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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR29 IGR24 IGR25 IGR23 IGR27 IGR21 IGR30 IGR28 IGR26 IGR22 genX, - HD0029 thdF, - HD0039 HD0035 frdD, - HD0034 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 genX, - HD0029 thdF, - HD0039 HD0035 frdD, - HD0034 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 genX, - HD0029 thdF, - HD0039 HD0035 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 frdD, - HD0034
* Calculated from Protein Sequence

Gene ID: HD0034

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
frdD  

Definition:
fumarate reductase 13 kD hydrophobic protein

Gene Start:
31535

Gene Stop:
31879

Gene Length:
345

Molecular Weight*:
12607

pI*:
9.40

Net Charge*:
3.37

EC:
1.3.99.1  

Functional Class:
Energy metabolism; Anaerobic respiration  

Pathway: pathway table
Butanoate metabolism
Citrate cycle (TCA cycle)
Oxidative phosphorylation
Reductive carboxylate cycle (CO2 fixation)

Secondary Evidence:
Cole,S.T.
Nucleotide sequence coding for the flavoprotein subunit the fumarate reductase of Escherichia coli.
Eur. J. Biochem. 122 (3), 479-484 (1982)
Medline: 82138876.

Blaut,M., Whittaker,K., Valdovinos,A., Ackrell,B.A., Gunsalus,R.P. and Cecchini,G.
Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin.
J. Biol. Chem. 264 (23), 13599-13604 (1989)
Medline: 89340438.

Schroder,I., Gunsalus,R.P., Ackrell,B.A., Cochran,B. and Cecchini,G.
Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis.
J. Biol. Chem. 266 (21), 13572-13579 (1991)
Medline: 91310624.

Iverson,T.M., Luna-Chavez,C., Cecchini,G. and Rees,D.C.
Structure of the Escherichia coli fumarate reductase respiratory complex.
Science 284 (5422), 1961-1966 (1999)
Medline: 99301923


Comment:
From GenBank (gi:1169739): This hydrophobic component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
From GenBank (gi:120489): In E. coli, two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth and the succinate dehydrogenase is used in aerobic growth. Catalytic activity of this protein in E. coli is: succinate + acceptor = fumarate + reduced acceptor, requiring FAD (covalently linked) as a cofactor. Fumerate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein (HD0030), an iron-sulfur protein (see HD0032), and two hydrophobic anchor proteins (see HD0033 and HD0034).

Blast Summary:  PSI-Blast Search
Several significant hits in gapped BLAST to fumarate reductase 13 kD hydrophobic proteins; residues 1-114 are 58% similar to FRDD_HAEIN [1169740], residues 1-114 are 36% similar to FRDD_ECOLI [120498], and residues 4-114 are 37% similar to FRDD_PROVU [120499].

COGS Summary:  COGS Search
No hits to the COGs database.

Blocks Summary:  Blocks Search
***** IPB003418 (Fumarate reductase subunit D) with a combined E-value of 1.1e-51.
    IPB003418A    6-43
    IPB003418B    70-98


ProDom Summary:  Protein Domain Search
Residues 6-114 are 59% similar to a (HYDROPHOBIC REDUCTASE FUMARATE) protein domain (PD015693) which is seen in FRDD_HAEIN.



Paralogs:  Local Blast Search


HD0034 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 2 to 113 (E-value = 3.7e-58) place HD0034 in the Fumarate_red_D family which is described as Fumarate reductase subunit D (PF02313)

PDB Hit:
pdb|1FUM|D Chain D, Structure Of The E. Coli Fumarate Reductase... 99 2e-022
pdb|1FUM|D Chain D, Structure Of The E. Coli Fumarate Reductase... 173 6e-045

Gene Protein Sequence:
MNKQDPKRSNEPPVWLMFSAGGTISAICFPVLILILGILLPLGLIPMDNI
IVFAHTWLGKLVILAVTIFPMWAGMHRVHHGLHDLKIHLPASGWLFYGLS
TLYSIVVLFAVIAL$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAACAAACAAGATCCAAAGCGTTCAAATGAGCCACCTGTATGGCTAAT
GTTTAGTGCAGGCGGTACTATTAGTGCAATTTGTTTTCCGGTGTTAATTT
TAATTTTAGGAATATTATTACCGCTTGGGCTGATTCCGATGGATAATATC
ATTGTGTTTGCGCATACTTGGTTAGGTAAATTAGTTATTCTAGCGGTCAC
CATTTTTCCGATGTGGGCAGGTATGCACCGCGTTCATCACGGGTTACATG
ATCTCAAAATTCATTTACCTGCATCGGGTTGGCTATTTTATGGTTTATCG
ACACTTTACTCGATCGTTGTGTTATTTGCGGTGATTGCACTTTAG


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