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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0754 IGR0756 IGR0757 IGR0758 IGR0761 IGR0759 IGR0756.1 IGR0753 IGR0755 IGR0760 IGR0756.2 fitA, - NG0908 NG0914 fitB, - NG0907 NG0910 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 NG0911 NG0906 fitA, - NG0908 NG0914 fitB, - NG0907 NG0910 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 NG0911 NG0906 Type: direct, Name:  - 117 NG0914 fitB, - NG0907 NG0910 tpn, - NG0909 sucD, - NG0912 sucC, - NG0913 sucB, - NG0916 dldH, - NG0915 sucA, - NG0917 fitA, - NG0908 NG0911 NG0906
* Calculated from Protein Sequence

Gene ID: NG0913

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sucC  

Definition:
succinyl-CoA synthetase beta subunit

Gene Start:
892696

Gene Stop:
891533

Gene Length:
1164

Molecular Weight*:
41295

pI*:
5.20

Net Charge*:
-6.48

EC:
6.2.1.5  

Functional Class:
Energy metabolism; TCA cycle  

Pathway: pathway table
C5-Branched dibasic acid metabolism
Citrate cycle (TCA cycle)
Propanoate metabolism
Reductive carboxylate cycle (CO2 fixation)

Secondary Evidence:
Fraser,M.E., James,M.N., Bridger,W.A. and Wolodko,W.T. A detailed structural description of Escherichia coli succinyl-CoA synthetase. J. Mol. Biol. 285 (4): 1633-1653 (1999) [Medline: 99141407].

Joyce,M.A., Fraser,M.E., James,M.N., Bridger,W.A. and Wolodko,W.T. ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography. Biochemistry 39 (1): 17-25 (2000) [Medline: 20092606].

Freestone,P., Grant,S., Toth,I. and Norris,V. Identification of phosphoproteins in Escherichia coli . Mol. Microbiol. 15 (3): 573-580 (1995) [Medline: 95302968].

Buck,D. and Guest,J.R. Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon. Biochem. J. 260 (3): 737-747 (1989) [Medline: 89350876].

Buck,D., Spencer,M.E. and Guest,J.R. Primary structure of the succinyl-CoA synthetase of Escherichia coli. Biochemistry 24 (22): 6245-6252 (1985) [Medline: 86104124].

Comment:
From GenBANK (gi:135028): The catalytic activity of this enzyme is: succinate + CoA + ATP = succinyl-CoA + ADP + orthophosphate. It exhibits two interesting properties: 'substrate synergism', in which the enzyme is most active for the catalysis of its partial reactions only when all the substrate binding sites are occupied, and 'catalytic cooperativity' between alternating active sites in the tetramer, whereby the interaction of substrates (particularly ATP) at one site is needed to promote catalysis at the other. In E. coli, this tetramer of two alpha and two beta chains catalyzes its reaction via 3 steps that involve phosphoryl enzyme and enzyme-bound succinyl phosphate as intermediates. During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP & thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The alpha subunit binds CoA, as well as ATP and catalyzes phosphoryl transfer to one of its histidine residues. The complete active site is probably located in the region of alpha-beta contact. The succinyl-CoA synthetases of eukaryotes and gram-positive bacteria differ from the gram-negative enzymes in containing single alpha-beta dimers. It also exhibits similarity to other alpha subunits of succinyl-CoA synthetase, of malate-CoA ligase and to ATP citrate-lyase.

See also the alpha subunit, NG0912.

Oklahoma ID: NGO.913c

Blast Summary:  PSI-Blast Search
NG0913 is orthologous to AE002447, N. meningitidis MC58 succinyl-CoA synthetase, beta subunit : residues 1-388 have 98% similarity to residues 1-388 in NG0913.
NG0913 also has very strong hits to succinyl-CoA synthetase, beta subunit proteins in several other organisms.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0045
COG name: Succinyl-CoA synthetase beta chain
Functional Class:  C
The phylogenetic pattern of COG0045 is Amt-yQ-cebrh------inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000303 (ATP-citrate lyase/succinyl-CoA ligases) with a combined E-value of 1.5e-61.
    IPB000303A    26-72
    IPB000303B    192-201
    IPB000303C    264-307
    IPB000303D    344-367
***** IPB003135 (ATP-grasp domain) with a combined E-value of 1.8e-08.
    IPB003135B    44-56
    IPB003135C    275-285


ProDom Summary:  Protein Domain Search
Residues 135-204 are 52% similar to a (BETA LIGASE SUCCINYL-COA SYNTHETASE) protein domain (PD111317) which is seen in SUCC_BACSU.

Residues 206-383 are 60% similar to a (BETA SUCCINYL-COA SYNTHETASE LIGASE) protein domain (PD003397) which is seen in SUCC_ECOLI.

Residues 8-129 are 50% similar to a (LIGASE SYNTHETASE CARBOXYLASE CARBAMOYL-PHOSPHATE) protein domain (PD000180) which is seen in SUCC_ECOLI.

Residues 1-134 are 41% similar to a (LIGASE BETA SYNTHETASE SUCCINYL-COA) protein domain (PD186273) which is seen in SUCC_HAEIN.



Paralogs:  Local Blast Search


NG0913 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 30 to 199 (E-value = 4.6e-23) place NG0913 in the ATP-grasp family which is described as ATP-grasp domain (PF02222)
Residues 247 to 383 (E-value = 7.8e-77) place NG0913 in the Ligase_CoA family which is described as CoA-ligase (PF00549)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
76
transmembrane  
332  
348

PDB Hit:
pdb|1CQI|1CQI-B CRYSTAL STRUCTURE OF THE COMPLEX OF ADP AND MG2+427.0 0e+00
pdb|1SCU|1SCU-B SUCCINYL-COA 427.0 0e+00
pdb|1JLL|1JLL-B CRYSTAL STRUCTURE ANALYSIS OF THE E197BETAA 425.0 0e+00
pdb|1EUD|1EUD-B CRYSTAL STRUCTURE OF PHOSPHORYLATED P

Gene Protein Sequence:
MNLHEYQAKELLASYGLPVQGGILAHNGEEAAAAYDKLGGKFAVVKAQVH
AGGRGKAGGVKVVKSREKAKEVAESLIGTNLVTYQTDANGQPVNSVLVCE
DMYPVQTELYLGAVVDRSTRRVTFMASTEGGVEIEKVAAETPEKIFKVTV
DPLVGLQPCQAREVAFQLGLKDKQINEFAKLMTGAYKAFVENDFALFEVN
PLAVRENGALACVDGKIGIDSNALYRLPKIAELRDKSQENERELKASEFD
LNYVALEGKIGCMVNGAGLAMATMDIIKLKGGQPANFLDVGGGATKDRVV
EAFKLILEDKSVKGVLINIFGGIVRCDMIAEAIVAAVKEINVNVPVVVRL
EGNNAELGAKILNESGLKLTSADGLNDAAEKIVAAVNA

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATTTACACGAGTATCAGGCTAAAGAACTGCTGGCTAGCTACGGTTT
GCCCGTACAAGGCGGTATTTTGGCGCACAACGGCGAAGAAGCCGCTGCAG
CTTACGACAAATTGGGCGGCAAATTCGCTGTTGTCAAAGCACAGGTACAC
GCCGGCGGCCGCGGTAAAGCGGGCGGCGTAAAAGTCGTTAAAAGCCGCGA
AAAAGCCAAAGAAGTGGCTGAAAGCCTGATTGGCACCAACTTGGTAACTT
ACCAAACCGATGCCAACGGCCAACCTGTCAACAGCGTTTTGGTTTGCGAA
GATATGTATCCTGTTCAAACCGAGCTGTACTTGGGCGCAGTGGTTGACCG
TTCTACCCGCCGCGTTACATTCATGGCTTCTACCGAAGGCGGCGTGGAAA
TCGAAAAAGTTGCTGCTGAAACTCCAGAAAAAATCTTCAAAGTAACCGTT
GATCCGCTGGTCGGCCTGCAACCTTGCCAAGCTCGCGAAGTTGCCTTCCA
ACTGGGCTTGAAAGACAAACAAATCAACGAGTTCGCCAAACTGATGACCG
GCGCGTACAAAGCGTTTGTCGAAAACGACTTCGCCCTGTTTGAAGTCAAC
CCGCTGGCAGTTCGCGAAAACGGCGCACTGGCTTGCGTGGACGGCAAAAT
CGGCATCGACAGCAACGCGCTCTACCGCCTGCCAAAAATCGCTGAATTGC
GCGACAAATCTCAAGAAAACGAACGTGAACTGAAAGCTTCTGAATTCGAC
CTGAACTATGTTGCCCTGGAAGGCAAAATCGGCTGTATGGTTAACGGTGC
CGGTTTGGCGATGGCCACCATGGACATCATCAAACTCAAAGGCGGCCAAC
CTGCCAACTTCTTGGACGTTGGCGGCGGCGCAACCAAAGACCGCGTGGTT
GAAGCGTTCAAACTGATTTTGGAAGACAAATCCGTTAAAGGCGTATTGAT
CAACATCTTCGGCGGTATCGTACGTTGCGACATGATTGCGGAAGCCATCG
TGGCAGCCGTTAAAGAAATCAACGTCAACGTTCCTGTCGTTGTTCGTTTG
GAAGGCAACAACGCCGAACTCGGCGCGAAAATCCTGAACGAATCAGGTCT
GAAACTGACTTCTGCAGACGGTCTGAATGACGCAGCCGAAAAAATTGTTG
CAGCCGTAAACGCC


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