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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0757 IGR0758 IGR0761 IGR0759 IGR0762 IGR0760 IGR0756.2 NG0914 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 sucA, - NG0917 NG0914 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 sucA, - NG0917 NG0914 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 sucA, - NG0917
* Calculated from Protein Sequence

Gene ID: NG0916

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sucB  

Definition:
dihydrolipoamide succinyltransferase E2 component

Gene Start:
896050

Gene Stop:
894872

Gene Length:
1179

Molecular Weight*:
41674

pI*:
5.00

Net Charge*:
-9.00

EC:
2.3.1.61  

Functional Class:
Energy metabolism; TCA cycle  

Pathway: pathway table
Citrate cycle (TCA cycle)
Lysine degradation

Secondary Evidence:
Spencer,M.E., Darlison,M.G., Stephens,P.E., Duckenfield,I.K. and
Guest,J.R.
Nucleotide sequence of the sucB gene encoding the dihydrolipoamide
succinyltransferase of Escherichia coli K12 and homology with the
corresponding acetyltransferase
Eur. J. Biochem. 141 (2), 361-374 (1984)
Medline: 84236169

Darlison,M.G., Spencer,M.E. and Guest,J.R.
Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate
dehydrogenase of Escherichia coli K12
Eur. J. Biochem. 141 (2), 351-359 (1984)
Medline: 84236168

Ricaud,P.M., Howard,M.J., Roberts,E.L., Broadhurst,R.W. and
Perham,R.N.
Three-dimensional structure of the lipoyl domain from the
dihydrolipoyl succinyltransferase component of the 2-oxoglutarate
dehydrogenase multienzyme complex of Escherichia coli
J.Mol.Biol. 264 (1), 179-190 (1996)
Medline: 97107536

Robien,M.A., Clore,G.M., Omichinski,J.G., Perham,R.N., Appella,E.,
Sakaguchi,K. and Gronenborn,A.M.
Three-dimensional solution structure of the E3-binding domain of
the dihydrolipoamide succinyltransferase core from the
2-oxoglutarate dehydrogenase multienzyme complex of Escherichia
coli
Biochemistry 31 (13), 3463-3471 (1992)
Medline: 92207970

Knapp,J.E., Mitchell,D.T., Yazdi,M.A., Ernst,S.R., Reed,L.J. and
Hackert,M.L.
Crystal structure of the truncated cubic core component of the
Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
J. Mol. Biol. 280 (4), 655-668 (1998)
Medline: 98344105





Comment:
From GenBANK (gi:1706443): The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). It performs by the reaction: dihydrolipoamide + NAD(+) = lipoamide + NADH, with a cofactor, FAD. The active site is a redox-active disulfide bond. It belongs to the pyridine nucleotide-disulfide oxidoreductases class-I.

Oklahoma ID: NGO.916c

Blast Summary:  PSI-Blast Search
NG0916 is 99% identical to a previously sequenced Neisseria gonorrhoeae protein in GenBank, 790863.

Residues 1-393 are 97% similar to 2-oxoglutarate dehydrogenase, E2 component,dihydrolipoamide succinyltransferase from Neisseria meningitidis group B strain MD58 (7226195|).

Numerous hits in gapped BLAST to 2-oxoglutarate dehydrogenase/ dihydrolipoamide S-succinyltransferase sequences, e.g. residues 3-393 are 56% similar to dihydrolipoamide S-succinyltransferase from Escherichia coli O157:H7 (13360210|), residues 1-393 are 59% similar to dihydrolipoamide succinyltransferase (E2 subunit)
Pseudomonas aeruginosa strain PAO1 (11348426|).




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 1.1e-100.
    IPB001078A    22-54
    IPB001078B    110-140
    IPB001078C    219-240
    IPB001078D    294-336
    IPB001078E    355-391
***** IPB000089 (Biotin / Lipoyl attachment) with a combined E-value of 6.5e-17.
    IPB000089A    256-275
    IPB000089B    310-329
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 1.6e-16.
    IPB003016    25-59
***** IPB002215 (HlyD family secretion protein) with a combined E-value of 2.3e-06.
    IPB002215A    42-78


ProDom Summary:  Protein Domain Search
Residues 17-76 are 96% similar to a (BIOTIN DIHYDROLIPOAMIDE PYRUVATE DEHYDROGENASE) protein domain (PD000268) which is seen in Q50993_NEIGO.

Residues 183-392 are 99% similar to a (DIHYDROLIPOAMIDE TRANSFERASE DEHYDROGENASE LIPOYL) protein domain (PD001115) which is seen in Q50993_NEIGO.

Residues 118-142 are identical to a (PROTEIN REPEAT PRECURSOR DNA-BINDING NUCLEAR SIGNAL) protein domain (PD000540) which is seen in Q50993_NEIGO.



Paralogs:  Local Blast Search


NG0916 is paralogously related to NG0564 (dihydrolipoamide S-acetyltransferase complex (E2 component of pyruvate dehydrogenase complex)) (2e-62), NG0562 (dihydrolipoamide dehydrogenase (pyruvate dehydrogenase, E3 component, lipoamide dehydrogenase) (glycine cleavage system L protein)) (1e-10), NG1286 (translation initiation factor IF-2) (3e-05) and NG0045 (acetyl-Co carboxylase/biotin carboxylase carrier protein (BCCP)) (0.001).


Pfam Summary:  Pfam Search
Residues 3 to 76 (E-value = 4e-28) place NG0916 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 108 to 144 (E-value = 1.5e-16) place NG0916 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 161 to 391 (E-value = 7.9e-139) place NG0916 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
188

PDB Hit:
pdb|1C4T|1C4T-A CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE 313.0 4e-86
pdb|1B5S|1B5S-A DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) 159.0 8e-40
pdb|1DPC|1DPC DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) 115.0 1e-26
pdb|1DPD|1DPD DIHYD

Gene Protein Sequence:
MIIDVKVPMLSESVSEGTLLEWKKKVGEAVARDEILIDIETDKVVLEVPS
PQAGVLVEIVAQDGETVVADQVLARIDTAATVAAEAPAAAPAEAAPAAVP
AAAQNNAAMPAAAKLAAETGVDVNVLQGSGRDGRVLKEDVQNAAAKPAAA
VAPAVALPAGARPEERVPMSRLRARVAERLLASQQENAILTTFNEVNMKP
IMDLRAKYKEKFEKEHGVKLGFMSFFVKAAVTALKKYPVVNASVDGKDIV
YHGYFDIGIAIGSPRGLVVPILRDADQMSIADIEQAIVDYAKKAKDGKIA
IEDLTGGTFSITNGGTFGSMMSTPIINPPQSAILGMHATKERAVVENGQV
VVRPMMYLALSYDHRIIDGREAVLTLVAIKDALEDPVRLLLDL

Gene Nucleotide Sequence:  Sequence Viewer
ATGATTATTGATGTAAAAGTACCTATGCTGTCTGAAAGCGTATCTGAAGG
CACACTCTTGGAATGGAAGAAAAAAGTTGGCGAAGCAGTTGCCCGTGACG
AAATCCTGATCGATATCGAAACGGACAAAGTGGTTTTGGAAGTACCTTCT
CCACAAGCCGGCGTATTGGTTGAAATCGTAGCGCAAGACGGTGAAACCGT
TGTTGCCGACCAAGTTTTGGCCCGTATCGATACAGCTGCTACTGTCGCTG
CTGAAGCACCTGCAGCCGCTCCTGCCGAAGCTGCCCCGGCTGCCGTTCCT
GCTGCTGCACAAAACAACGCCGCCATGCCTGCCGCTGCAAAACTGGCTGC
CGAGACCGGTGTTGACGTGAACGTATTGCAAGGTTCCGGCCGTGACGGTC
GCGTATTGAAAGAAGACGTACAAAATGCCGCTGCCAAACCTGCCGCAGCC
GTGGCCCCTGCCGTTGCACTTCCTGCCGGCGCACGTCCTGAAGAACGCGT
ACCAATGAGCCGCCTGCGTGCCCGTGTTGCAGAACGCCTCTTGGCTTCTC
AACAAGAAAACGCCATTCTGACTACATTCAACGAAGTCAACATGAAACCG
ATCATGGACTTGCGTGCGAAGTACAAAGAAAAATTCGAGAAAGAACATGG
CGTAAAACTGGGCTTTATGTCCTTCTTCGTTAAAGCCGCTGTTACAGCCC
TGAAAAAATACCCGGTTGTGAATGCTTCTGTTGACGGCAAAGACATTGTG
TACCACGGCTACTTCGACATCGGTATCGCAATTGGCAGCCCACGCGGTTT
GGTTGTACCAATCCTGCGCGATGCCGACCAAATGAGCATTGCCGACATCG
AACAAGCAATTGTTGATTACGCAAAAAAAGCCAAAGACGGCAAAATCGCT
ATCGAAGACCTGACCGGCGGTACATTCAGTATTACCAACGGCGGTACTTT
CGGTTCTATGATGTCCACCCCGATCATCAACCCGCCTCAATCTGCGATTT
TGGGTATGCATGCCACTAAAGAGCGCGCTGTGGTTGAAAACGGCCAAGTT
GTTGTCCGTCCAATGATGTATCTGGCTCTGTCTTACGACCACCGTATCAT
TGACGGCCGCGAAGCTGTATTGACCTTGGTAGCCATTAAAGACGCGTTGG
AAGACCCGGTCCGCCTGTTGTTGGATCTG


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