

Family and domain databases

CDDicd01362 Fumarase_classII, 1 hit
Gene3Di1.10.275.10, 1 hit
HAMAPiMF_00743 FumaraseC, 1 hit
InterProiView protein in InterPro
IPR005677 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
PANTHERiPTHR11444 PTHR11444, 1 hit
PfamiView protein in Pfam
PF10415 FumaraseC_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SUPFAMiSSF48557 SSF48557, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

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
PATRICifig|391037.6.peg.4723

Similar proteinsi

Entry informationi

Entry nameiA8M7R1_SALAI
AccessioniPrimary (citable) accession number: A8M7R1
Entry historyiIntegrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: February 28, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health