Fumarate hydratase class II - Mycobacterium marinum (strain ATCC BAA-535 / M)

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B2HT54 (B2HT54_MYCMM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 37. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Fumarate hydratase class II HAMAP-Rule MF_00743
Short name=Fumarase C HAMAP-Rule MF_00743
EC=4.2.1.2 HAMAP-Rule MF_00743

Gene names

Name:	fum EMBL ACC42775.1
Synonyms:	fumC HAMAP-Rule MF_00743
Ordered Locus Names:	MMAR_4368 EMBL ACC42775.1

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] EMBL ACC42775.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H₂O. HAMAP-Rule MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743
Subunit structure	Homotetramer By similarity. HAMAP-Rule MF_00743
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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-Rule MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. HAMAP-Rule MF_00743

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle HAMAP-Rule MF_00743
Cellular component	Cytoplasm HAMAP-Rule MF_00743
Molecular function	Lyase SAAS SAAS018951 HAMAP-Rule MF_00743
Technical term	3D-structure PDB 3QBP Complete proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

4

B site By similarity HAMAP-Rule MF_00743

Region

3

Substrate binding By similarity HAMAP-Rule MF_00743

Sites

Binding site

1

Substrate By similarity HAMAP-Rule MF_00743

Sequences

Sequence

Length

Mass (Da)

Tools

B2HT54 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: EA3DEA92B5FFD49F
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476

50,192

        10         20         30         40         50         60 
MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG LERAQIRALG 

        70         80         90        100        110        120 
LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF PIDVFQTGSG TSSNMNTNEV 

       130        140        150        160        170        180 
IASIAGANGV AVHPNDDVNM SQSSNDTFPT ATHIAATEAA VSHLIPALEI LQDALATKAL 

       190        200        210        220        230        240 
EWQSVVKSGR THLMDAVPVT LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL 

       250        260        270        280        290        300 
NAPEGFGVKV VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI 

       310        320        330        340        350        360 
RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA AVAWGGANGA 

       370        380        390        400        410        420 
FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA EHLRELAESS PSIVTPLNSA 

       430        440        450        460        470 
IGYEEAAAVA KQALKERKTI RQTVIDRGLI GDKLSLEELD RRLDVLAMAK VEATDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T. Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000854 Genomic DNA. Translation: ACC42775.1.

RefSeq

YP_001852630.1. NC_010612.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QBP	X-ray	1.85	A/B/C/D	1-474	[»]

ProteinModelPortal

ModBase

Protein-protein interaction databases

STRING

216594.MMAR_4368.

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

EnsemblBacteria

ACC42775; ACC42775; MMAR_4368.

GeneID

KEGG

PATRIC

18070061. VBIMycMar75906_4696.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

KO

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

MMAR216594:GJOB-4401-MONOMER.

UniPathway

UPA00223; UER01007.

Family and domain databases

Gene3D

1.10.275.10. 1 hit.

HAMAP

MF_00743. FumaraseC.

InterPro

IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]

Pfam

PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Other

EvolutionaryTrace

Entry information

Entry name

B2HT54_MYCMM

Accession

Primary (citable) accession number: B2HT54

Entry history

Integrated into UniProtKB/TrEMBL:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info