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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR246 IGR243 IGR238 IGR241 IGR242 IGR239 IGR247 IGR236 IGR235 IGR245 IGR237 IGR244 IGR240 IGR248 ydhD, - HD0324 HD0326 exbB, - HD0329 exbD, - HD0328 HD0338 HD0343 HD0340 recR, - HD0325 engB, - HD0342 rluC, - HD0337 tonB, - HD0327 HD0339 glpE, - HD0330 kdsB,kpsU, - HD0334 trxA,ybbN, - HD0331 trxB, - HD0333 nrfA, - HD0344 ydhD, - HD0324 HD0326 exbB, - HD0329 exbD, - HD0328 HD0338 HD0343 HD0340 recR, - HD0325 engB, - HD0342 rluC, - HD0337 tonB, - HD0327 HD0339 glpE, - HD0330 kdsB,kpsU, - HD0334 trxA,ybbN, - HD0331 trxB, - HD0333 nrfA, - HD0344 HD0326 exbB, - HD0329 exbD, - HD0328 HD0338 HD0343 HD0340 recR, - HD0325 engB, - HD0342 rluC, - HD0337 tonB, - HD0327 HD0336 HD0336 ydhD, - HD0324 HD0339 glpE, - HD0330 kdsB,kpsU, - HD0334 trxA,ybbN, - HD0331 trxB, - HD0333 nrfA, - HD0344 HD0332 HD0332
* Calculated from Protein Sequence

Gene ID: HD0333

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
trxB  

Definition:
thioredoxin reductase

Gene Start:
262868

Gene Stop:
263863

Gene Length:
996

Molecular Weight*:
35447

pI*:
6.30

Net Charge*:
-5.10

EC:
1.8.1.9  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Thioredoxin, glutaredoxin, and glutathione  
Purines, pyrimidines, nucleosides, and nucleotides; 2'-Deoxyribonucleotide metabolism  

Pathway: pathway table
Pyrimidine metabolism

Secondary Evidence:
Tong Q, Yang YG, Zhang HT, Chen Y, Yang SL, Gong Y.
The Thioredoxin Reductase-deficient E.coli Mutant Enhances Expression into Solution of Recombinant Proteins Containing Cys Residues.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao
(Shanghai). 2001;33(1):30-34.
PMID: 12053185

Lee JH, Kim MS, Cho JH, Kim SC.
Enhanced expression of tandem multimers of the antimicrobial peptide buforin II in Escherichia coli by the DEAD-box protein and trxB mutant.
Appl Microbiol Biotechnol. 2002 May;58(6):790-6.
PMID: 12021800

Comment:
0

Blast Summary:  PSI-Blast Search
Residues 18 to 329 are 71% ( EScore : 1e-128 ) identical to sp|P43788|TRXB_HAEIN THIOREDOXIN REDUCTASE between residues 5 and 316 in [Haemophilus influenzae Rd]
Residues 17 to 330 are 68% ( EScore : 1e-122 ) identical to sp|P09625|TRXB_ECOLI THIOREDOXIN REDUCTASE between residues 4 and 318 in [Escherichia coli]
Residues 17 to 330 are 68% ( EScore : 1e-122 ) identical to pdb|1CL0|A between residues 3 and 317
Residues 17 to 327 are 68% ( EScore : 1e-122 ) identical to pdb|1TDE| between residues 3 and 314
Residues 17 to 330 are 67% ( EScore : 1e-121 ) identical to pdb|1TRB| between residues 3 and 317
Residues 17 to 327 are 68% ( EScore : 1e-120 ) identical to pdb|1TDF| between residues 3 and 314
Residues 16 to 327 are 58% ( EScore : 1e-103 ) identical to gb|AAF84257.1|AE003974_12 thioredoxin reductase between residues 7 and 318 in [Xylella fastidiosa]
Residues 17 to 329 are 57% ( EScore : 1e-99 ) identical to emb|CAB84765.1| (AL162756) thioredoxin reductase between residues 2 and 314 in [Neisseria meningitidis]
Residues 17 to 329 are 57% ( EScore : 7e-99 ) identical to gb|AAF41699.1| (AE002480) thioredoxin reductase between residues 2 and 314 in [Neisseria meningitidis MC58]
Residues 19 to 328 are 51% ( EScore : 9e-95 ) identical to sp|P81433|TRXB_BUCAP THIOREDOXIN REDUCTASE between residues 6 and 317 in [Buchnera aphidicola]

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 1.3e-86.
    IPB000103A    21-41
    IPB000103B    54-68
    IPB000103C    127-175
    IPB000103D    251-262
    IPB000103E    289-326
    IPB000103A    161-181
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 4.1e-32.
    PR00368A    21-43
    PR00368B    122-131
    PR00368C    161-186
    PR00368D    250-264
    PR00368E    294-301
    PR00368C    21-46


ProDom Summary:  Protein Domain Search
Residues 123-158 are 83% similar to a (REDUCTASE FLAVOPROTEIN FAD OXIDOREDUCTASE THIOREDOXIN) protein domain (PD329455) which is seen in TRXB_COXBU.

Residues 115-303 are 79% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD CENTER REDOX-ACTIVE) protein domain (PD000139) which is seen in Q9CN66_PASMU.

Residues 228-297 are 52% similar to a (THIOREDOXIN REDUCTASE OXIDOREDUCTASE) protein domain (PD332305) which is seen in TRXB_COXBU.

Residues 162-203 are 61% similar to a (OXIDOREDUCTASE THIOREDOXIN FAD) protein domain (PD345560) which is seen in TRXB_BUCAP.

Residues 253-327 are 58% similar to a (PROTEOME REDUCTASE-LIKE THIOREDOXIN) protein domain (PD232972) which is seen in Q9HHD5_HALN1.

Residues 66-320 are 27% similar to a (COMPLETE PROTEOME OXIDOREDUCTASE) protein domain (PD329335) which is seen in Q9KCS6_BACHD.



Paralogs:  Local Blast Search
HD0333 is paralogously related to HD0354 (6e-08) and HD1623 (1e-04).


Pfam Summary:  Pfam Search
Residues 21 to 310 (E-value = 9.3e-66) place HD0333 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)

PDB Hit:
pdb|1CL0|A Chain A, Crystal Structure Of Reduced Thioredoxin Re... 437 7e-124
pdb|1TDE| Thioredoxin Reductase (E.C.1.6.4.5) (Wild Type) 437 1e-123
pdb|1F6M|A Chain A, Crystal Structure Of A Complex Between Thio... 434 1e-122

Gene Protein Sequence:
MKHFRTLKVTRIKYMATKHTKLLILGSGPAGYTAAVYAARANLSPILVTG
MQQGGQLTTTDEIENWPGEYEQTTGTALMDKMLKHAEKFETEIVFDHIHH
VDLSVRPFVLTGDNHSFTCDALIIATGASAKYLGLASEEAFKGKGVSACA
TCDGFFYRNKPVAVVGGGNTAVEEALYLANIASEVHLVHRRDSFSAEKIL
LGRLAKRVEQGKIILHTDRVVDEILGDDFGVTGVRLSSTQQNLSEEIAVA
GCFIAIGHAPNTAIFEGQLALENGYIKVNSGLEGNATATSVAGVFAAGDV
MDHIYRQAITSAGTGCMAALDAERFLDAQAH$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAGCATTTCAGAACGTTAAAAGTAACAAGGATTAAGTATATGGCAAC
CAAACATACCAAACTATTGATTTTAGGCTCCGGACCAGCGGGTTATACTG
CGGCAGTTTATGCTGCACGGGCAAATTTATCGCCGATTTTAGTTACCGGA
ATGCAACAAGGTGGACAATTAACCACAACCGATGAAATTGAAAACTGGCC
CGGTGAATATGAACAGACAACAGGCACAGCATTAATGGATAAAATGTTAA
AACACGCTGAAAAATTTGAAACAGAGATTGTGTTTGATCATATTCATCAT
GTTGATTTATCGGTCCGTCCATTTGTGTTAACCGGAGATAATCATTCTTT
TACTTGCGATGCTTTGATTATTGCAACAGGTGCATCAGCTAAATACCTTG
GATTAGCTTCTGAAGAAGCGTTTAAAGGCAAGGGCGTGTCAGCTTGCGCT
ACTTGTGATGGTTTTTTTTACCGCAATAAGCCCGTTGCTGTCGTGGGTGG
CGGTAATACAGCGGTTGAAGAAGCGCTCTATCTTGCAAATATTGCTAGTG
AGGTCCATTTAGTTCATCGGCGTGATAGTTTCAGTGCTGAAAAAATTTTA
TTAGGGCGATTGGCAAAACGCGTCGAACAAGGCAAGATTATTCTGCATAC
TGATCGGGTAGTAGATGAAATATTAGGTGATGATTTTGGTGTTACTGGTG
TTCGTTTATCCTCCACGCAACAAAACTTGTCAGAAGAAATTGCGGTAGCA
GGTTGTTTTATTGCCATTGGGCATGCGCCTAATACTGCTATTTTTGAAGG
GCAGTTAGCATTAGAAAATGGCTATATTAAAGTCAATTCAGGTTTGGAAG
GGAATGCTACTGCAACCTCAGTAGCGGGTGTTTTTGCAGCAGGTGATGTA
ATGGATCATATTTATCGCCAAGCCATCACTTCTGCCGGCACAGGTTGTAT
GGCAGCGTTAGATGCTGAGCGCTTTTTAGATGCGCAAGCGCACTAA


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