Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B2HT54

- B2HT54_MYCMM

UniProt

B2HT54 - B2HT54_MYCMM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fumarate hydratase class II

Gene

fum

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 – 1111SubstrateUniRule 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 annotation

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 UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_4368.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QBPX-ray1.85A/B/C/D1-474[»]
ProteinModelPortaliB2HT54.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB2HT54.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1364B siteUniRule annotation
Regioni143 – 1453Substrate bindingUniRule annotation

Sequence similaritiesi

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

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

        10         20         30         40         50
MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG
60 70 80 90 100
LERAQIRALG LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF
110 120 130 140 150
PIDVFQTGSG TSSNMNTNEV IASIAGANGV AVHPNDDVNM SQSSNDTFPT
160 170 180 190 200
ATHIAATEAA VSHLIPALEI LQDALATKAL EWQSVVKSGR THLMDAVPVT
210 220 230 240 250
LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL NAPEGFGVKV
260 270 280 290 300
VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI
310 320 330 340 350
RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA
360 370 380 390 400
AVAWGGANGA FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA
410 420 430 440 450
EHLRELAESS PSIVTPLNSA IGYEEAAAVA KQALKERKTI RQTVIDRGLI
460 470
GDKLSLEELD RRLDVLAMAK VEATDD
Length:476
Mass (Da):50,192
Last modified:June 10, 2008 - v1
Checksum:iEA3DEA92B5FFD49F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC42775.1 .
RefSeqi YP_001852630.1. NC_010612.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 / MImported.
  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: October 1, 2014
This is version 43 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.UniRule annotation

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3