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Q7V024 (FUMC_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:PMM1466
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length461 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
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 – 461461Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161298

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
Q7V024 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D696F9A39BF50149

FASTA46150,624
        10         20         30         40         50         60 
MTKNFRFEKD SMGQIKVPSE ALWGAQTQRS IINFSIGEEL IPIELIYSLT VIKRAAAISN 

        70         80         90        100        110        120 
FKLGLINNVK KDLIIEACTE ILDGKHDSQF PLKIWQTGSG TQTNMNINEV ISNIAALKTN 

       130        140        150        160        170        180 
SGLGSHHPIH PNDDVNKSQS TNDTFPAAIQ ISVVTQIIKK LVPSIKELTK VLDSKSNKWK 

       190        200        210        220        230        240 
DLIKIGRTHF QDAVPISLGQ EVSAWSKQLK DAEDALIISL NELCFLPLGG TAVGTGINCP 

       250        260        270        280        290        300 
KDFSKESIKS ISEYTGLFFY KSKNHFSLMA SHDRLAQVMG QIKILASALF KISNDIKILS 

       310        320        330        340        350        360 
SGPRSGIYEL IIPKNEPGSS IMPGKVNPTQ CEALSMVCTQ VMGFEYAVSI ANASGTLQMN 

       370        380        390        400        410        420 
EYKPLIGFNI LTSIKLLNHA ISNFRLKLVE GIQPNPKTIK ANLENSLMLV TALVPKIGYE 

       430        440        450        460 
KAAEIANLAF NESINLKEAT IKLGYLTANE FEDAINTNKM I 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE19925.1.
RefSeqNP_893583.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V024.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM1466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE19925; CAE19925; PMM1466.
GeneID1725618.
KEGGpmm:PMM1466.
PATRIC23034108. VBIProMar68066_1707.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAGDECARI.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-1506-MONOMER.
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.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_PROMP
AccessionPrimary (citable) accession number: Q7V024
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways