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P95331

- FUMC_MYXXD

UniProt

P95331 - FUMC_MYXXD

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Myxococcus xanthus (strain DK 1622)
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 sitei190 – 1901Proton donor/acceptorBy similarity
Active sitei320 – 3201By similarity
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei333 – 3331Important 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

BioCyciMXAN246197:GIWU-6388-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
Synonyms:fhy
Ordered Locus Names:MXAN_6439
OrganismiMyxococcus xanthus (strain DK 1622)
Taxonomic identifieri246197 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus
ProteomesiUP000002402: 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 – 466466Fumarate hydratase class IIPRO_0000161290Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi246197.MXAN_6439.

Structurei

3D structure databases

ProteinModelPortaliP95331.
SMRiP95331. Positions 6-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023Substrate bindingUniRule annotation
Regioni131 – 1344B siteUniRule annotation
Regioni141 – 1433Substrate bindingUniRule annotation
Regioni189 – 1902Substrate bindingUniRule annotation
Regioni326 – 3283Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
KOiK01679.
OMAiMESFNIH.
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.

P95331-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTKNVRTEK DTFGPIDVPA DRLWGAQTQR SLQNFAISTE RMPLALIRAL
60 70 80 90 100
VLVKKAAARV NVENGSLAKE KGEAIIRAAD EVLAGQHDAE FPLSVWQTGS
110 120 130 140 150
GTQTNMNTNE VLANRASELL GGERGERRKV HPNDDVNKGQ SSNDVFPTAM
160 170 180 190 200
SVAAVAAITE HVLPELKALR DVLAQKARAF HDVVKVGRTH LQDATPLTLG
210 220 230 240 250
QEVGGFVAQL DHAKGHLERT LPHLLELALG GTAVGTGLNA PKGYAERVAQ
260 270 280 290 300
ELAQLTGHPF VTAPNKFEAL AANDALVQAH GALKGLAAVL FKVANDVRWL
310 320 330 340 350
SSGPRSGLAE ITIPENEPGS SIMPGKVNPT QSEALTMLCA QVMGNDVAVT
360 370 380 390 400
VGGASGNFQL NVFKPLIAHN LLQSCRLLAD GMRSFRLHCA VGIEPNRPRI
410 420 430 440 450
QENLERSLML VTALNPHIGY DNAAKIAKTA HRDGTTLKET AVALGLVTPE
460
QFDQWVRPED MTGHKG
Length:466
Mass (Da):49,913
Last modified:June 1, 1998 - v2
Checksum:i9496DDD6C1690C55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013216 Genomic DNA. Translation: AAB97818.1.
CP000113 Genomic DNA. Translation: ABF86177.1.
RefSeqiYP_634563.1. NC_008095.1.

Genome annotation databases

EnsemblBacteriaiABF86177; ABF86177; MXAN_6439.
GeneIDi4105200.
KEGGimxa:MXAN_6439.
PATRICi22655381. VBIMyxXan43560_6334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013216 Genomic DNA. Translation: AAB97818.1 .
CP000113 Genomic DNA. Translation: ABF86177.1 .
RefSeqi YP_634563.1. NC_008095.1.

3D structure databases

ProteinModelPortali P95331.
SMRi P95331. Positions 6-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246197.MXAN_6439.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF86177 ; ABF86177 ; MXAN_6439 .
GeneIDi 4105200.
KEGGi mxa:MXAN_6439.
PATRICi 22655381. VBIMyxXan43560_6334.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061737.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MXAN246197:GIWU-6388-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

« Hide 'large scale' publications
  1. "Myxococcus xanthus fumarate hydratase, major proteosome subunit, and acyl-CoA oxidase genes."
    Salmi D., Creighton C., Youderian P.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DK 1622.

Entry informationi

Entry nameiFUMC_MYXXD
AccessioniPrimary (citable) accession number: P95331
Secondary accession number(s): Q1CYG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 1998
Last modified: October 1, 2014
This is version 91 of the entry and version 2 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