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Q9CMK1

- FUMC_PASMU

UniProt

Q9CMK1 - FUMC_PASMU

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-849-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:PM0823
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Fumarate hydratase class IIPRO_0000161294Add
BLAST

Proteomic databases

PRIDEiQ9CMK1.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272843.PM0823.

Structurei

3D structure databases

ProteinModelPortaliQ9CMK1.
SMRiQ9CMK1. Positions 4-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNAHPEYH.
OrthoDBiEOG6V1M4M.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CMK1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTFRIEKDTM GEVQVPADKY WAAQTERSRN NFKIGPEASM PKEIIEAFGY
60 70 80 90 100
LKKAAAYANH DLGVLPVEKR DLIAQACDEI LANKLDDQFP LVIWQTGSGT
110 120 130 140 150
QSNMNLNEVI SNRAHVLNGG KLGEKSIIHP NDDVNKSQSS NDTYPTAMHI
160 170 180 190 200
AAYKKVVEVT IPCVERLQKT LAQKADAFKD VVKIGRTHLM DATPLTLGQE
210 220 230 240 250
FSAYAAQLDF GLRALKNTLP HLAQLALGGT AVGTGLNTPK GYDVKVADYI
260 270 280 290 300
AKFTGLPFIT AENKFEALAT HDAVVETHGA LKQLAVSLYK IANDIRLLAS
310 320 330 340 350
GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EAMTMVCAQV LGNDTTISFA
360 370 380 390 400
GTQGHFQLNV FKPVMAANFL QSAQLLADAC VSFDEHCAVG IEPNFPRIKK
410 420 430 440 450
QLDDSLMLVT ALNTHIGYEN AAKIAKTAHK NGTTLKEEAI NLGLVTAEQF
460
DEWVRPEDMV GSLK
Length:464
Mass (Da):50,419
Last modified:June 1, 2001 - v1
Checksum:i0814F76FB379F1A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02907.1.
RefSeqiNP_245760.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02907; AAK02907; PM0823.
GeneIDi1244170.
KEGGipmu:PM0823.
PATRICi22870846. VBIPasMul88067_0833.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02907.1 .
RefSeqi NP_245760.1. NC_002663.1.

3D structure databases

ProteinModelPortali Q9CMK1.
SMRi Q9CMK1. Positions 4-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272843.PM0823.

Proteomic databases

PRIDEi Q9CMK1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK02907 ; AAK02907 ; PM0823 .
GeneIDi 1244170.
KEGGi pmu:PM0823.
PATRICi 22870846. VBIPasMul88067_0833.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi NAHPEYH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci PMUL272843:GC8W-849-MONOMER.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pm70.

Entry informationi

Entry nameiFUMC_PASMU
AccessioniPrimary (citable) accession number: Q9CMK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2001
Last modified: October 1, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3