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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR257 IGR252 IGR255 IGR254 IGR259 IGR251 IGR258 IGR253 IGR250 IGR256 HD0359 HD0358 yjjV, - HD0356 cstA, - HD0357 HD0352 HD0360 nrfC,fdoH, - HD0349 htpX, - HD0353 nrfD, - HD0350 gor, - HD0354 prfC, - HD0351 HD0359 HD0358 yjjV, - HD0356 cstA, - HD0357 HD0352 HD0360 nrfC,fdoH, - HD0349 htpX, - HD0353 nrfD, - HD0350 gor, - HD0354 prfC, - HD0351 HD0358 yjjV, - HD0356 cstA, - HD0357 HD0359 HD0352 HD0360 nrfC,fdoH, - HD0349 htpX, - HD0353 nrfD, - HD0350 gor, - HD0354 prfC, - HD0351
* Calculated from Protein Sequence

Gene ID: HD0354

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
gor  

Definition:
glutathione reductase

Gene Start:
275168

Gene Stop:
276538

Gene Length:
1371

Molecular Weight*:
49322

pI*:
6.60

Net Charge*:
-2.89

EC:
1.6.4.2  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Thioredoxin, glutaredoxin, and glutathione  

Pathway: pathway table
Glutamate metabolism
Glutathione metabolism

Secondary Evidence:
Greer,S. and Perham,R.N.
Glutathione reductase from Escherichia coli: cloning and sequence
analysis of the gene and relationship to other flavoprotein
disulfide oxidoreductases
Biochemistry 25 (9), 2736-2742 (1986)
MEDLINE: 86243410

Ermler,U. and Schulz,G.E.
The three-dimensional structure of glutathione reductase from
Escherichia coli at 3.0 A resolution
Proteins 9 (3), 174-179 (1991)
MEDLINE: 91172742

Mittl,P.R. and Schulz,G.E.
Structure of glutathione reductase from Escherichia coli at 1.86 A
resolution: comparison with the enzyme from human erythrocytes
Protein Sci. 3 (5), 799-809 (1994)
MEDLINE: 94339840


Comment:
0

Blast Summary:  PSI-Blast Search
Residues 1 to 456 are 76% ( EScore : 0.0 ) identical to sp|P43783|GSHR_HAEIN GLUTATHIONE REDUCTASE between residues 1 and 456 in [Haemophilus influenzae Rd]
Residues 1 to 456 are 69% ( EScore : 0.0 ) identical to sp|P06715|GSHR_ECOLI GLUTATHIONE REDUCTASE between residues 1 and 450 in [Escherichia coli]
Residues 1 to 456 are 68% ( EScore : 0.0 ) identical to pdb|1GES|B between residues 1 and 450
Residues 1 to 456 are 58% ( EScore : 1e-151 ) identical to dbj|BAA76640.1| (AB019579) glutathione reductase between residues 1 and 450 in [Streptococcus mutans]
Residues 1 to 456 are 58% ( EScore : 1e-148 ) identical to sp|Q60151|GSHR_STRTR GLUTATHIONE REDUCTASE between residues 1 and 450 in [Streptococcus thermophilus]
Residues 3 to 456 are 51% ( EScore : 1e-127 ) identical to dbj|BAA93433.1| (AB022189) glutathione reductase between residues 5 and 452 in [Physarum polycephalum]
Residues 3 to 456 are 49% ( EScore : 1e-120 ) identical to emb|CAA72516.1| (Y11830) glutathione reductase between residues 8 and 454 in [Onchocerca volvulus]
Residues 5 to 456 are 49% ( EScore : 1e-118 ) identical to gb|AAF37572.1|AF228703_1 mitochondrial glutathione reductase between residues 65 and 522 in [Homo sapiens]
Residues 5 to 456 are 49% ( EScore : 1e-118 ) identical to sp|P00390|GSHR_HUMAN GLUTATHIONE REDUCTASE between residues 22 and 479 in [Homo sapiens]
Residues 5 to 456 are 49% ( EScore : 1e-118 ) identical to pdb|3GRS| between residues 21 and 478

COGS Summary:  COGS Search
BeTs to 12 clades of COG1249
COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymes
Functional Class:  C
The phylogenetic pattern of COG1249 is amt-YqvCEBRH--gp--inX
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 3.4e-33.
    PR00368A    6-28
    PR00368B    140-149
    PR00368C    174-199
    PR00368D    260-274
    PR00368E    303-310
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 1.3e-11.
    IPB000103A    6-26
    IPB000103B    39-53
    IPB000103D    261-272
    IPB000103E    298-335
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 5.9e-10.
    IPB001100    39-53


ProDom Summary:  Protein Domain Search
No significant hits to the ProDom database.

Paralogs:  Local Blast Search

HD0354 is paralogously related to HD1623 (6e-43) and HD0333 (9e-08).


Pfam Summary:  Pfam Search
Residues 6 to 319 (E-value = 4.4e-89) place HD0354 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 345 to 456 (E-value = 4.6e-51) place HD0354 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

PDB Hit:
pdb|1GER|B Chain B, Glutathione Reductase (E.C.1.6.4.2) Complex... 654 0.0
pdb|1GES|B Chain B, Glutathione Reductase (E.C.1.6.4.2) Nad Mut... 638 0.0
pdb|1XAN| Human Glutathione Reductase In Complex With A Xant... 425 5e-120

Gene Protein Sequence:
MSKHYDYIAIGGGSGGIASINRAASYGKKCAIIEAKQLGGTCVNVGCVPK
KVMFYGAHIADAINHYAEDYGFDVSLKQFDFKKLVASRQAYISRIHSSYQ
QVLSKNNVDVFNGFARFVDPKTIEVHYPDGSTENLTADHILIATGGRPTI
PEVIGAEYGIDSNGIFALTELPKRVAIVGAGYIAVELAGVFNSFGVETHL
FVRQHALLRTQDPLIVDTLLAVLAQQNIKLHTQAISKQVVKNADGSLTLT
LQDGRQTEVDCLVWAIGREPTTDVINLAAAGVETNSRGFIKVDKFQNTNV
TGIYAVGDIIEGGIELTPVAVAAGRRLAERLFNNKPNEHLDYSLVPTVVF
SHPPIGTVGLTEPQAIEQYGAENVKVYTSSFTAMYTAVTQHRQPCRMKLV
CIGEQEKIVGLHGIGFGVDEMIQGFAVAIKMGAVKADFDNTVAIHPTGSE
EFVTMR$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTAAACATTATGACTATATTGCAATTGGTGGTGGAAGTGGGGGCAT
TGCTTCTATTAACCGTGCTGCAAGTTATGGTAAAAAATGTGCAATTATTG
AAGCAAAACAGTTAGGCGGTACTTGTGTTAATGTGGGGTGTGTACCTAAA
AAAGTAATGTTTTATGGTGCACATATTGCCGATGCAATTAATCATTATGC
TGAAGATTATGGCTTTGATGTGAGCCTTAAGCAATTTGATTTTAAAAAGC
TAGTGGCGAGCCGACAAGCCTATATTTCGCGGATTCATAGTTCTTACCAA
CAGGTATTATCTAAAAATAATGTGGATGTATTCAATGGTTTTGCACGTTT
TGTTGATCCTAAAACAATTGAAGTGCATTACCCAGATGGCTCGACCGAGA
ACTTGACTGCAGATCATATTTTAATTGCTACGGGTGGACGCCCAACGATT
CCTGAGGTAATCGGTGCAGAATATGGCATTGATTCGAATGGTATATTTGC
TTTAACTGAATTACCAAAGCGTGTTGCGATTGTGGGCGCGGGCTATATTG
CAGTTGAGCTAGCGGGCGTATTTAACAGTTTTGGGGTTGAAACACATTTA
TTTGTTCGTCAACACGCACTGTTACGGACTCAAGATCCATTAATTGTTGA
TACATTATTAGCCGTATTAGCACAGCAAAATATTAAATTGCATACACAAG
CGATATCAAAACAAGTCGTTAAAAATGCAGATGGATCTTTAACGCTCACG
TTACAAGATGGGCGTCAGACTGAAGTTGATTGTTTAGTGTGGGCCATTGG
TCGTGAGCCTACAACGGATGTAATAAATCTAGCCGCTGCCGGTGTTGAAA
CAAATAGCCGTGGTTTTATTAAAGTAGATAAATTCCAAAATACGAATGTC
ACGGGCATTTATGCGGTAGGCGATATTATTGAAGGTGGCATTGAACTAAC
GCCAGTAGCCGTGGCGGCTGGTCGCCGTTTAGCGGAGCGTTTATTCAATA
ACAAGCCAAATGAGCATTTAGATTATTCTCTAGTGCCAACCGTAGTGTTT
AGTCATCCTCCGATAGGCACTGTTGGGTTAACTGAACCACAAGCAATTGA
GCAGTATGGTGCAGAGAATGTTAAAGTTTATACTTCATCATTTACCGCAA
TGTACACCGCAGTTACTCAACATCGTCAACCTTGCCGAATGAAGTTGGTG
TGTATAGGCGAACAAGAAAAGATTGTTGGCTTGCATGGTATTGGCTTTGG
TGTTGATGAAATGATACAAGGCTTTGCGGTGGCGATTAAAATGGGCGCAG
TAAAGGCCGACTTTGATAATACTGTGGCTATTCATCCAACCGGCTCAGAA
GAGTTTGTAACTATGCGATAA


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