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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR104 IGR103 IGR105 IGR107 IGR102 IGR108 IGR106 IGR101 SMu0119 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116 SMu0119 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116 SMu0119 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116


LANL Gene ID: SMu0116

GenBank Locus Tag: SMU.130

DNA Molecule Name:
1  

GenBank ID:
24378648

Gene Name:
adhD  acoL  

Definition:
dihydrolipoamide dehydrogenase

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
132644

Gene Stop:
134389

Gene Length:
1746

Molecular Weight*:
61738

pI*:
4.70

Net Charge*:
-23.14

EC:
1.8.1.4  

Functional Class:
Energy metabolism; Glycolysis/gluconeogenesis  
Energy metabolism; TCA cycle  

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

Comment:
For other 'adh' genes see SMu0107 (adh);SMu0113 (adhA); SMu0114 (adhB); SMu0115 (adhC); SMu0131 (adhE); SMu1698 (adhB) and SMu1299 (adhD).



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Several matches in gapped BLAST to dihydrolipoamide dehydrogenase
sequences. Residues 1-581 are 78% similar to the enzyme from S.pyogenes (gi15675028). Residues 1-580 are 55% similar to gi17223676 from S.pneumoniae.





The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG0881 (0.0).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24378648|ref|NP_720603.1|  putative dihydrolipoamide dehy...  1072   0.0  
 gi|55822999|ref|YP_141440.1|  acetoin/pyruvate dehydrogenase...   923   0.0  
 gi|55821073|ref|YP_139515.1|  acetoin/pyruvate dehydrogenase...   922   0.0  
 gi|94990382|ref|YP_598482.1|  Dihydrolipoamide dehydrogenase...   921   0.0  
 gi|50914126|ref|YP_060098.1|  Dihydrolipoamide dehydrogenase...   919   0.0  
 gi|139473841|ref|YP_001128557.1|  dihydrolipoamide dehydroge...   910   0.0  
 gi|19746013|ref|NP_607149.1|  putative dihydrolipoamide dehy...   910   0.0  
 gi|21910200|ref|NP_664468.1|  putative dihydrolipoamide dehy...   909   0.0  
 gi|56808318|ref|ZP_00366080.1|  COG1249: Pyruvate/2-oxogluta...   907   0.0  
 gi|94988500|ref|YP_596601.1|  dihydrolipoamide dehydrogenase...   907   0.0


InterPro Summary:  InterProScan

InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364 [3-76]T 6.699996876259569E-19 PF00364 Biotin_lipoyl Biotin_lipoyl
PS50968 [3-76]T 0.0 PS50968 BIOTINYL_LIPOYL BIOTINYL_LIPOYL
InterPro
IPR000815
Family
Mercuric reductase
PR00945 [136-154]T 4.9E-17 PR00945 HGRDTASE[257-274]T 4.9E-17 PR00945 HGRDTASE[292-309]T 4.9E-17 PR00945 HGRDTASE[312-327]T 4.9E-17 PR00945 HGRDTASE[489-509]T 4.9E-17 PR00945 HGRDTASE HGRDTASE
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411 [126-148]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[158-173]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[256-265]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[292-317]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[377-391]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[417-424]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[453-474]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[518-533]T 5.2999999999999995E-64 PR00411 PNDRDTASEI[540-560]T 5.2999999999999995E-64 PR00411 PNDRDTASEI PNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139 [260-325]T 0.0 PD000139 FAD_pyr_redox FAD_pyr_redox
PF00070 [292-384]T 8.100007343233421E-26 PF00070 Pyr_redox Pyr_redox
InterPro
IPR003016
Binding_site
2-oxo acid dehydrogenase, lipoyl-binding site
PS00189 [27-56]T 8.0E-5 PS00189 LIPOYL LIPOYL
InterPro
IPR004099
Domain
Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30 [456-581]T 1.49999648196318E-39 G3DSA:3.30.390.30 Pyr_redox_dim Pyr_redox_dim
PF02852 [457-566]T 7.6000001111579085E-50 PF02852 Pyr_redox_dim Pyr_redox_dim
InterPro
IPR006258
Family
Dihydrolipoamide dehydrogenase
TIGR01350 [124-576]T 0.0 TIGR01350 lipoamide_DH lipoamide_DH
InterPro
IPR011053
Domain
Single hybrid motif
SSF51230 [1-98]T 2.7999999999999995E-26 SSF51230 Hybrid_motif Hybrid_motif
InterPro
IPR012999
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076 [159-169]T 8.0E-5 PS00076 PYRIDINE_REDOX_1 PYRIDINE_REDOX_1
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368 [126-148]T 9.999999999999999E-31 PR00368 FADPNR[256-265]T 9.999999999999999E-31 PR00368 FADPNR[292-317]T 9.999999999999999E-31 PR00368 FADPNR[377-391]T 9.999999999999999E-31 PR00368 FADPNR[417-424]T 9.999999999999999E-31 PR00368 FADPNR FADPNR
PF07992 [126-428]T 5.30001985225048E-55 PF07992 Pyr_redox_2 Pyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100 [4-98]T 3.30000526807179E-22 G3DSA:2.40.50.100 G3DSA:2.40.50.100 G3DSA:2.40.50.100
G3DSA:3.50.50.60 [124-449]T 3.99998544139379E-55 G3DSA:3.50.50.60 G3DSA:3.50.50.60 G3DSA:3.50.50.60
PTHR22912 [128-574]T 0.0 PTHR22912 PTHR22912 PTHR22912
PTHR22912:SF20 [128-574]T 0.0 PTHR22912:SF20 PTHR22912:SF20 PTHR22912:SF20
SSF51905 [124-418]T 1.8999999999999998E-68 SSF51905 SSF51905 SSF51905
SSF55424 [453-581]T 1.5E-39 SSF55424 SSF55424 SSF55424


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 1.8e-26.
    PR00368A    126-148
    PR00368B    256-265
    PR00368C    292-317
    PR00368D    377-391
    PR00368E    417-424
***** IPB001078 (2-Oxo acid dehydrogenase acyltransferase catalytic domain) with a combined E-value of 5.1e-15.
    IPB001078A    22-54
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 1.8e-14.
    IPB000103A    126-146
    IPB000103C    258-306
    IPB000103E    412-449
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 7.5e-14.
    IPB003016    25-59
***** IPB000171 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 8.3e-08.
    IPB000171A    128-158
    IPB000171A    294-324
***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 7.4e-06.
    IPB001100    159-173


 ProDom Summary:  Protein Domain Search
Residues 145-565 are 37% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD CENTER REDOX-ACTIVE) protein domain (PD000139 which is seen in Q9KES0_BACHD.

Residues 7-73 are 50% similar to a (BIOTIN DIHYDROLIPOAMIDE LIPOYL CARBOXYLASE TRANSFERASE) protein domain (PD000268 which is seen in Q9KES1_BACHD.


Paralogs:  Local Blast Search
SMu0116 is paralogously related (blast p-value < 1e-3) to SMu1299, another dihydrolipoamide dehydrogenase, to SMu0762, a predicted glutathione reductase, and to SMu0115, SMu0126, SMu1296, SMu1020, SMu0693, SMu0420, SMu0792, SMu0162, and SMu0331.


Pfam Summary:  Pfam Search
Residues 3 to 76 (E-value = 6e-22) place SMu0116 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 126 to 432 (E-value = 1.4e-86) place SMu0116 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)
Residues 457 to 566 (E-value = 1.8e-52) place SMu0116 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  
292  
308

Top PDB Hits:
pdb3LADA Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4... 275 7e-075
pdb1LPFA Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4... 260 3e-070
pdb1DXLA Chain A, Dihydrolipoamide Dehydrogenase Of Glycine D... 252 1e-067

Gene Protein Sequence:
MAVEIIMPKLGVDMQEGEIIEWKKQEGDEVKEGDILLEIMSDKTNMEIEA
EDSGVLLKIVKGNGQVVPVTEVIGYIGSAGETIETNAAPAASADDLKAAG
LEVPDTLGESAAPAAQKTPLADDEYDMIVVGGGPAGYYAAIRGAQLGGKV
AIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGIKIAAGRGINFASTNYTI
DMDKTVAFKDTVVKTLTSGVQGLLKANKVTIFNGLGQVNPDKTVTVGSET
IKGHNIILATGSKVSRINIPGIDSPLVLTSDDILDLREIPKSLAVMGGGV
VGIELGLVYASYGTEVTVIEMADRIIPAMDKEVSLELQKILSKKGMNIKT
SVGVAEIVEANNQLTLKLNDGSEVVAEKALLSIGRVPQLSGLENLNLELE
RGRIKVDDYQETSISGIYAPGDVNGRKMLAHAAYRMGEVAAENAIWGNVR
KANLKYTPAAVYTHPEVAMCGITEEQARQEYGNVLVGKSSFSGNGRAIAS
NEAQGFVKVVADAKYHEILGVHIIGPAAAEMINEASTIMENELTVDELLR
SIHGHPTFSEVMYEAFADVLGEAIHNPPKRR

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAGTCGAAATTATTATGCCTAAACTCGGTGTTGATATGCAGGAAGG
CGAAATCATCGAGTGGAAAAAACAAGAAGGTGATGAGGTCAAAGAAGGGG
ATATCCTCCTTGAAATCATGTCTGACAAGACCAATATGGAAATTGAAGCT
GAGGATTCAGGTGTCCTGCTCAAAATTGTTAAAGGAAATGGTCAAGTTGT
CCCTGTGACTGAGGTCATTGGTTATATTGGTTCTGCTGGTGAAACGATTG
AAACAAATGCAGCGCCAGCAGCTTCAGCTGATGATCTCAAAGCAGCGGGT
CTTGAAGTTCCTGATACTTTAGGCGAGTCAGCAGCACCAGCAGCTCAAAA
AACTCCGCTTGCTGATGATGAGTATGATATGATTGTCGTTGGTGGTGGTC
CTGCTGGTTATTATGCTGCTATTCGCGGTGCACAATTGGGCGGCAAGGTT
GCTATCGTCGAAAAATCAGAATTTGGAGGGACTTGTTTAAATAAAGGCTG
CATTCCAACTAAAACTTATCTTAAGAATGCTGAAATCCTTGATGGCATCA
AAATTGCAGCGGGTCGCGGTATTAATTTTGCTTCAACCAACTATACCATT
GACATGGACAAAACGGTTGCCTTTAAAGATACCGTTGTTAAAACATTGAC
AAGTGGGGTTCAGGGTCTTCTTAAAGCCAATAAAGTGACTATTTTCAATG
GTCTCGGTCAGGTTAATCCTGATAAGACAGTGACTGTCGGTTCGGAAACG
ATTAAAGGACATAATATTATCCTTGCAACAGGTTCAAAAGTGTCTCGTAT
TAATATTCCGGGAATTGATTCACCTCTTGTTTTAACATCGGATGATATTC
TTGATCTTCGTGAAATTCCAAAGTCACTTGCTGTTATGGGCGGTGGTGTT
GTCGGCATTGAACTCGGTCTTGTTTACGCTTCCTATGGTACAGAAGTGAC
TGTTATTGAAATGGCTGATCGCATTATTCCTGCTATGGACAAGGAAGTAT
CGCTTGAACTGCAAAAAATTCTATCCAAGAAAGGAATGAACATTAAGACT
TCTGTTGGTGTGGCTGAAATTGTTGAAGCTAACAATCAATTAACGCTGAA
ACTCAATGACGGCTCTGAAGTTGTGGCTGAAAAGGCCCTGCTTTCTATTG
GTCGTGTCCCACAATTAAGCGGTTTAGAAAATCTTAATCTGGAACTTGAA
CGCGGTCGCATCAAAGTGGACGATTATCAGGAAACCTCTATTTCAGGTAT
TTATGCCCCGGGTGATGTTAATGGAAGAAAGATGTTAGCGCATGCTGCCT
ATCGTATGGGTGAAGTAGCTGCCGAAAATGCTATCTGGGGAAATGTTCGT
AAGGCTAACCTGAAATATACACCAGCAGCTGTTTACACCCATCCAGAGGT
TGCTATGTGCGGTATTACTGAAGAACAAGCCCGTCAAGAATATGGAAACG
TCTTAGTTGGGAAATCCTCTTTTTCAGGAAATGGACGTGCGATCGCTTCT
AATGAAGCACAAGGATTTGTCAAAGTTGTCGCAGATGCTAAATACCATGA
AATTCTTGGAGTCCATATTATTGGACCAGCAGCTGCTGAGATGATTAATG
AAGCCTCAACGATTATGGAAAATGAGTTGACGGTTGATGAGCTGCTACGT
TCTATTCATGGCCATCCTACCTTCTCGGAGGTTATGTATGAAGCCTTTGC
AGACGTCCTTGGCGAAGCTATCCATAACCCGCCAAAGCGTCGTTAA

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