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Q8Z6R6

- FUMC_SALTI

UniProt

Q8Z6R6 - FUMC_SALTI

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Salmonella typhi
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

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:STY1653, t1337
OrganismiSalmonella typhi
Taxonomic identifieri90370 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000000541: Chromosome, UP000002670: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Fumarate hydratase class IIPRO_0000161308Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi220341.STY1653.

Structurei

3D structure databases

ProteinModelPortaliQ8Z6R6.
SMRiQ8Z6R6. Positions 4-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
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.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8Z6R6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVTVRREKDS MGVIEVPADK LWGAQTQRSL EHFRISTEKM PVSLIHALAL
60 70 80 90 100
TKRAAAKVNQ DLGLLAAEKA SAIIEAADEV LAGKHADEFP LAIWQTGSGT
110 120 130 140 150
QSNMNMNEVL ANRASEILGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV
160 170 180 190 200
AALLALREHL IPQLSALTDT LRDKSHAFAD IVKIGRTHLQ DATPLTLGQE
210 220 230 240 250
ISGWVAMLEH NLRHIEHSLP HVAELALGGT AVGTGLNTHP EYARRVAEEL
260 270 280 290 300
ATITAAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS
310 320 330 340 350
GPRCGIGEIA IPENEPGSSI MPGKVNPTQC EAVTMLCCQV MGNDVAINMG
360 370 380 390 400
GASGNFELNV YRPMVIHNFL QTVRLLADGM ASFNQHCASG IEPNRERITQ
410 420 430 440 450
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKASAV ALGYLSDAEF
460
DAWVRPELMV GSMTPGR
Length:467
Mass (Da):50,216
Last modified:March 1, 2002 - v1
Checksum:i4D5E53A59EAE28F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL513382 Genomic DNA. Translation: CAD01898.1.
AE014613 Genomic DNA. Translation: AAO68985.1.
RefSeqiNP_456063.1. NC_003198.1.
NP_805136.1. NC_004631.1.

Genome annotation databases

EnsemblBacteriaiAAO68985; AAO68985; t1337.
CAD01898; CAD01898; CAD01898.
GeneIDi1248027.
KEGGisty:STY1653.
PATRICi18541200. VBISalEnt120419_1664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL513382 Genomic DNA. Translation: CAD01898.1 .
AE014613 Genomic DNA. Translation: AAO68985.1 .
RefSeqi NP_456063.1. NC_003198.1.
NP_805136.1. NC_004631.1.

3D structure databases

ProteinModelPortali Q8Z6R6.
SMRi Q8Z6R6. Positions 4-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 220341.STY1653.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO68985 ; AAO68985 ; t1337 .
CAD01898 ; CAD01898 ; CAD01898 .
GeneIDi 1248027.
KEGGi sty:STY1653.
PATRICi 18541200. VBISalEnt120419_1664.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi 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.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CT18.
  2. "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
    Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
    J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700931 / Ty2.

Entry informationi

Entry nameiFUMC_SALTI
AccessioniPrimary (citable) accession number: Q8Z6R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: October 1, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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 (By similarity).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3