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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0489 IGR0485 IGR0486 IGR0487 IGR0490 IGR0482 IGR0481 IGR0491 IGR0483 IGR0484 IGR0488 NG0577 NG0587 pss, - NG0586 NG0585 uvrC, - NG0578 copA, - NG0579 rpsR, - NG0583 NG0582 rpsF, - NG0581 rplI, - NG0584 NG0588 trxB, - NG0580 NG0577 NG0587 pss, - NG0586 NG0585 uvrC, - NG0578 copA, - NG0579 rpsR, - NG0583 NG0582 rpsF, - NG0581 rplI, - NG0584 NG0588 trxB, - NG0580 NG0577 NG0587 pss, - NG0586 NG0585 uvrC, - NG0578 copA, - NG0579 rpsF, - NG0581 rplI, - NG0584 NG0588 trxB, - NG0580 NG0582 rpsR, - NG0583
* Calculated from Protein Sequence

Gene ID: NG0580

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
trxB  

Definition:
thioredoxin reductase

Gene Start:
568254

Gene Stop:
569201

Gene Length:
948

Molecular Weight*:
33641

pI*:
5.00

Net Charge*:
-7.97

EC:
1.6.4.5  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; 2'-Deoxyribonucleotide metabolism  

Pathway: pathway table
Pyrimidine metabolism

Secondary Evidence:
Waksman,G., Krishna,T.S., Williams,C.H. Jr. and Kuriyan,J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational changeduring catalysis. J. Mol. Biol. 236 (3): 800-816 (1994) Medline: 94157914.
Russel,M. and Model,P. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263 (18): 9015-9019 (1988) Medline: 88243771.
Ueshima,R., Fujita,N. and Ishihama,A. Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit. Biochem. Biophys. Res. Commun. 184 (2): 634-639 (1992) Medline: 92246944.
Kuriyan,J., Krishna,T.S., Wong,L., Guenther,B., Pahler,A.,Williams,C.H. Jr. and Model,P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 352 (6331): 172-174 (1991) Medline: 91296031.
Lennon,B.W., Williams,C.H. Jr. and Ludwig,M.L. Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of theflavin adenine dinucleotide cofactor. Protein Sci. 8 (11): 2366-2379 (1999) Medline: 20060988.

Comment:
From GenBANK (gi:136404): In E. coli, thioredoxin reductase catalyzes the reaction: NADPH + oxidized thioredoxin = NADP(+) + reduced thioredoxin, requiring a cofactor, FAD. The active site is a redox-active disulfide bond.

Oklahoma ID: NGO.580

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to thioredoxin reductases; e.g. residues 3-313 are 68% similar to gb|AAG04238.1|AE004520_1 (AE004520) thioredoxin reductase 2 of Pseudomonas aeruginosa.

Residues 1-316 are 99% similar to NMB1324 and NMA1538, both thioredoxin reductases of N.meningitidis (11253114, 11253109).

COGS Summary:  COGS Search
BeTs to 16 clades of COG0492
COG name: Thioredoxin reductase/alkyl hydroperoxide reductase
Functional Class:  O
The phylogenetic pattern of COG0492 is amtkYQVcEBrhUJgpolinX
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 6.1e-89.
    IPB000103A    6-26
    IPB000103B    39-53
    IPB000103C    112-160
    IPB000103D    235-246
    IPB000103E    274-311
    IPB000103A    146-166
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 1.8e-32.
    PR00368A    6-28
    PR00368B    107-116
    PR00368C    146-171
    PR00368D    234-248
    PR00368E    279-286
    PR00368C    6-31


ProDom Summary:  Protein Domain Search
Residues 7-304 are 63% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE REDOX-ACTIVE) protein domain (PD000139) which is seen in TRXB_ECOLI.



Paralogs:  Local Blast Search


NG0580 is paralogously related to NG0915 (dihydrolipoamide dehydrogenase E3 component) (7e-06).


Pfam Summary:  Pfam Search
Residues 6 to 295 (E-value = 6.2e-67) place NG0580 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)

Structural Feature(s):
Feature Type  Start  Stop
uncleavable N-terminal sequence N-terminal sequence  
1  
20

PDB Hit:
pdb|1TDE|1TDE THIOREDOXIN REDUCTASE (E.C.1.6.4.5) (WILD TYPE) 397.0 0e+00
pdb|1CL0|1CL0-A CRYSTAL STRUCTURE OF REDUCED THIOREDOXIN 397.0 0e+00
pdb|1TRB|1TRB THIOREDOXIN REDUCTASE (E.C.1.6.4.5) MUTANT WITH 393.0 0e+00
pdb|1F6M|1F6M-A CRYS

Gene Protein Sequence:
MSQHRKLIILGSGPAGYTAAVYAARANLNPVIITGIAQGGQLMTTTEVDN
WPADADGVQGPELMARFLAHAERFGTEIIFDQINAVDLQKRPFALKGDMG
EYTCDALIVATGASAKYLGLPSEEAFAGKGVSACATCDGFFYKNQDVAVV
GGGNTAVEEALYLANIAKTVTLIHRRSEFRAEKIMIDKLMKRVEEGKIIL
KLESNLQEVLGDDRGVNGALLKNNDGSDQQIAVSGIFIAIGHKPNTDIFK
GQLEMDEAGYLKTKGGTADNVGATNIEGVWAAGDVKDHTYRQAITSAASG
CQAALDAERWLGSQNI

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCCCAACACCGCAAACTGATTATTTTGGGTTCCGGCCCCGCCGGATA
CACCGCCGCCGTCTATGCCGCACGTGCCAATTTAAACCCCGTCATTATTA
CAGGTATCGCGCAAGGCGGGCAACTGATGACAACGACTGAAGTGGACAAC
TGGCCTGCCGATGCCGACGGCGTGCAAGGGCCGGAATTGATGGCGCGGTT
TCTCGCCCACGCCGAACGTTTCGGAACGGAAATCATTTTTGACCAAATCA
ACGCCGTCGATCTGCAAAAACGCCCGTTCGCACTCAAAGGCGATATGGGC
GAGTACACTTGCGATGCCCTGATTGTCGCCACCGGCGCGTCCGCCAAATA
CCTTGGTTTGCCGAGTGAGGAAGCGTTTGCAGGGAAAGGCGTTTCCGCCT
GCGCCACCTGCGACGGTTTCTTCTACAAAAATCAAGATGTTGCCGTAGTC
GGCGGCGGCAATACGGCAGTTGAGGAGGCACTCTACCTTGCCAATATCGC
CAAAACCGTTACGCTGATTCACCGCCGCAGCGAGTTCCGTGCTGAAAAAA
TCATGATTGACAAACTGATGAAACGCGTGGAAGAGGGCAAAATCATCCTC
AAGCTGGAAAGCAACCTGCAAGAAGTACTGGGCGACGATCGGGGCGTAAA
TGGCGCATTATTAAAAAACAACGACGGTTCTGATCAACAAATTGCCGTCA
GCGGCATCTTTATCGCCATCGGGCACAAGCCGAATACCGATATTTTCAAA
GGGCAGTTGGAAATGGACGAAGCCGGCTACCTGAAAACAAAAGGCGGCAC
GGCGGACAATGTCGGTGCAACCAATATCGAAGGCGTATGGGCGGCGGGCG
ACGTAAAAGACCATACCTACCGTCAGGCAATTACCAGCGCGGCCTCCGGC
TGTCAGGCGGCTTTGGACGCGGAACGTTGGCTGGGCAGCCAAAACATT


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