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Q8ZEB6

- FUMC_YERPE

UniProt

Q8ZEB6 - FUMC_YERPE

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Yersinia pestis
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

BioCyciYPES214092:GKDD-2231-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
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:YPO2264, y2106, YP_2061
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000815: Chromosome, UP000001019: Chromosome, UP000002490: 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 – 465465Fumarate hydratase class IIPRO_0000161331Add
BLAST

Proteomic databases

PRIDEiQ8ZEB6.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi214092.YPO2264.

Structurei

3D structure databases

ProteinModelPortaliQ8ZEB6.
SMRiQ8ZEB6. Positions 5-460.
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.
OMAiNAHPEYH.
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.

Q8ZEB6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATTRSEKDS MGSIDVPANQ LWGAQTQRSL AHFRISQEKM PTELIHALAL
60 70 80 90 100
TKRAAAQVNM DLGLLPAERA KAIMRAADEV LDGAHPTEFP LAIWQTGSGT
110 120 130 140 150
QTNMNMNEVL ANRASELLGG ARGNNRLVHP NDDVNKSQSS NDVFPTAMHV
160 170 180 190 200
AAVMGVSEHL LPELKVLQKT LADKAEAYRD IVKIGRTHLQ DATPLTLGQE
210 220 230 240 250
ISGWAAMLSH SVRHIEATLP HLCELALGGT AVGTGLNTHP EYAVRVANEI
260 270 280 290 300
ATLTRQPFIT APNKFESLGT CDALVHGHGA LKGLAASLMK IANDVRWLSS
310 320 330 340 350
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EAMTMLCAQV MGNDVAINIG
360 370 380 390 400
GASGNFELNV FRPLVIHNFL QSVRLLADGM RGFNEHCALG IEPNRDRITQ
410 420 430 440 450
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAM ALGYLTDAEF
460
DEWVRPEDMV GSMKK
Length:465
Mass (Da):50,129
Last modified:March 1, 2002 - v1
Checksum:iACCDACBCD38851A7
GO

Sequence cautioni

The sequence AAS62274.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL20891.1.
AE009952 Genomic DNA. Translation: AAM85669.1.
AE017042 Genomic DNA. Translation: AAS62274.1. Different initiation.
PIRiAH0275.
RefSeqiNP_669418.1. NC_004088.1.
YP_008853946.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM85669; AAM85669; y2106.
AAS62274; AAS62274; YP_2061.
GeneIDi1147053.
17699570.
KEGGiype:YPO2263a.
ypk:y2106.
PATRICi18594167. VBIYerPes7843_2794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL20891.1 .
AE009952 Genomic DNA. Translation: AAM85669.1 .
AE017042 Genomic DNA. Translation: AAS62274.1 . Different initiation.
PIRi AH0275.
RefSeqi NP_669418.1. NC_004088.1.
YP_008853946.1. NC_003143.1.

3D structure databases

ProteinModelPortali Q8ZEB6.
SMRi Q8ZEB6. Positions 5-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 214092.YPO2264.

Proteomic databases

PRIDEi Q8ZEB6.

Protocols and materials databases

DNASUi 1147053.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM85669 ; AAM85669 ; y2106 .
AAS62274 ; AAS62274 ; YP_2061 .
GeneIDi 1147053.
17699570.
KEGGi ype:YPO2263a.
ypk:y2106.
PATRICi 18594167. VBIYerPes7843_2794.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci YPES214092:GKDD-2231-MONOMER.

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: CO-92 / Biovar Orientalis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KIM10+ / Biovar Mediaevalis.
  3. "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
    Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R.
    , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
    DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 91001 / Biovar Mediaevalis.

Entry informationi

Entry nameiFUMC_YERPE
AccessioniPrimary (citable) accession number: Q8ZEB6
Secondary accession number(s): Q0WEQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: October 1, 2014
This is version 96 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, Reference proteome

Documents

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

External Data

Dasty 3