Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR29 IGR24 IGR25 IGR23 IGR27 IGR21 IGR28 IGR26 IGR20 IGR22 genX, - HD0029 dcuB, - HD0025 HD0035 frdD, - HD0034 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 genX, - HD0029 dcuB, - HD0025 HD0035 frdD, - HD0034 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 genX, - HD0029 dcuB, - HD0025 HD0035 frdC, - HD0033 HD0038 frdB, - HD0032 dapF, - HD0026 lysA, - HD0036 frdA, - HD0030 hemN, - HD0037 frdD, - HD0034
* Calculated from Protein Sequence

Gene ID: HD0032

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
frdB  

Definition:
fumarate reductase iron-sulfur protein

Gene Start:
30396

Gene Stop:
31130

Gene Length:
735

Molecular Weight*:
27442

pI*:
6.80

Net Charge*:
-0.60

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.

Cole,S.T., Grundstrom,T., Jaurin,B., Robinson,J.J. and Weiner,J.H. Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli.
Eur. J. Biochem. 126 (1), 211-216 (1982)
Medline: 83027298.

Werth,M.T., Cecchini,G., Manodori,A., Ackrell,B.A., Schroder,I., Gunsalus,R.P. and Johnson,M.K.
Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.
Proc. Natl. Acad. Sci. U.S.A. 87 (22), 8965-8969 (1990)
Medline: 91062400


Comment:
From GenBank (gi:120492): 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 cofactors (binds three different iron-sulfur clusters: a 2FE-2S, a 3FE-4S and a 4FE-4S). The iron-sulfur centers are similar to those of "plant-type" 2FE-2S and "bacterial-type" 4FE-4S ferredoxins. 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
Numerous significant hits in gapped BLAST to fumarate reductase iron-sulfur proteins; e.g., residues 1-244 are 81% similar to FRDB_HAEIN [1169738], residues 1-243 are 73% similar to FRDB_ECOLI [120492], and residues 4-243 are 72% similar to FRDB_PROVU [120493].

COGS Summary:  COGS Search
BeTs to 12 clades of COG0479
COG name: Succinate dehydrogenase/fumarate reductase Fe-S protein
Functional Class:  C
The phylogenetic pattern of COG0479 is amt-yQ-CEbRhuj----inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000564 (2Fe-2S Ferredoxin) with a combined E-value of 1.5e-08.
    IPB000564A    55-73
    IPB000564B    76-85


ProDom Summary:  Protein Domain Search
Residues 146-225 are 37% similar to a (IRON-SULFUR SUCCINATE DEHYDROGENASE) protein domain (PD375410) which is seen in Q9JRX8_CHLPN.

Residues 145-220 are 47% similar to a (IRON-SULFUR PROTEOME COMPLETE REDUCTASE) protein domain (PD016240) which is seen in O29575_ARCFU.

Residues 23-142 are 76% similar to a (IRON-SULFUR DEHYDROGENASE SUCCINATE) protein domain (PD001472) which is seen in Q9CP57_PASMU.

Residues 182-228 are 82% similar to a (IRON-SULFUR DEHYDROGENASE SUCCINATE) protein domain (PD000788) which is seen in Q9CP57_PASMU.



Paralogs:  Local Blast Search


HD0032 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
No significant hits to the Pfam 11.0 database

PDB Hit:
pdb|1FUM|B Chain B, Structure Of The E. Coli Fumarate Reductase... 385 3e-108
pdb|1QLA|B Chain B, Respiratory Complex Ii-Like Fumarate Reduct... 127 1e-030

Gene Protein Sequence:
MATLSKMTIEVLRYNPEIDCEPHLDKYEVPFDSQTSLLDALGYIKDELEP
ELSYRWSCRMAICGSCGMMVNGKPKLACKTFLRDYSGFMRIEPLANFPIE
RDLVVDLSHFIDSIEAIKPYVIDNKTPEGQRAKQTPAQLEKYRQFSMCIN
CGLCYAACPQFGLNPEFIGPAAITLAHRYNLDNRDNGVEQRMKLLNSKNG
VWSCTFVGYCSEVCPKHVGPASAINQGKLESAKDYVISMLKPKG$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAACTTTAAGTAAAATGACTATTGAAGTGCTTCGTTATAATCCAGA
AATAGATTGCGAACCACATTTAGATAAATATGAAGTGCCTTTTGATAGCC
AAACGTCATTATTAGATGCGCTTGGTTATATTAAAGATGAACTTGAGCCA
GAGCTTTCTTATCGTTGGTCTTGTCGAATGGCAATTTGTGGATCTTGCGG
TATGATGGTAAATGGCAAACCTAAATTAGCGTGTAAAACATTCTTACGTG
ACTATAGTGGTTTTATGCGGATTGAACCGTTAGCTAACTTCCCAATTGAG
CGTGATTTAGTGGTTGATTTAAGCCATTTTATTGACTCAATTGAAGCGAT
TAAGCCTTACGTGATTGATAATAAAACACCGGAAGGTCAGCGCGCTAAAC
AAACTCCGGCGCAATTAGAAAAATACCGTCAATTTTCAATGTGTATTAAT
TGTGGCTTATGTTATGCCGCTTGCCCGCAATTTGGTTTGAATCCAGAGTT
TATTGGTCCTGCTGCAATCACTTTAGCGCACCGTTATAACTTAGATAATC
GTGATAATGGCGTTGAGCAAAGAATGAAACTGCTTAACTCAAAAAATGGT
GTTTGGAGTTGTACTTTCGTGGGGTATTGTTCAGAAGTGTGTCCAAAACA
TGTAGGGCCTGCTTCTGCGATTAACCAAGGCAAATTAGAAAGTGCCAAAG
ATTACGTGATCTCAATGTTAAAACCGAAAGGCTAG


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy