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Q7V024 (FUMC_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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 lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm By similarity HAMAP 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. HAMAP MF_00743

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Fumarate hydratase class II HAMAP MF_00743
PRO_0000161298

Regions

Region130 – 1334B site By similarity
Region140 – 1423Substrate binding By similarity

Sites

Binding site1011Substrate 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 

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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: 12917642] [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...

Protein-protein interaction databases

STRINGQ7V024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1725618.
GenomeReviewsGene locus PMM1466 in contig BX548174_GR.
KEGGpmm:PMM1466.
NMPDRfig|59919.1.peg.1462.
PATRIC23034108. VBIProMar68066_1707.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHBG284369.
OMAEALSMVC.
PhylomeDBQ7V024.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycPMAR167540:PMM1466-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01679.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 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: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families