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Q8NRN8 (FUMC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fumarate hydratase class II
Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Synonyms:fum
Ordered Locus Names:Cgl1010, cg1145
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm By similarity.

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-Rule MF_00743

Sequence similarities

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

Sequence caution

The sequence CAF19712.1 differs from that shown. Reason: Erroneous initiation.

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: HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161272

Regions

Region104 – 1063Substrate binding By similarity
Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity
Region186 – 1872Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1871Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NRN8 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 315AF884777A39F0

FASTA47350,244
        10         20         30         40         50         60 
MSDFMTEQEF RIEHDTMGEV KVPAKALWQA QTQRAVENFP ISGRGLESAQ IRAMGLLKAA 

        70         80         90        100        110        120 
CAQVNKDSGA LDAEKADAII AAGKEIASGK HDAEFPIDVF QTGSGTSSNM NTNEVIASIA 

       130        140        150        160        170        180 
KANGVEVHPN DHVNMGQSSN DTFPTATHVA ATEAAVNDLI PGLKVLHESL AKKANEWSEV 

       190        200        210        220        230        240 
VKSGRTHLMD AVPVTLGQEF GGYARQIQLG IERVEATLPR LGELAIGGTA AGTGINTSAD 

       250        260        270        280        290        300 
FGGKVVAELI NLTDVKELKE AENHFEAQAA RDALVEFSGA MRVIAVSLYK IANDIRLMGS 

       310        320        330        340        350        360 
GPLTGLGEIR LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFS GTQGQFELNV 

       370        380        390        400        410        420 
FIPVMARNVL ESARLLANTS RVFATRLVDG IEPNEAHMKE LAESSPSIVT PLNSAIGYEA 

       430        440        450        460        470 
AAKVAKTALA EGKTIRQTVI DLGLVDGEKL TEEELDKRLD VLAMAHTERE NKF

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000036 Genomic DNA. Translation: BAB98403.1.
BX927151 Genomic DNA. Translation: CAF19712.1. Different initiation.
RefSeqNP_600233.1. NC_003450.3.
YP_225298.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NRN8.
ModBaseSearch...

Protein-protein interaction databases

STRING196627.cg1145.

2D gel databases

World-2DPAGE0001:Q8NRN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98403; BAB98403; BAB98403.
CAF19712; CAF19712; cg1145.
GeneID1018996.
3344954.
KEGGcgb:cg1145.
cgl:NCgl0967.
PATRIC21494066. VBICorGlu203724_0990.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061737.
KOK01679.
OMAKDTMGEV.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-999-MONOMER.
BRENDA4.2.1.2. 1648.
SABIO-RKQ8NRN8.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_CORGL
AccessionPrimary (citable) accession number: Q8NRN8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2002
Last modified: May 1, 2013
This is version 69 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

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