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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1434 IGR1437 IGR1433 IGR1435 IGR1438 IGR1436 IGR1438.1 IGR1438.2 IGR1439 NG1759 NG1760 RP54, - NG1766 pyrD, - NG1761 glnE, - NG1758 acpP, - NG1762 NG1438.1 NG1764 pglA, - NG1765 fabF, - NG1763 NG1759 NG1760 RP54, - NG1766 pyrD, - NG1761 glnE, - NG1758 acpP, - NG1762 NG1438.1 NG1764 pglA, - NG1765 fabF, - NG1763 Type: tandem, Name:  - 82 Type: tandem, Name:  - 83 NG1760 RP54, - NG1766 pyrD, - NG1761 glnE, - NG1758 NG1759 acpP, - NG1762 NG1438.1 NG1764 pglA, - NG1765 fabF, - NG1763
* Calculated from Protein Sequence

Gene ID: NG1763

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fabF  

Definition:
3-oxoacyl-[acyl-carrier-protein] synthase II

Gene Start:
1724804

Gene Stop:
1726048

Gene Length:
1245

Molecular Weight*:
43030

pI*:
5.40

Net Charge*:
-9.00

EC:
2.3.1.41  

Functional Class:
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Fatty acid biosynthesis (path 1)

Secondary Evidence:
Siggaard-Andersen,M., Wissenbach,M., Chuck,J.A., Svendsen,I.,
Olsen,J.G. and von Wettstein-Knowles,P.
The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV
from Escherichia coli is sensitive to cerulenin and specific for
short-chain substrates
Proc. Natl. Acad. Sci. U.S.A. 91 (23),11027-11031 (1994)
Medline: 95062198

Magnuson,K., Carey,M.R. and Cronan,J.E. Jr.
The putative fabJ gene of Escherichia coli fatty acid synthesis is
the fabF gene
J. Bacteriol. 177 (12), 3593-3595 (1995)
Medline: 95286559

Jackowski,S. and Rock,C.O.
Altered molecular form of acyl carrier protein associated with
beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants
J. Bacteriol. 169 (4), 1469-1473 (1987)
Medline: 87165751

Garwin,J.L., Klages,A.L. and Cronan,J.E. Jr.
Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli.Evidence for function in the thermal regulation of fatty acid
synthesis
J. Biol. Chem. 255 (8), 3263-3265 (1980)
Medline: 80159932

Moche,M., Schneider,G., Edwards,P., Dehesh,K. and Lindqvist,Y.
Structure of the complex between the antibiotic cerulenin and its
target, beta-ketoacyl-acyl carrier protein synthase
J. Biol. Chem. 274 (10), 6031-6034 (1999)
Medline: 99156870






Comment:
For other 'Fab' genes see NG1666 (FabI),NG1352 (fabF2),NG1804 (fabZ), NG2163 (fabG), NG2166 (fabD) and NG2168 (fabH).

Oklahoma ID: NGO.1763

Blast Summary:  PSI-Blast Search
Residues 1-415 are 98% similar to 3-oxoacyl-[acyl-carrier-protein] synthase from Neisseria meningitidis group A strain Z2491 (emb|CAB83362.1|).

Numerous hits in gapped BLAST to 3-oxoacyl-[acyl-carrier-protein] synthase sequences,e.g.residues 1-413 are 59% similar to 3-oxoacyl-acyl carrier protein synthase II from Pseudomonas aeruginosa strain PAO1 (gb|AAB94396.1|).Residues 1-412 are 60% similar to 3-oxoacyl-[acyl-carrier-protein] synthase II from Escherichia coli O157:H7,Escherichia coli K12 (gb|AAG55841.1|),(gb|AAC74179.1|).Residues 1-414 are 48% similar to probable acyl carrier protein synthase from Chlamydia trachomatis serotype D, strain UW3/Cx (7433742|).



COGS Summary:  COGS Search
BeTs to 10 clades of COG0304
COG name: 3-oxoacyl-(acyl-carrier-protein) synthase I
Functional Class:  I
The phylogenetic pattern of COG0304 is ----YqvCEBRhuj----inx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB000794 (Beta-ketoacyl synthase) with a combined E-value of 1.9e-12.
    IPB000794B    220-232
    IPB000794C    335-344


ProDom Summary:  Protein Domain Search
Residues 286-320 are 71% similar to a (SYNTHASE TRANSFERASE POLYKETIDE BIOSYNTHESIS) protein domain (PD000237) which is seen in O67612_AQUAE.

Residues 379-412 are 73% similar to a (SYNTHASE BETA-KETOACYL-ACP TRANSFERASE II) protein domain (PD003436) which is seen in O54440_PSEAE.

Residues 225-278 are 77% similar to a (SYNTHASE TRANSFERASE POLYKETIDE BIOSYNTHESIS) protein domain (PD000224) which is seen in FABF_VIBHA.

Residues 72-140 are 53% similar to a (SYNTHASE TRANSFERASE POLYKETIDE ACYLTRANSFERASE PROTEIN) protein domain (PD001987) which is seen in O54440_PSEAE.

Residues 322-378 are 71% similar to a (SYNTHASE TRANSFERASE POLYKETIDE BIOSYNTHESIS PROTEIN) protein domain (PD000208) which is seen in O34340_BACSU.

Residues 148-211 are 62% similar to a (SYNTHASE TRANSFERASE POLYKETIDE ACYLTRANSFERASE PROTEIN) protein domain (PD000145) which is seen in O67612_AQUAE.

Residues 5-147 are 33% similar to a (F10G8.9 PROTEIN) protein domain (PD083816) which is seen in Q93458_CAEEL.

Residues 4-69 are 43% similar to a (SYNTHASE TRANSFERASE POLYKETIDE BIOSYNTHESIS) protein domain (PD000325) which is seen in KAS1_STRVN.

Residues 3-71 are 53% similar to a (SYNTHASE TRANSFERASE ACYLTRANSFERASE BETA-KETOACYL-ACP) protein domain (PD001234) which is seen in P73283_SYNY3.



Paralogs:  Local Blast Search


NG1763 is paralogously related to NG1352 (probable 3-oxoacyl-(acyl-carrier-protein) synthase) (2e-17).


Pfam Summary:  Pfam Search
Residues 4 to 248 (E-value = 4.9e-74) place NG1763 in the ketoacyl-synt family which is described as Beta-ketoacyl synthase, N-terminal domain (PF00109)
Residues 256 to 414 (E-value = 1.8e-71) place NG1763 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain (PF02801)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
63  
146
transmembrane  
341  
357

PDB Hit:
pdb|1B3N|1B3N-A BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG498.0 0e+00
pdb|1E5M|1E5M-A BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II 438.0 0e+00
pdb|1DD8|1DD8-A CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER280.0 3e-76
pdb|1FJ4|1FJ4-A THE

Gene Protein Sequence:
MSQRRVVITGLGQVSPVGNTAAEAWDNLLAGKSGIGAITRFDASDINSRV
AGEVRGFDIGQYISAKEARRMDVFIHYGIAAALQAIADSGLDDVENLDKD
RIGVNIGSGIGGLPSIEATGKAVIEGGARKINPFFIPGSLINLISGHVTI
LKGYRGPSYGMVSACTTGAHAIGDSARLIKYGDADIMVAGGAEGAISTLG
VGGFAAMKALSTRNDDPATASRPWDKGRDGFVIGEGAGILVLEELEHAKK
RGAKIYAEIVGFGMSSDAYHITAPNEEGPALAVTRALKDAGINPEDVDYV
NAHGTSTPLGDANETKALKRAFGEHACKTVISSTKSMTGHLLGAAGGVEA
VYSILAIHDGKIPPTINIFEQDVEAGCDLDYCANEARDAEIDVAISNSFG
FGGTNGTLVFKRFKG

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTCAGAGAAGAGTAGTCATTACAGGCTTAGGTCAGGTTTCCCCTGT
CGGCAACACTGCCGCAGAGGCTTGGGACAACCTGCTCGCCGGCAAAAGCG
GCATCGGCGCGATTACCCGCTTTGACGCATCCGACATCAACAGCCGTGTC
GCCGGCGAAGTGCGCGGTTTCGACATCGGACAATACATCAGCGCGAAAGA
AGCGCGCCGGATGGACGTGTTCATCCACTACGGCATCGCCGCCGCATTGC
AGGCGATTGCCGATTCGGGTTTGGACGATGTGGAAAACCTCGACAAAGAC
CGCATCGGCGTGAACATCGGTTCCGGCATCGGCGGACTGCCCAGCATCGA
GGCCACCGGCAAAGCCGTAATCGAAGGCGGCGCGCGCAAAATCAACCCTT
TCTTTATCCCCGGTTCGCTGATCAACCTGATTTCCGGACACGTTACCATC
CTCAAAGGCTACCGCGGCCCGAGCTACGGCATGGTTTCCGCCTGTACCAC
CGGCGCGCACGCCATCGGCGATTCCGCCCGACTGATCAAATACGGCGACG
CGGACATAATGGTTGCCGGCGGCGCGGAAGGCGCAATCAGCACCTTGGGC
GTGGGCGGTTTTGCTGCGATGAAAGCCCTCTCCACCCGCAACGACGACCC
CGCCACCGCTTCCCGTCCGTGGGACAAAGGCCGCGACGGCTTCGTCATCG
GCGAAGGCGCGGGCATATTGGTGTTGGAAGAATTAGAACACGCCAAAAAA
CGCGGCGCGAAAATCTACGCCGAAATCGTCGGCTTCGGCATGAGTTCCGA
TGCTTACCATATCACCGCGCCGAACGAAGAAGGCCCCGCCCTTGCCGTTA
CCCGCGCGCTGAAAGATGCCGGCATCAATCCCGAAGACGTGGATTACGTC
AACGCGCACGGCACGTCCACCCCCTTGGGCGATGCCAACGAAACCAAAGC
CCTCAAACGCGCGTTCGGCGAACACGCCTGCAAAACCGTCATCAGCTCGA
CCAAATCCATGACCGGCCACCTGCTCGGCGCGGCGGGCGGCGTGGAGGCC
GTGTACAGCATTTTGGCGATACACGACGGCAAAATCCCGCCGACCATCAA
CATTTTTGAACAAGACGTTGAAGCCGGCTGCGATTTGGACTACTGCGCCA
ACGAAGCGCGCGACGCGGAAATCGACGTTGCCATTTCCAACTCCTTCGGC
TTCGGCGGCACCAACGGTACGCTGGTCTTCAAACGCTTCAAAGGC


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