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Q8YB50 (FUMC_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:BMEII1051
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length463 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.

Sequence caution

The sequence AAL54293.1 differs from that shown. Reason: Erroneous initiation.

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 – 463463Fumarate hydratase class II HAMAP MF_00743
PRO_0000161261

Regions

Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity

Sites

Binding site1001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YB50 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: C2F6DD271F19B4F8

FASTA46349,624
        10         20         30         40         50         60 
MAATRTETDT FGPIDVPADR YWGAQTQRSL QNFRIGGERM PLPLVHALGV VKRAAAETNI 

        70         80         90        100        110        120 
ALGKLDPVLG QVIAVAASEV IEGKLDDHFP LVVWQTGSGT QSNMNANEVI SNRAIELLGG 

       130        140        150        160        170        180 
EMGSKKPIHP NDHVNMSQSS NDSFPTAIHI ATAVETVNRL YPALEHLTKA LKVKEEAFKD 

       190        200        210        220        230        240 
IIKIGRTHTQ DATPVTLGQE FSGYRAALEY ARHRLEQSLA DVFLLAQGGT AVGTGLNAPV 

       250        260        270        280        290        300 
GFDKGFAEAV SEITGLSFKT APNKFEALAS HGAVLNFHGS LNALAADLFK IANDIRFLGS 

       310        320        330        340        350        360 
GPRSGLGELS LPENEPGSSI MPGKVNPTQA EAMTMVATQV FGNQTAVTVA ASQGHFELNV 

       370        380        390        400        410        420 
FKPVIAYNVL QSIRLLSDTM VSFADHCVEG IEPNTARIKE LLERSLMLVT ALAPAIGYDN 

       430        440        450        460 
AARIAKTAHK NGTTLREEAL ASGLVSEEDY DRLVRAERMI APQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008918 Genomic DNA. Translation: AAL54293.1. Different initiation.
PIRAB3641.
RefSeqNP_542029.2. NC_003318.1.

3D structure databases

ProteinModelPortalQ8YB50.
SMRQ8YB50. Positions 5-463.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1198823.
GenomeReviewsGene locus BMEII1051 in contig AE008918_GR.
KEGGbme:BMEII1051.
PATRIC17856895. VBIBruMel92729_3406.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284369.
OMARIEKDTM.
PhylomeDBQ8YB50.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycBMEL224914:BMEII1051-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. 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]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00979. FumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_BRUME
AccessionPrimary (citable) accession number: Q8YB50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families