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B2HT54

- B2HT54_MYCMM

UniProt

B2HT54 - B2HT54_MYCMM

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Protein

Fumarate hydratase class II

Gene
fum, fumC, MMAR_4368
Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate By similarityUniRule annotation

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

LyaseUniRule annotationSAAS annotations

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-4401-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:fumImported
Synonyms:fumCUniRule annotation
Ordered Locus Names:MMAR_4368Imported
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)Imported
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000001190: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotationSAAS annotations

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_4368.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBPX-ray1.85A/B/C/D1-474[»]
ProteinModelPortaliB2HT54.

Miscellaneous databases

EvolutionaryTraceiB2HT54.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1364B site By similarityUniRule annotation
Regioni143 – 1453Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
KOiK01679.
OMAiENYRIES.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HT54-1 [UniParc]FASTAAdd to Basket

« Hide

MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG    50
LERAQIRALG LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF 100
PIDVFQTGSG TSSNMNTNEV IASIAGANGV AVHPNDDVNM SQSSNDTFPT 150
ATHIAATEAA VSHLIPALEI LQDALATKAL EWQSVVKSGR THLMDAVPVT 200
LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL NAPEGFGVKV 250
VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI 300
RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA 350
AVAWGGANGA FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA 400
EHLRELAESS PSIVTPLNSA IGYEEAAAVA KQALKERKTI RQTVIDRGLI 450
GDKLSLEELD RRLDVLAMAK VEATDD 476
Length:476
Mass (Da):50,192
Last modified:June 10, 2008 - v1
Checksum:iEA3DEA92B5FFD49F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000854 Genomic DNA. Translation: ACC42775.1.
RefSeqiYP_001852630.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC42775; ACC42775; MMAR_4368.
GeneIDi6228650.
KEGGimmi:MMAR_4368.
PATRICi18070061. VBIMycMar75906_4696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000854 Genomic DNA. Translation: ACC42775.1 .
RefSeqi YP_001852630.1. NC_010612.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QBP X-ray 1.85 A/B/C/D 1-474 [» ]
ProteinModelPortali B2HT54.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 216594.MMAR_4368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACC42775 ; ACC42775 ; MMAR_4368 .
GeneIDi 6228650.
KEGGi mmi:MMAR_4368.
PATRICi 18070061. VBIMycMar75906_4696.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MMAR216594:GJOB-4401-MONOMER.

Miscellaneous databases

EvolutionaryTracei B2HT54.

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.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-535 / M.
  2. "Crystal structure of fumarase Fum from Mycobacterium marinum."
    Edwards T.E., Gardberg A.S., Sankaran B.
    Submitted (JAN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-474.

Entry informationi

Entry nameiB2HT54_MYCMM
AccessioniPrimary (citable) accession number: B2HT54
Entry historyi
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

Similar proteinsi