Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q55674 (FUMC_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Ordered Locus Names:slr0018
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00743.

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161325

Regions

Region99 – 1013Substrate binding By similarity
Region130 – 1334B site By similarity
Region140 – 1423Substrate binding By similarity
Region188 – 1892Substrate binding By similarity
Region325 – 3273Substrate binding By similarity

Sites

Active site1891Proton donor/acceptor By similarity
Active site3191 By similarity
Binding site3201Substrate By similarity
Site3321Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55674 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7C46A68EA26233C7

FASTA46649,687
        10         20         30         40         50         60 
MVNSHRLETD SMGSLEVQAD RLWGAQTQRS LMFFDIGSDV MPPDLIRAFA ILKKAAAITN 

        70         80         90        100        110        120 
QDLGKLPADK AELIITAADE IIAGQWLDHF PLRIWQTGSG TQTNMNVNEV IANRAIAICG 

       130        140        150        160        170        180 
GELGSKNPIH PNDHVNMSQS SNDTFPTAMH IAAVAGLQTK LIPSLQALRD SLNEKAECFA 

       190        200        210        220        230        240 
GITKIGRTHL MDAVPLTLGQ EFSGYVAQLD QGLTQINYCL PGLLELALGG TAVGTGLNSH 

       250        260        270        280        290        300 
PQFAKKVAEE IAQLTGYTFI SAPNKFAALA GHEAIAFASG VLKSIAASLM KIANDLRWMG 

       310        320        330        340        350        360 
SGPRCGLGEL ALPANEPGSS IMPGKVNPTQ CEAMTMVCVQ VMGNDATIGF AASQGNFELN 

       370        380        390        400        410        420 
VFKPVIIHNF LHSLHLLSDA CASFRQHLVV GLQVNESKVK DFLDTSLMLV TALNPHIGYD 

       430        440        450        460 
NAALVAKTAF AQGITLKQAA VDLGLLTPAQ FDAWVVPEQM IAPIAD 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10200.1.
PIRS76348.
RefSeqNP_442130.1. NC_000911.1.
YP_005652188.1. NC_017277.1.
YP_007452007.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55674.
SMRQ55674. Positions 6-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ55674. 1 interaction.
STRING1148.slr0018.

Proteomic databases

PaxDbQ55674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10200; BAA10200; BAA10200.
GeneID12253405.
14617681.
952663.
KEGGsyn:slr0018.
syy:SYNGTS_2235.
syz:MYO_122590.
PATRIC23841868. VBISynSp132158_2478.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
PhylomeDBQ55674.
ProtClustDBPRK00485.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. 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]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_SYNY3
AccessionPrimary (citable) accession number: Q55674
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways