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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0764 IGR0758 IGR0765 IGR0761 IGR0763 IGR0759 IGR0762 IGR0760 NG0919 NG0914 sdhB,dhsB, - NG0920 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 dhsA,sdhA, - NG0921 sucA, - NG0917 NG0919 NG0914 sdhB,dhsB, - NG0920 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 dhsA,sdhA, - NG0921 sucA, - NG0917 NG0919 sdhB,dhsB, - NG0920 sucC, - NG0913 sucB, - NG0916 cisY,gltA, - NG0918 dldH, - NG0915 dhsA,sdhA, - NG0921 sucA, - NG0917 NG0914
* Calculated from Protein Sequence

Gene ID: NG0917

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sucA  

Definition:
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase

Gene Start:
898978

Gene Stop:
896153

Gene Length:
2826

Molecular Weight*:
105115

pI*:
6.80

Net Charge*:
-3.53

EC:
1.2.4.2  

Functional Class:
Energy metabolism; TCA cycle  

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

Secondary Evidence:
Hein,S. and Steinbuchel,A.
Cloning and characterization of the Alcaligenes eutrophus
2-oxoglutarate dehydrogenase complex
FEMS Microbiol. Lett. 136 (3), 231-238 (1996)
Medline: 97021018

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

Schulze,E., Westphal,A.H., Hanemaaijer,R. and de Kok,A.
The 2-oxoglutarate dehydrogenase complex from Azotobacter
vinelandii. 1. Molecular cloning and sequence analysis of the gene
encoding the 2-oxoglutarate dehydrogenase component
Eur. J.Biochem. 187 (1), 229-234 (1990)
Medline: 90126823




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.917c

Blast Summary:  PSI-Blast Search
NG0917 is 98% identical to a previously sequenced Neisseria gonorrhoeae protein in GenBank, 790863.

Residues 1-942 are 99% similar to probable oxoglutarate dehydrogenase from Neisseria meningitidis group B strain MD58, group A strain Z2491 (11252292|).

Numerous hits in gapped BLAST to oxoglutarate dehydrogenase sequences,e.g.residues 1-942 are 51% similar to 2-oxoglutarate dehydrogenase from Vibrio cholerae group O1 strain N16961 (11252270|).Residues 1-942 are 51% similar to 2-oxoglutarate dehydrogenase from Pseudomonas aeruginosa strain PAO1 (11347271|).Residues 6-940 are 51% similar to 2-oxoglutarate dehydrogenase from Escherichia coli K12 (1786945|).

COGS Summary:  COGS Search
BeTs to 6 clades of COG0567
COG name: Pyruvate and 2-oxoglutarate dehydrogenases, E1 component
Functional Class:  C
The phylogenetic pattern of COG0567 is ----y---ebrh------inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 2-60 are 46% similar to a (DEHYDROGENASE 2-OXOGLUTARATE E1 COMPONENT) protein domain (PD006490) which is seen in ODO1_ALCEU.



Paralogs:  Local Blast Search


NG0917 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 207 to 533 (E-value = 4.4e-32) place NG0917 in the E1_dh family which is described as Dehydrogenase E1 component (PF00676)
Residues 594 to 792 (E-value = 7.6e-69) place NG0917 in the Transket_pyr family which is described as Transketolase, pyridine binding domain (PF02779)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
351  
367

PDB Hit:
pdb|1IK6|1IK6-A 3D STRUCTURE OF THE E1BETA SUBUNIT OF PYRUVATE 41.4 7e-04
pdb|1DTW|1DTW-B HUMAN BRANCHED-CHAIN ALPHA-KETO ACID 145.0 4e-35
pdb|1QS0|1QS0-B CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 138.0 4e-33
pdb|1DTW|1DTW-B HUMA

Gene Protein Sequence:
MMDEKLNFSYLFGSNAPYIEELYEAFLENPDAVDEKWKQYFTDLSKQPGT
VAVDVAHTPIRESFVTLAKKKIASAVAGGADEAMLKKQVSVLRLISAYRI
QGVGAAQLDPLKRIPPRDIEALDPKFHGLSDADMALRFNMGEGDFANRGK
LLLSQIISNLKQTYCGHIALEYIYIPNTEERRWVRNYFESVLSTPHYNAD
QKRRILKEMTAAETLERYLHTKYVGQKRFGVEGGESAIAGLNYLIQNAGK
DGVEEVIIGMAHRGRLNVLVNILGKKPGDLFAEFEGRAEIKLPSGDVKYH
MGFSSDIATPHGPMHVSLAFNPSHLEIVNPVVEGSARAKQKRLGENGRDK
VLPVLIHGDSAFIGLGVNQATFNLSKTRGYTTGGTVHIVINNQIGFTTSD
IRDTRSTVHCTDIAKMVSAPVIHVNGDDPERVCFAIQAALDYRKKFHKDI
VIDVVCYRKWGHNEGDDPTLTQPMMYKKVSQHPGARALYTEQLIAEGVVT
QVEADGYIQAYRDALDKGEHVEQTTLSNFQRTQIDWSKYQGKDWREKIET
GLPAADIERLTEKFTAVPEGFALHPTAKRVIEARKAMASGKQAIDWGMAE
TLAYASLLTKGHGVRISGEDSGRGTFSHRHAVLHDQKREKWDDGTYVPLR
NMGEGLGEFLVIDSILNEEAVMAFEYGFACSAPDKLTIWEAQFGDFANGA
QVTIDQFLSSGETKWGRLCGLTTILPHGYDGQGPEHSSARVERWLQLCSE
NNMQVIMPSEASQMFHLLQRQVLGSYRKPLVIFMSKRLLRFKGAMSPLEN
FTEGSTFRPVIGDTAERASNDSVKRVVLCAGQVYYDLEAGRAERKLEDDV
AIVRVEQLYPFPYDEVKAELAKYPNAKSVVWAQEEPKNQGAFYQIRHRIE
DVISEEQKLSYAGRPSSASPAVGYSSKHIAQLKQLVEDALAL

Gene Nucleotide Sequence:  Sequence Viewer
ATGATGGACGAAAAACTCAATTTCTCTTATCTGTTCGGTTCGAACGCACC
CTACATTGAGGAATTGTACGAGGCTTTTTTGGAAAACCCCGATGCGGTTG
ATGAAAAATGGAAGCAGTATTTCACCGATTTGAGCAAACAGCCGGGGACG
GTTGCTGTCGATGTCGCACACACACCGATTCGCGAATCATTTGTTACTTT
GGCGAAAAAGAAAATTGCATCTGCCGTTGCGGGCGGTGCGGATGAGGCAA
TGCTGAAAAAGCAAGTCAGCGTTTTACGGCTGATTTCTGCCTATCGTATC
CAAGGCGTGGGTGCGGCCCAACTTGATCCGCTCAAACGTATCCCTCCGCG
CGATATTGAAGCCCTCGATCCGAAATTCCACGGTCTGTCAGATGCCGATA
TGGCGCTTCGATTCAATATGGGCGAGGGTGATTTTGCCAATCGCGGCAAA
CTGCTCTTGTCCCAAATCATCAGCAACCTCAAACAAACCTACTGCGGCCA
CATCGCATTGGAATATATCTATATTCCCAATACCGAAGAGCGCCGTTGGG
TACGCAACTATTTTGAAAGCGTATTGTCCACACCGCATTACAATGCCGAT
CAAAAACGCCGTATCTTGAAAGAGATGACCGCTGCCGAGACTTTGGAACG
TTATCTGCATACCAAATATGTCGGTCAGAAACGTTTCGGTGTCGAAGGCG
GCGAAAGCGCGATTGCCGGTTTGAACTACCTGATTCAAAACGCCGGTAAG
GACGGCGTGGAAGAAGTCATCATCGGTATGGCGCACCGTGGCCGTCTGAA
TGTTTTGGTGAACATTTTGGGCAAAAAACCCGGCGATTTGTTTGCCGAAT
TTGAAGGCCGTGCCGAAATCAAACTGCCTAGTGGCGACGTGAAATACCAT
ATGGGCTTCAGCTCCGATATTGCCACCCCTCACGGCCCGATGCACGTTTC
TTTGGCGTTCAACCCGTCACACTTGGAAATCGTCAATCCGGTAGTGGAAG
GTTCTGCACGCGCCAAACAAAAACGTTTGGGCGAAAACGGCCGCGATAAA
GTCTTGCCGGTATTGATTCACGGCGATTCCGCATTTATCGGTTTGGGTGT
CAACCAAGCAACATTCAACCTGTCTAAAACGCGCGGTTATACCACAGGCG
GTACGGTCCATATCGTCATCAACAACCAAATCGGCTTTACCACTTCCGAT
ATCCGCGATACCCGTTCAACCGTACACTGTACCGATATCGCAAAAATGGT
TTCCGCTCCGGTTATCCATGTGAACGGCGATGATCCCGAACGCGTTTGCT
TTGCCATTCAAGCCGCTTTGGATTACCGCAAAAAATTCCATAAAGACATC
GTAATCGACGTTGTCTGCTACCGTAAATGGGGTCACAACGAGGGCGATGA
TCCGACTTTGACCCAACCGATGATGTACAAAAAAGTATCGCAACATCCGG
GTGCGCGTGCTTTGTACACCGAGCAACTGATTGCCGAAGGCGTGGTAACT
CAAGTTGAGGCCGACGGTTACATCCAAGCCTACCGTGATGCTTTGGACAA
AGGCGAACATGTTGAGCAAACAACGTTGAGCAACTTCCAACGCACACAAA
TCGACTGGAGCAAATACCAAGGTAAAGATTGGCGCGAAAAAATCGAAACC
GGTTTGCCTGCCGCCGACATTGAGCGTCTTACTGAGAAATTCACCGCTGT
GCCGGAAGGCTTTGCCCTGCATCCGACTGCAAAACGTGTGATCGAAGCGC
GTAAAGCCATGGCATCCGGCAAACAAGCCATCGACTGGGGTATGGCCGAA
ACCCTCGCATACGCAAGCCTGCTGACCAAAGGTCATGGCGTGCGTATCTC
CGGTGAGGACTCCGGCCGCGGTACATTCTCACACCGTCATGCCGTTCTGC
ACGATCAAAAACGCGAAAAATGGGACGACGGTACTTATGTTCCTCTTCGC
AACATGGGCGAAGGCTTGGGCGAGTTCCTGGTTATCGACTCTATCTTGAA
CGAAGAAGCCGTGATGGCGTTCGAGTACGGCTTTGCCTGCTCCGCTCCTG
ACAAGCTGACCATTTGGGAAGCTCAATTCGGTGACTTCGCCAACGGCGCG
CAAGTAACTATTGATCAATTCCTGTCTTCAGGCGAAACCAAGTGGGGTCG
CTTGTGCGGTCTGACCACCATCCTGCCGCACGGCTACGACGGTCAAGGCC
CTGAACACTCTTCTGCACGCGTAGAACGTTGGTTGCAACTGTGTTCTGAG
AACAATATGCAAGTCATCATGCCGTCTGAAGCGTCGCAAATGTTCCATCT
CTTGCAACGCCAAGTCTTGGGTTCATACCGCAAACCGCTGGTGATTTTCA
TGTCCAAACGCCTGTTGCGCTTCAAAGGTGCAATGAGCCCGCTGGAAAAC
TTCACCGAAGGTTCGACTTTCCGTCCGGTTATTGGTGATACCGCCGAACG
CGCAAGCAACGACAGCGTGAAACGCGTGGTATTGTGTGCCGGTCAGGTTT
ACTATGACTTGGAAGCCGGTCGAGCCGAACGTAAACTGGAAGATGATGTC
GCTATCGTCCGCGTTGAGCAGCTGTATCCGTTCCCATACGACGAGGTTAA
AGCCGAACTGGCGAAATATCCGAACGCAAAATCTGTGGTTTGGGCGCAAG
AAGAGCCGAAAAACCAAGGCGCGTTCTACCAAATCCGCCACCGCATCGAA
GACGTTATCAGCGAAGAGCAAAAACTGTCTTATGCCGGCCGTCCAAGCAG
CGCATCGCCTGCAGTGGGCTACTCAAGCAAACACATTGCTCAATTGAAAC
AATTGGTTGAAGACGCTTTGGCGTTA


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