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Q7U8I1

- FUMC_SYNPX

UniProt

Q7U8I1 - FUMC_SYNPX

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Protein

Fumarate hydratase class II

Gene
fumC, SYNW0637
Organism
Synechococcus sp. (strain WH8102)
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton donor/acceptor By similarity
Active sitei319 – 3191 By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei332 – 3321Important for catalytic activity By 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 II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:SYNW0637
OrganismiSynechococcus sp. (strain WH8102)
Taxonomic identifieri84588 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001422: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 IIUniRule annotationPRO_0000161324Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi84588.SYNW0637.

Structurei

3D structure databases

ProteinModelPortaliQ7U8I1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate binding By similarity
Regioni130 – 1334B site By similarity
Regioni140 – 1423Substrate binding By similarity
Regioni188 – 1892Substrate binding By similarity
Regioni325 – 3273Substrate binding By similarity

Sequence similaritiesi

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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7U8I1-1 [UniParc]FASTAAdd to Basket

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MGQPMRQEHD SIGGVDVPAA ALWGAQTQRS LNNFAIGHQK IPAELIHALA    50
RIKQCCAAVN GRHGLLNDQQ VALIERAGQA IQTGQQDDHF PLSVWQTGSG 100
TQTNMNVNEV ISNLAAQESG ENLGSHRPLH PNDHINRSQS TNDVFPAAIH 150
VAAALQLQQE LLPELKRLIA SLDAKAVAWQ DIIKIGRTHL QDAVPLRLGD 200
EVSAWRDRLS DGAHWLTTAH QDLLALPLGG TAVGSGLNTP DRFAHEVCAE 250
LASRTGSDFQ PADNLFAVMA GHDSLVQTMA QLRRLAVTLL TIANDIRLLA 300
CGPRAGLGEL LLPANEPGSS IMPGKVNPTQ CEAMAMVCTQ VIGMDAAVAA 350
AGAGGHLQMN VYKPLIGYNL IEGIRLLQDA CRCFRLNLLT GMEADRDRIA 400
FYVERSLMLV TALTPEIGYE KACAIAQHAH RDGLTLREAA MQSGAITDER 450
FDQLIDPAAM ASPHR 465
Length:465
Mass (Da):50,057
Last modified:December 15, 2003 - v2
Checksum:iCA67233D2BEC464D
GO

Sequence cautioni

The sequence CAE07152.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX569690 Genomic DNA. Translation: CAE07152.1. Different initiation.
RefSeqiNP_896730.1. NC_005070.1.
WP_011127504.1. NC_005070.1.

Genome annotation databases

EnsemblBacteriaiCAE07152; CAE07152; SYNW0637.
GeneIDi1732420.
KEGGisyw:SYNW0637.
PATRICi23832697. VBISynSp27240_0657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX569690 Genomic DNA. Translation: CAE07152.1 . Different initiation.
RefSeqi NP_896730.1. NC_005070.1.
WP_011127504.1. NC_005070.1.

3D structure databases

ProteinModelPortali Q7U8I1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 84588.SYNW0637.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE07152 ; CAE07152 ; SYNW0637 .
GeneIDi 1732420.
KEGGi syw:SYNW0637.
PATRICi 23832697. VBISynSp27240_0657.

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.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH8102.

Entry informationi

Entry nameiFUMC_SYNPX
AccessioniPrimary (citable) accession number: Q7U8I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: September 3, 2014
This is version 69 of the entry and version 2 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.

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

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