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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR104 IGR100 IGR103 IGR105 IGR107 IGR102 IGR99 IGR106 IGR101 ykoM, - SMu0111 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116 polC, - SMu0110 ykoM, - SMu0111 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116 polC, - SMu0110 ykoM, - SMu0111 SMu0112 lplA, - SMu0117 adhA,acoA, - SMu0113 adhB,acoB, - SMu0114 hipO, - SMu0118 adhC,yugF,acoC, - SMu0115 adhD,acoL, - SMu0116 polC, - SMu0110


LANL Gene ID: SMu0115

GenBank Locus Tag: SMU.129

DNA Molecule Name:
1  

GenBank ID:
24378647

Gene Name:
adhC  yugF  acoC  

Definition:
dihydrolipoamide S-acetyltransferase

Cellular Location:
Cytoplasm, Extracellular [Evidence]

Gene Start:
131203

Gene Stop:
132570

Gene Length:
1368

Molecular Weight*:
48664

pI*:
5.50

Net Charge*:
-5.80

EC:
2.3.1.12  

Functional Class:
Energy metabolism; Glycolysis/gluconeogenesis  

Gene Ontology:
Biological process
  GO:0008152    metabolic process

Molecular function
  GO:0005515    protein binding
  GO:0008415    acyltransferase activity


Pathway: pathway table
Glycolysis / Gluconeogenesis
Pyruvate metabolism

Comment:
For other 'adh' genes see SMu0107 (adh);SMu0113 (adhA); SMu0114 (adhB); SMu0116 (adhD); SMu0131 (adhE); SMu1698 (adhB) and SMu1299 (adhD).



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Several matches in gapped BLAST to dihydrolipoamide S-acetyltransferase sequences. Residues 1-455 are 75% similar to the enzyme from S.pyogenes (gi15675027) and 41% similar to the enzyme from B.halodurans (gi15613341).





The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG0880 (0.0).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24378647|ref|NP_720602.1|  dihydrolipoamide acetyltransfe...   823   0.0  
 gi|56808319|ref|ZP_00366081.1|  COG0508: Pyruvate/2-oxogluta...   627   e-178
 gi|25010951|ref|NP_735346.1|  dihydrolipoamide acetyltransfe...   624   e-177
 gi|22537043|ref|NP_687894.1|  dihydrolipoamide acetyltransfe...   623   e-177
 gi|77407949|ref|ZP_00784699.1|  acetoin dehydrogenase, thymi...   621   e-176
 gi|19746012|ref|NP_607148.1|  dihydrolipoamide acetyltransfe...   612   e-173
 gi|21910199|ref|NP_664467.1|  dihydrolipoamide acetyltransfe...   612   e-173
 gi|50914124|ref|YP_060096.1|  dihydrolipoamide acetyltransfe...   612   e-173
 gi|94988498|ref|YP_596599.1|  dihydrolipoamide acetyltransfe...   610   e-173
 gi|15675027|ref|NP_269201.1|  dihydrolipoamide acetyltransfe...   610   e-173


InterPro Summary:  InterProScan

InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364 [3-76]T 1.2999992446818299E-18 PF00364 Biotin_lipoyl Biotin_lipoyl
PS50968 [3-76]T 0.0 PS50968 BIOTINYL_LIPOYL BIOTINYL_LIPOYL
InterPro
IPR001078
Domain
Catalytic domain of components of various dehydrogenase complexes
PD001115 [375-446]T 0.0 PD001115 2Oxoacid_dh 2Oxoacid_dh
PF00198 [221-455]T 1.5000096574885398E-114 PF00198 2-oxoacid_dh 2-oxoacid_dh
InterPro
IPR003016
Binding_site
2-oxo acid dehydrogenase, lipoyl-binding site
PS00189 [27-56]T 8.0E-5 PS00189 LIPOYL LIPOYL
InterPro
IPR004167
Domain
E3 binding
PF02817 [123-159]T 1.2000011745814E-12 PF02817 E3_binding[165-201]T 1.80000149287196E-10 PF02817 E3_binding E3_binding
InterPro
IPR011053
Domain
Single hybrid motif
SSF51230 [1-98]T 2.1E-25 SSF51230 Hybrid_motif Hybrid_motif
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100 [4-81]T 5.69999708784002E-21 G3DSA:2.40.50.100 G3DSA:2.40.50.100 G3DSA:2.40.50.100
G3DSA:3.30.559.10 [210-455]T 3.99998544139379E-73 G3DSA:3.30.559.10 G3DSA:3.30.559.10 G3DSA:3.30.559.10
G3DSA:4.10.320.10 [122-162]T 6.89999963379704E-8 G3DSA:4.10.320.10 G3DSA:4.10.320.10[164-204]T 6.09999977126217E-5 G3DSA:4.10.320.10 G3DSA:4.10.320.10 G3DSA:4.10.320.10
PTHR23151 [3-158]T 7.19996395544636E-129 PTHR23151 PTHR23151[199-428]T 7.19996395544636E-129 PTHR23151 PTHR23151 PTHR23151
PTHR23151:SF19 [3-158]T 7.19996395544636E-129 PTHR23151:SF19 PTHR23151:SF19[199-428]T 7.19996395544636E-129 PTHR23151:SF19 PTHR23151:SF19 PTHR23151:SF19
SSF47005 [112-162]T 6.8E-13 SSF47005 SSF47005[163-204]T 1.7000000000000001E-9 SSF47005 SSF47005 SSF47005
SSF52777 [221-455]T 7.300000000000001E-79 SSF52777 SSF52777 SSF52777


COGS Summary:  COGS Search
BeTs to 8 clades of COG0508
COG name: Dihydrolipoamide acyltransferases
Functional Class: C
The phylogenetic pattern of COG0508 is ----Y--cEBRH--gp--INX
Number of proteins in this genome belonging to this COG is 2
Blocks Summary:  Blocks Search
***** IPB001078 (2-Oxo acid dehydrogenase acyltransferase catalytic domain) with a combined E-value of 1.7e-72.
    IPB001078A    22-54
    IPB001078B    125-155
    IPB001078C    279-300
    IPB001078D    358-400
    IPB001078E    419-455
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 4.4e-14.
    IPB003016    25-59
***** IPB000089 (Biotin / Lipoyl attachment) with a combined E-value of 1.7e-11.
    IPB000089A    320-339
    IPB000089B    374-393


 ProDom Summary:  Protein Domain Search
Residues 7-73 are 52% similar to a (BIOTIN DIHYDROLIPOAMIDE LIPOYL CARBOXYLASE TRANSFERASE) protein domain (PD000268 which is seen in Q9KES1_BACHD.

Residues 77-168 are 33% similar to a (COMPONENT TRANSFERASE PYRUVATE) protein domain (PD168210 which is seen in ODP2_ACHLA.

Residues 89-158 are 43% similar to a (TRANSFERASE DIHYDROLIPOAMIDE LIPOYL) protein domain (PD293828 which is seen in ODP2_YEAST.

Residues 77-167 are 36% similar to a (PYRUVATE PROTEOME COMPONENT TRANSFERASE) protein domain (PD394956 which is seen in Q9YBC6_AERPE.

Residues 233-455 are 42% similar to a (DIHYDROLIPOAMIDE TRANSFERASE LIPOYL DEHYDROGENASE E2) protein domain (PD001115 which is seen in Q9KES1_BACHD.


Paralogs:  Local Blast Search
SMu0115 is paralogously related (blast p-value < 1e-3) to SMu1296, a predicted dihydrolipoamide acetyltransferase, E2 component, and to SMu0116, a predicted dihydrolipoamide dehydrogenase.


Pfam Summary:  Pfam Search
Residues 3 to 76 (E-value = 1.2e-21) place SMu0115 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 123 to 159 (E-value = 8.3e-16) place SMu0115 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 165 to 201 (E-value = 1.3e-13) place SMu0115 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 221 to 455 (E-value = 4.9e-118) place SMu0115 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

 Top PDB Hits:
pdb1B5SA Chain A, Dihydrolipoyl Transacetylase (E.C.2.3.1.12)... 166 5e-042
pdb1E2O Catalytic Domain From Dihydrolipoamide Succinyltra... 141 2e-034
pdb1DPC Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catal... 109 5e-025

Gene Protein Sequence:
MAVEIIMPKLGVDMQEGEIIEWKKQEGDEVKEGEILLEIMSDKTNMEIEA
EDSGVLLKIVKGNGQVVPVTEVIGYIGQAGEVLEIADVPASTVPKENSAA
PAEKTKAMSSPTVAAAPQGKIRATPAARKAARDLGVNLNQVSGTGAKGRV
HKEDVESFKAAQPKATPLARKIAIDKGIDLASVSGTGFGGKIIKEDILNL
FEAAQPVNDVSDPAKEAAALPEGVEVIKMSAMRKAVAKSMVNSYLTAPTF
TLNYDIDMTEMIALRKKLIDPIMEKTGFKVSFTDLIGLAVVKTLMKPEHR
YLNASLINDATEIELHQFVNLGIAVGLDEGLLVPVVHGADKMSLSDFVIA
SKDVIKKAQTGKLKATEMSGSTFSITNLGMFGTKTFNPIINQPNSAILGV
GATIQTPTVVDGEIKIRPIMALCLTIDHRLVDGMNGAKFMVDLKKLMENP
FTLLI

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAGTCGAAATTATTATGCCTAAACTTGGTGTTGATATGCAGGAAGG
CGAAATCATCGAGTGGAAAAAACAAGAAGGTGATGAGGTCAAAGAAGGGG
AGATCCTCCTTGAGATTATGTCTGACAAGACCAATATGGAAATCGAAGCT
GAGGATTCAGGTGTCCTGCTTAAGATTGTTAAAGGAAATGGTCAAGTTGT
TCCTGTAACTGAGGTCATTGGTTATATTGGTCAAGCAGGTGAAGTTCTTG
AAATAGCTGATGTTCCTGCAAGTACAGTTCCTAAAGAAAATAGTGCAGCA
CCTGCTGAAAAAACAAAAGCAATGTCTTCTCCGACAGTTGCAGCAGCCCC
TCAAGGAAAGATTCGAGCAACACCAGCAGCTCGTAAGGCGGCTCGTGATC
TGGGAGTTAACCTGAATCAGGTTTCAGGGACAGGCGCTAAAGGCCGTGTT
CACAAGGAAGATGTTGAAAGCTTTAAAGCAGCTCAGCCTAAAGCAACACC
ATTAGCTAGGAAAATTGCTATAGATAAAGGTATTGATCTAGCCAGTGTCT
CAGGAACAGGTTTTGGCGGCAAAATTATCAAGGAAGATATTTTAAATCTG
TTTGAGGCAGCTCAGCCTGTTAATGATGTGTCAGATCCTGCTAAAGAAGC
AGCTGCCTTACCAGAGGGTGTTGAAGTCATTAAGATGTCTGCCATGCGTA
AGGCAGTGGCTAAAAGCATGGTCAATTCTTACCTGACAGCTCCAACTTTT
ACTCTCAATTATGACATTGACATGACTGAGATGATTGCGTTGCGTAAAAA
GTTAATTGATCCTATCATGGAAAAAACAGGTTTTAAAGTTAGCTTCACAG
ATTTGATTGGTCTGGCAGTCGTAAAAACCTTAATGAAACCAGAACATCGT
TACCTCAATGCTTCACTCATTAATGACGCGACTGAGATTGAACTTCATCA
ATTTGTTAACCTTGGTATCGCCGTTGGACTTGATGAAGGACTGTTAGTAC
CTGTTGTTCATGGTGCAGATAAGATGAGCTTGTCAGATTTTGTTATAGCT
TCAAAGGATGTCATTAAGAAAGCTCAGACCGGTAAATTAAAAGCCACTGA
AATGTCTGGTTCAACCTTTTCCATTACAAACTTGGGGATGTTTGGCACTA
AGACTTTCAACCCCATTATCAATCAGCCAAATTCGGCTATTTTGGGTGTA
GGAGCAACTATCCAAACGCCAACTGTTGTGGATGGTGAAATTAAGATTCG
TCCAATCATGGCACTGTGCTTGACCATCGATCACCGCTTGGTTGATGGCA
TGAACGGCGCTAAGTTCATGGTTGATCTTAAAAAACTGATGGAAAATCCA
TTTACATTATTGATTTGA

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