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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR1124 IGR1123 IGR1125 IGR1122 IGR1127 IGR1126 acoB, - SMu1297 acoA, - SMu1298 acoC,yugF, - SMu1296 adhD,acoL, - SMu1299 glmM,femD, - SMu1301 clpB, - SMu1300 acrR2, - SMu1294 acoB, - SMu1297 acoA, - SMu1298 acoC,yugF, - SMu1296 adhD,acoL, - SMu1299 glmM,femD, - SMu1301 clpB, - SMu1300 acrR2, - SMu1294 acoB, - SMu1297 acoA, - SMu1298 acoC,yugF, - SMu1296 adhD,acoL, - SMu1299 glmM,femD, - SMu1301 clpB, - SMu1300 qr1, - SMu1295 acrR2, - SMu1294 qr1, - SMu1295


LANL Gene ID: SMu1299

GenBank Locus Tag: SMU.1424c

DNA Molecule Name:
1  

GenBank ID:


Gene Name:
adhD  acoL  

Definition:
dihydrolipoamide dehydrogenase

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
1354699

Gene Stop:
1353362

Gene Length:
1338

Molecular Weight*:
48655

pI*:
5.80

Net Charge*:
-8.22

EC:
1.8.1.4  

Functional Class:
Energy metabolism; Fermentation  

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

Cellular component
  GO:0005737    cytoplasm

Molecular function
  GO:0004148    dihydrolipoyl dehydrogenase activity
  GO:0016491    oxidoreductase activity
  GO:0050660    FAD binding


Pathway: pathway table
Citrate cycle (TCA cycle)
Glycine, serine and threonine metabolism
Glycolysis / Gluconeogenesis
Pyruvate metabolism

Secondary Evidence:
Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN.
Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.
Eur J Biochem. 2001 Sep;268(18):4908-17.
PMID: 11559360

Kruger,N., Oppermann,F.B., Lorenzl,H. and Steinbuchel,A.
Biochemical and molecular characterization of the Clostridium
magnum acetoin dehydrogenase enzyme system
J. Bacteriol. 176 (12), 3614-3630 (1994)
PubMed: 8206840


Comment:
For other 'aco' genes see SMu1297 (acoB);SMu1296 (acoC); SMu1298 (acoA) and SMu0113 (acoA)

For other 'adh' genes see SMu0107 (adh);SMu0113 (adhA); SMu0114 (adhB); SMu0115 (adhC); SMu0116 (adhD); SMu0131 (adhE) and SMu1698 (adhB).



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Several matches in gapped BLAST to dihydrolipoamide dehydrogenase
sequences. Residues 1-440 are 36% similar to the enzyme from B.halodurans (15613342|). Residues 3-438 are 36% similar to 15675028| from S.pyogenes





The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG0881 (4e-72).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24379827|ref|NP_721782.1|  putative dihydrolipoamide dehy...   842   0.0  
 gi|125717964|ref|YP_001035097.1|  Dihydrolipoamide dehydroge...   646   0.0  
 gi|57865799|ref|YP_189876.1|  acetoin dehydrogenase, E3 comp...   405   e-111
 gi|27467171|ref|NP_763808.1|  dihydrolipoamide dehydrogenase...   404   e-111
 gi|70725224|ref|YP_252138.1|  hypothetical protein SH0223 [S...   400   e-109
 gi|126649884|ref|ZP_01722120.1|  acetoin dehydrogenase, E3 c...   364   7e-99
 gi|70725228|ref|YP_252142.1|  hypothetical protein SH0227 [S...   345   4e-93
 gi|56964551|ref|YP_176282.1|  acetoin dehydrogenase E3 compo...   335   4e-90
 gi|15615327|ref|NP_243630.1|  dihydrolipoamide dehydrogenase...   296   3e-78
 gi|50914126|ref|YP_060098.1|  Dihydrolipoamide dehydrogenase...   294   6e-78


InterPro Summary:  InterProScan

InterPro
IPR000759
Family
Adrenodoxin reductase
PR00419 [5-27]T 1.7e-05 PR00419 ADXRDTASE[170-184]T 1.7e-05 PR00419 ADXRDTASE ADXRDTASE
InterPro
IPR000815
Family
Mercuric reductase
PR00945 [15-33]T 2e-19 PR00945 HGRDTASE[134-151]T 2e-19 PR00945 HGRDTASE[169-186]T 2e-19 PR00945 HGRDTASE[189-204]T 2e-19 PR00945 HGRDTASE[363-383]T 2e-19 PR00945 HGRDTASE HGRDTASE
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411 [5-27]T 5.7e-65 PR00411 PNDRDTASEI[37-52]T 5.7e-65 PR00411 PNDRDTASEI[133-142]T 5.7e-65 PR00411 PNDRDTASEI[169-194]T 5.7e-65 PR00411 PNDRDTASEI[250-264]T 5.7e-65 PR00411 PNDRDTASEI[291-298]T 5.7e-65 PR00411 PNDRDTASEI[327-348]T 5.7e-65 PR00411 PNDRDTASEI[392-407]T 5.7e-65 PR00411 PNDRDTASEI[414-434]T 5.7e-65 PR00411 PNDRDTASEI PNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139 [137-196]T 5e-27 PD000139 Q8DTC8_STRMU_Q8DTC8; Q8DTC8_STRMU_Q8DTC8;
PF00070 [169-257]T 2.3e-21 PF00070 Pyr_redox Pyr_redox
InterPro
IPR004099
Domain
Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30 [324-445]T 7.2e-33 G3DSA:3.30.390.30 no description no description
PF02852 [331-440]T 7.5e-39 PF02852 Pyr_redox_dim Pyr_redox_dim
InterPro
IPR006258
Family
Dihydrolipoamide dehydrogenase
TIGR01350 [3-445]T 9.6e-161 TIGR01350 lipoamide_DH: dihydrolipoamide dehydrogenas lipoamide_DH: dihydrolipoamide dehydrogenas
InterPro
IPR012999
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076 [38-48]T 8e-5 PS00076 PYRIDINE_REDOX_1 PYRIDINE_REDOX_1
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368 [5-27]T 3.8e-35 PR00368 FADPNR[133-142]T 3.8e-35 PR00368 FADPNR[169-194]T 3.8e-35 PR00368 FADPNR[250-264]T 3.8e-35 PR00368 FADPNR[291-298]T 3.8e-35 PR00368 FADPNR FADPNR
PF07992 [5-302]T 2e-66 PF07992 Pyr_redox_2 Pyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60 [2-323]T 1.1e-61 G3DSA:3.50.50.60 no description no description
PTHR22912 [7-440]T 2.3e-154 PTHR22912 DISULFIDE OXIDOREDUCTASE DISULFIDE OXIDOREDUCTASE
PTHR22912:SF20 [7-440]T 2.3e-154 PTHR22912:SF20 DIHYDROLIPOAMIDE DEHYDROGENASE-RELATED DIHYDROLIPOAMIDE DEHYDROGENASE-RELATED


COGS Summary:  COGS Search
BeTs to 11 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 9.5e-37.
    PR00368A    5-27
    PR00368B    133-142
    PR00368C    169-194
    PR00368D    250-264
    PR00368E    291-298
    PR00368A    169-191
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 4.9e-18.
    IPB000103A    5-25
    IPB000103C    135-183
    IPB000103D    251-262
    IPB000103E    286-323
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 6.6e-08.
    IPB001100    38-52
***** IPB000171 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 2.2e-07.
    IPB000171A    7-37
    IPB000171A    171-201


 ProDom Summary:  Protein Domain Search
Residues 133-197 are 40% similar to a (REDUCTASE OXIDOREDUCTASE FAD) protein domain (PD040523 which is seen in O52935_MOOTH.

Residues 24-440 are 38% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD CENTER REDOX-ACTIVE) protein domain (PD000139 which is seen in Q9KES0_BACHD.


Paralogs:  Local Blast Search
SMu1299 is paralogously related (blast p-value < 1e-3) to SMu0116,another dihydrolipoamide dehydrogenase, to SMu0762 and SMu0126, both predicted glutathione reductase,SMu1020 and SMu0693, both predicted NADH oxidases, SMu0420 and SMu0792, both predicted thioredoxin reductase (NADPH) and SMu1286, a predicted fumarate reductase.


Pfam Summary:  Pfam Search
Residues 5 to 306 (E-value = 4.9e-79) place SMu1299 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 331 to 440 (E-value = 5.1e-39) place SMu1299 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)

 Structural Feature(s):
Feature Type  Start  Stop
uncleavable  
1  
18
transmembrane  
170  
186

Top PDB Hits:
pdb|1EBD|A Chain A, Dihydrolipoamide Dehydrogenase Complexed Wi... 261 9e-071
pdb|3LAD|A Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4... 251 1e-067
pdb|1LPF|A Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4... 242 7e-065

Gene Protein Sequence:
MAKYDLLIIGAGPGGYIAAEEAARLGKKVAVVEKKDIGGTCLNVGCIPSK
AYLQHSHWLLSMQEANKYGISTNLESVDFAKLVNRKDQVVSTLQGGIHTT
FKSLKIDYYEGQAQFLKDKSFMVNGEKISGKDVILATGSHPFIPQIHGIN
SVNYLTTDSFFNLKVLPEKLVIIGGGVIAIELAFAMQPLGVNVTVIEIAP
QILLTEDKAARAIIRKKLKTMGAHIFEAAKIEEVHAQSVILEGDGAQEFD
QLLVATGRKPNTELAQEMGLKLTERGFVKVDDYYETSTPHVYAIGDLTES
YMLAHVASMEGIKAVRAICRQAQDPVDAQGVPRSLYTNPEVASFGLSEEE
AKEQGYDVLVEQLPFSFNGRAIASTETQGFVKLISERRYHQILGAVIVGE
HGTDLLQQLILLRQAEGTFDQVVDAVYAHPTISELIQEVAKRIVQ

Gene Nucleotide Sequence:  Sequence Viewer
TTGGCTAAGTATGATCTTTTAATTATTGGTGCTGGACCCGGTGGTTATAT
TGCAGCTGAAGAGGCTGCAAGATTAGGCAAAAAAGTTGCTGTCGTTGAAA
AAAAAGACATTGGCGGAACTTGTTTAAACGTTGGCTGTATTCCTTCCAAG
GCTTATCTGCAGCACAGTCATTGGTTATTATCAATGCAGGAAGCTAACAA
ATACGGCATTTCAACTAATCTTGAAAGTGTAGACTTTGCTAAGTTAGTCA
ATCGTAAAGATCAGGTTGTTTCGACTTTACAAGGAGGTATTCACACAACT
TTTAAATCTCTAAAAATTGATTATTATGAAGGCCAAGCACAATTTCTTAA
AGACAAGAGCTTTATGGTCAATGGTGAAAAGATTTCTGGGAAAGATGTTA
TTTTAGCGACTGGTAGCCATCCTTTTATTCCGCAAATTCATGGTATTAAT
TCGGTGAATTACCTAACAACAGATAGCTTTTTCAATTTAAAAGTTTTACC
AGAGAAATTGGTTATCATTGGTGGGGGTGTTATTGCGATTGAATTAGCCT
TTGCCATGCAGCCATTGGGTGTGAATGTCACTGTCATTGAAATTGCACCG
CAAATACTATTGACAGAGGATAAAGCTGCACGTGCTATTATCAGAAAGAA
ACTCAAAACAATGGGAGCTCATATTTTTGAAGCTGCTAAGATAGAAGAAG
TACATGCTCAATCAGTTATTTTAGAGGGGGATGGCGCTCAAGAATTTGAC
CAGTTGTTAGTTGCAACAGGACGTAAGCCTAATACAGAATTAGCTCAGGA
AATGGGATTAAAGCTAACAGAACGTGGTTTTGTCAAAGTTGATGATTACT
ATGAAACGTCTACTCCACATGTTTATGCTATCGGTGACTTGACGGAAAGT
TATATGCTAGCTCATGTTGCCAGCATGGAAGGCATCAAAGCTGTTAGAGC
TATTTGTCGTCAGGCACAGGATCCTGTTGATGCTCAAGGTGTACCGCGTT
CGCTCTACACCAATCCGGAAGTGGCTTCCTTTGGACTGAGTGAAGAGGAG
GCTAAAGAACAAGGTTATGATGTCCTCGTTGAACAATTACCATTTTCTTT
CAACGGACGGGCCATTGCATCAACAGAGACGCAAGGATTTGTTAAACTGA
TTTCGGAAAGGAGGTATCATCAAATTTTAGGGGCTGTTATTGTTGGCGAA
CATGGGACAGATTTGTTGCAACAATTGATTTTATTGAGACAGGCAGAAGG
AACTTTTGATCAAGTTGTTGATGCAGTCTATGCCCATCCGACAATTTCAG
AACTCATTCAAGAAGTTGCTAAGCGAATTGTTCAGTAA

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