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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR664 IGR667 IGR662 IGR666 IGR663 IGR661 IGR665 SMu0764 folC, - SMu0763 ycgG, - SMu0761 SMu0765 thiI, - SMu0766 gshR,gor, - SMu0762 SMu0760 SMu0759 SMu0764 folC, - SMu0763 ycgG, - SMu0761 SMu0765 thiI, - SMu0766 gshR,gor, - SMu0762 SMu0760 SMu0759 SMu0764 folC, - SMu0763 ycgG, - SMu0761 SMu0765 thiI, - SMu0766 gshR,gor, - SMu0762 SMu0760 SMu0759


LANL Gene ID: SMu0762

GenBank Locus Tag: SMU.838

DNA Molecule Name:
1  

GenBank ID:
24379293

Gene Name:
gshR  gor  

Definition:
glutathione reductase

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
788354

Gene Stop:
789706

Gene Length:
1353

Molecular Weight*:
48967

pI*:
5.60

Net Charge*:
-12.26

EC:
1.6.4.2  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Glutathione and analogs  
Cellular processes; Detoxification  

Gene Ontology:
Biological process
  GO:0006118    electron transport
  GO:0006749    glutathione metabolic process
  GO:0045454    cell redox homeostasis

Cellular component
  GO:0005737    cytoplasm

Molecular function
  GO:0004362    glutathione-disulfide reductase activity
  GO:0016491    oxidoreductase activity
  GO:0050660    FAD binding
  GO:0050661    NADP binding


Pathway: pathway table
Glutamate metabolism
Glutathione metabolism

Secondary Evidence:
Pebay,M., Holl,A.C., Simonet,J.M. and Decaris,B.
Characterization of the gor gene of the lactic acid bacterium
Streptococcus thermophilus CNRZ368
Res. Microbiol. 146 (5), 371-383 (1995)
PubMed: 8525054

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)
PubMed: 3521741

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)
PubMed: 2006135

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)
PubMed: 8061609





Comment:
This enzyme maintains a high level of reduced glutathione in the cytosol [gi:8928150].






View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Matches in gapped BLAST to glutathione reductase:residues 1-450 are 96% similar to the previously published enzyme in S.mutans (gi4587160).

Residues 1-450 are 71% similar to glutathione reductase in S.pyogenes (gi15674854)







The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG1375 (1e-161).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24379293|ref|NP_721248.1|  glutathione reductase [Strepto...   869   0.0  
 gi|4587160|dbj|BAA76640.1|  glutathione reductase (GR) [Stre...   857   0.0  
 gi|15674854|ref|NP_269028.1|  glutathione reductase [Strepto...   677   0.0  
 gi|55820496|ref|YP_138938.1|  glutathione reductase [Strepto...   676   0.0  
 gi|116627309|ref|YP_819928.1|  Pyruvate/2-oxoglutarate dehyd...   675   0.0  
 gi|94990192|ref|YP_598292.1|  Glutathione reductase [Strepto...   675   0.0  
 gi|50913990|ref|YP_059962.1|  glutathione reductase [Strepto...   674   0.0  
 gi|94988313|ref|YP_596414.1|  glutathione reductase [Strepto...   673   0.0  
 gi|19745893|ref|NP_607029.1|  glutathione reductase [Strepto...   672   0.0  
 gi|139474006|ref|YP_001128722.1|  glutathione reductase [Str...   672   0.0


InterPro Summary:  InterProScan

InterPro
IPR000815
Family
Mercuric reductase
PR00945 [16-34]T 4.1E-10 PR00945 HGRDTASE[136-153]T 4.1E-10 PR00945 HGRDTASE[189-204]T 4.1E-10 PR00945 HGRDTASE HGRDTASE
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411 [6-28]T 4.3E-64 PR00411 PNDRDTASEI[38-53]T 4.3E-64 PR00411 PNDRDTASEI[135-144]T 4.3E-64 PR00411 PNDRDTASEI[169-194]T 4.3E-64 PR00411 PNDRDTASEI[255-269]T 4.3E-64 PR00411 PNDRDTASEI[298-305]T 4.3E-64 PR00411 PNDRDTASEI[335-356]T 4.3E-64 PR00411 PNDRDTASEI[402-417]T 4.3E-64 PR00411 PNDRDTASEI[424-444]T 4.3E-64 PR00411 PNDRDTASEI PNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139 [139-209]T 0.0 PD000139 FAD_pyr_redox FAD_pyr_redox
PF00070 [169-262]T 2.80000504261125E-29 PF00070 Pyr_redox Pyr_redox
InterPro
IPR004099
Domain
Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30 [338-450]T 1.10000150671643E-32 G3DSA:3.30.390.30 Pyr_redox_dim Pyr_redox_dim
PF02852 [339-450]T 3.2999907750333796E-48 PF02852 Pyr_redox_dim Pyr_redox_dim
InterPro
IPR006322
Family
Glutathione reductase, animal and bacterial
TIGR01421 [3-450]T 0.0 TIGR01421 gluta_reduc_1 gluta_reduc_1
InterPro
IPR012999
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076 [39-49]T 8.0E-5 PS00076 PYRIDINE_REDOX_1 PYRIDINE_REDOX_1
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368 [6-28]T 6.0E-28 PR00368 FADPNR[135-144]T 6.0E-28 PR00368 FADPNR[169-194]T 6.0E-28 PR00368 FADPNR[255-269]T 6.0E-28 PR00368 FADPNR[298-305]T 6.0E-28 PR00368 FADPNR FADPNR
PF07992 [6-308]T 1.10000150671643E-59 PF07992 Pyr_redox_2 Pyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60 [3-335]T 1.1000015067164299E-61 G3DSA:3.50.50.60 G3DSA:3.50.50.60 G3DSA:3.50.50.60
PTHR22912 [8-450]T 0.0 PTHR22912 PTHR22912 PTHR22912
PTHR22912:SF27 [8-450]T 0.0 PTHR22912:SF27 PTHR22912:SF27 PTHR22912:SF27
SSF51905 [4-299]T 1.5000000000000002E-68 SSF51905 SSF51905 SSF51905
SSF55424 [336-450]T 5.400000000000001E-33 SSF55424 SSF55424 SSF55424


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 4
Blocks Summary:  Blocks Search
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 2.2e-32.
    PR00368A    6-28
    PR00368B    135-144
    PR00368C    169-194
    PR00368D    255-269
    PR00368E    298-305
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 5.8e-10.
    IPB001100    39-53
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 2.2e-09.
    IPB000103A    6-26
    IPB000103B    39-53
    IPB000103D    256-267
    IPB000103E    293-330
***** IPB000172 (Glucose-methanol-choline (GMC) oxidoreductase) with a combined E-value of 1.9e-08.
    IPB000172A    5-32
***** IPB000171 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 2.7e-07.
    IPB000171A    8-38
    IPB000171A    171-201


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

Paralogs:  Local Blast Search
SMu0762 is paralogously related (blast p-value < 1e-3) to SMu0116, and SMu1299,both dihydrolipoamide dehydrogenases, SMu0126, a predicted glutathione reductase, SMu0420,a predicted NADH oxidase, SMu0792, a predicted thioredoxin reductase, SMu1020,a predicted H2O-forming NADH oxidase, SMu0693,a predicted NADH oxidase/alkyl hydroperoxidase reductase, SMu0331, a predicted glutamate synthase small subunit, and SMu1286, a predicted fumarate reductase.


Pfam Summary:  Pfam Search
Residues 6 to 313 (E-value = 1.5e-87) place SMu0762 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 339 to 450 (E-value = 1.9e-50) place SMu0762 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

 Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
170  
186

Top PDB Hits:
pdb1GERB Chain B, Glutathione Reductase (E.C.1.6.4.2) Complex... 577 8e-166
pdb1GESB Chain B, Glutathione Reductase (E.C.1.6.4.2) Nad Mut... 569 3e-163
pdb1XAN Human Glutathione Reductase In Complex With A Xant... 437 2e-123

Gene Protein Sequence:
MTKQYDYIVIGGGSGGIASANRAAMHGAKVILFEGKQVGGTCVNVGCVPK
KVMWYGAQVAETINNYAADYGFDVTTQAFHFDVLKQNRQAYIDRIHDSYE
RGFDSNGVERVYGYATFVDAHTVEVAGEHYTAPHILIATGGHALLPDIPG
SEYGITSDGFFELDAIPKRTAVVGAGYIAVEISGILHALGSETHLFVRRD
RPLRKFDKEIVGTLVDEMKKDGPHLHTFSVPKEVIKNTDNSLTLILENGE
EYTVDTLIWAIGRAANTKGFNLEVTGVTLDSRGFIATDAFENTNVEGLYA
LGDVNGKLELTPVAVKAGRQLSERLFNHKPQAKMDYKDVATVIFSHPVIG
SIGLSEEAALDQYGEENVTVYRSTFTSMYTAVTSHRQACKMKLVTVGEDE
KIVGLHGIGYGVDEMIQGFAVAIKMGATKADFDNTVAIHPTGSEEFVTMR


Gene Nucleotide Sequence:  Sequence Viewer
ATGACTAAACAATATGATTATATCGTTATTGGTGGTGGTTCAGGCGGGAT
TGCCTCTGCTAACCGCGCGGCTATGCATGGGGCTAAGGTGATTCTGTTTG
AAGGCAAGCAAGTCGGTGGAACCTGTGTTAATGTTGGCTGTGTTCCTAAG
AAAGTCATGTGGTATGGAGCTCAAGTAGCAGAAACCATTAATAATTATGC
AGCTGACTACGGTTTTGATGTAACAACTCAGGCCTTTCATTTCGATGTCT
TGAAGCAAAATCGTCAGGCTTATATTGATCGTATTCATGATTCTTATGAA
CGTGGTTTTGATAGCAATGGTGTTGAACGTGTTTATGGCTATGCTACTTT
TGTAGATGCTCATACAGTAGAAGTAGCTGGGGAACATTATACTGCACCGC
ATATTTTGATTGCGACGGGTGGTCATGCCTTACTGCCGGATATTCCTGGT
AGTGAGTATGGTATTACTTCAGATGGCTTCTTTGAGTTAGATGCCATTCC
TAAACGGACAGCAGTTGTTGGTGCTGGTTATATTGCTGTGGAAATTTCAG
GTATTCTGCATGCTCTTGGCAGTGAGACACATCTTTTTGTCCGTCGGGAT
CGTCCCCTTCGCAAATTTGATAAGGAAATTGTTGGAACACTTGTGGACGA
AATGAAAAAGGATGGTCCTCATCTTCATACTTTTTCAGTCCCTAAAGAAG
TGATTAAAAATACTGATAATAGTCTAACACTTATTTTGGAAAATGGTGAG
GAGTACACTGTTGATACATTGATTTGGGCAATTGGCCGTGCTGCCAATAC
AAAAGGTTTTAATCTGGAAGTGACTGGTGTCACATTAGATAGTAGAGGTT
TTATTGCGACTGATGCATTTGAAAATACTAATGTTGAAGGTTTGTATGCT
CTTGGAGATGTCAATGGAAAATTAGAATTAACACCAGTTGCTGTAAAGGC
TGGCCGTCAACTGTCTGAACGCCTTTTTAACCATAAGCCTCAGGCTAAGA
TGGATTATAAGGATGTTGCTACCGTTATTTTCAGCCATCCAGTTATTGGT
TCAATCGGCCTATCTGAAGAGGCGGCTTTAGATCAGTATGGTGAAGAAAA
TGTCACCGTTTATCGTTCAACTTTTACTTCAATGTATACGGCAGTAACCA
GTCACCGTCAAGCTTGCAAGATGAAGTTGGTAACAGTAGGTGAGGATGAA
AAGATTGTTGGTCTACATGGTATTGGTTATGGTGTTGATGAGATGATTCA
AGGTTTTGCGGTTGCTATCAAAATGGGAGCAACTAAGGCTGATTTTGACA
ATACCGTTGCCATTCACCCAACAGGTTCAGAAGAGTTTGTCACTATGCGC
TGA

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