Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0441 IGR0443 IGR0442 IGR0440 IGR0439 IGR0444 IGR0438 NG0533 NG0535 NG0532 NG0534 yhfL,lcfA,fadD, - NG0530 NG0531 tpn, - NG0528 purM, - NG0526 opuD,betT, - NG0529 NG0533 NG0535 NG0532 NG0534 yhfL,lcfA,fadD, - NG0530 NG0531 tpn, - NG0528 purM, - NG0526 opuD,betT, - NG0529 NG0533 NG0535 NG0532 NG0534 yhfL,lcfA,fadD, - NG0530 NG0531 tpn, - NG0528 purM, - NG0526 opuD,betT, - NG0529 NG0527 NG0527
* Calculated from Protein Sequence

Gene ID: NG0530

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
yhfL  lcfA  fadD  

Definition:
long-chain-fatty-acid--CoA ligase (acyl-CoA ligase) (long-chain acyl-CoA synthetase)

Gene Start:
505275

Gene Stop:
503725

Gene Length:
1551

Molecular Weight*:
57442

pI*:
9.90

Net Charge*:
11.35

EC:
6.2.1.-  6.2.1.3  

Functional Class:
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Ethylbenzene degradation
Fatty acid metabolism
Propanoate metabolism

Secondary Evidence:
Fulda,M., Heinz,E. and Wolter,F.P.
The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family.
Mol. Gen. Genet. 242 (3), 241-249 (1994)
Medline: 94150456.

Black,P.N., DiRusso,C.C., Metzger,A.K. and Heimert,T.L.
Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase.
J. Biol. Chem. 267 (35), 25513-25520 (1992)
Medline: 93094273.

Weimar,J.D., DiRusso,C.C., Delio,R. and Black,P.N.
Functional role of fatty acyl-coenzyme A synthetase in the
transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the
ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport
J. Biol. Chem. 277 (33), 29369-29376 (2002)
MEDLINE: 22162442

Comment:
From GenBANK (gi:462484): In E. coli, LcfA performs esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It catalyzes the reaction: ATP + a long-chain carboxylic acid + CoA = AMP + pyrophosphate + an acyl-CoA. Magnesium is required as a cofactor in this reaction.

Oklahoma ID: NGO.530c

Blast Summary:  PSI-Blast Search
Numerous significant hits to long-chain-fatty-acid--CoA ligase proteins in gapped BLAST; e.g. residues 34-511 are 37% similar to emb|CAB12867.1| similar to long-chain fatty-acid-CoA ligase of Bacillus subtilis, residues 9-512 are 34% similar to residues 41-562 of gb|AAB89478.1| long-chain-fatty-acid--CoA ligase (fadD-7) of Archaeoglobus fulgidus, residues 9-509 are 35% similar to residues 39-567 of gb|AAF11250.1|AE002011_1 long-chain fatty acid--CoA ligase of Deinococcus radiodurans.

Residues 1-517 of NG0530 are 98% similar to NMB1276 and 97% similar to NMA1482, both long-chain-fatty-acid--CoA ligases in N.meningitidis (11271976, 11271974).

COGS Summary:  COGS Search
BeTs to 8 clades of COG0318
COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases II
Functional Class:  I
The phylogenetic pattern of COG0318 is A-t-Y---EBRh------inx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB000873 (AMP-dependent synthetase and ligase) with a combined E-value of 6.8e-10.
    IPB000873A    174-189
    IPB000873B    209-219


ProDom Summary:  Protein Domain Search
Residues 329-504 are 29% similar to a (AAS 2-ACYLGLYCEROPHOSPHOETHANOLAMINE) protein domain (PD091442) which is seen in Q9ZCU1_RICPR.

Residues 338-429 are 43% similar to a (SIMILAR TO AMP-BINDING PROTEIN) protein domain (PD091472) which is seen in O02171_CAEEL.

Residues 82-251 are 28% similar to a (LIGASE SYNTHETASE PROTEIN ENZYME) protein domain (PD000070) which is seen in O07610_BACSU.

Residues 351-404 are 51% similar to a (LIGASE SYNTHETASE PROTEIN ENZYME) protein domain (PD000107) which is seen in O30302_ARCFU.

Residues 408-484 are 42% similar to a (LIGASE SYNTHETASE PROTEIN ENZYME BIOSYNTHESIS ANTIBIOTIC) protein domain (PD000081) which is seen in LCFA_BACSU.



Paralogs:  Local Blast Search


NG0530 is paralogously related to NG1213 (long-chain-fatty-acid--CoA-ligase) (2e-55).


Pfam Summary:  Pfam Search
Residues 33 to 444 (E-value = 3.6e-119) place NG0530 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
69  
85
transmembrane  
224  
240
non-globular  
399  
481

PDB Hit:
pdb|1BA3|1BA3 FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM 138.0 2e-33
pdb|1MD9|1MD9-A CRYSTAL STRUCTURE OF DHBE IN COMPLEX WITH DHB 126.0 1e-29
pdb|1AMU|1AMU-A PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN 110.0 5e-25
pdb|1MD9|1MD9-A CRYS

Gene Protein Sequence:
MNRTYANFYEMLAAACRKNGNGTAVFDGKEKTAYRALKQEAEAVAAYLQN
IGVKFGDTVALAVSNSTEFITAYFAVSAIGAVAVPMNTFLKNSEYAYILN
DCKARFLFASAGLSKELAGLKAQTPVEKIIWTDKSRPAGETAEGDAFFEN
VRRFPEKPDLGRQPRINDLAHIIYTSGTTGHPKGALISYANLFANLNGIE
RIFKISKRDRFIVFLPMFHSFTLTAMVLLPIYMACSIILVKSVFPFSNVL
KQALLKRATVFLGVPAIYTAMSKAKIPWYFRWFNRIRLFISGGAPLAEQT
ILDFKAKFPRAKLLEGYGLSEASPVVAVNTPERQKARSVGIPLPGLEAKA
VDEELVEVPRGEVGELIVRGGSVMRGYLNMPAATDETIVNGWLKTGDFVT
IDEDGFIFIVDRKKDLIISKGQNVYPREIEEEIHKLDAVEAAAVIGVKDR
YADEEIVAFVQLKEGMDLGEDEIRRHLRTVLANFKIPKQIHFKDGLPRNA
TGKVLKRVLKEQFEGNK

Gene Nucleotide Sequence:  Sequence Viewer
ATGAACCGGACTTATGCCAATTTCTACGAAATGCTCGCCGCCGCCTGCCG
CAAAAACGGCAACGGCACGGCAGTGTTCGACGGCAAGGAAAAAACCGCCT
ACCGCGCGCTCAAGCAGGAAGCCGAAGCCGTCGCGGCGTATCTGCAAAAT
ATCGGCGTGAAGTTCGGCGACACGGTCGCGCTGGCGGTTTCCAATTCCAC
AGAATTTATTACCGCCTATTTCGCCGTCTCCGCCATCGGCGCGGTCGCCG
TACCGATGAACACATTTTTGAAAAACAGCGAATACGCGTATATCCTGAAC
GACTGCAAGGCGCGCTTCCTGTTCGCCTCGGCCGGCCTGTCAAAAGAATT
GGCGGGCCTGAAGGCGCAAACGCCCGTCGAAAAAATCATTTGGACGGACA
AAAGCCGGCCGGCCGGCGAAACGGCGGAAGGCGATGCCTTTTTTGAAAAC
GTGCGCCGCTTCCCCGAAAAACCCGACTTGGGCCGCCAACCCCGGATAAA
TGATTTGGCACACATCATCTACACCTCCGGCACGACGGGGCATCCCAAAG
GCGCGCTAATCAGTTACGCCAACCTGTTCGCCAACCTGAACGGCATCGAA
CGCATCTTTAAAATTTCCAAACGCGACCGCTTTATCGTTTTCCTGCCGAT
GTTCCACAGCTTCACGCTGACGGCTATGGTGCTGCTGCCGATTTATATGG
CGTGTTCGATTATTTTGGTCAAATCCGTTTTCCCCTTTTCCAACGTTTTG
AAACAGGCCCTGCTCAAACGCGCAACCGTGTTTTTGGGCGTACCCGCGAT
TTACACCGCGATGAGCAAGGCAAAAATCCCTTGGTATTTCAGATGGTTCA
ACCGCATCCGCCTGTTTATCAGCGGCGGCGCGCCTTTGGCGGAACAAACC
ATCCTCGATTTTAAAGCCAAGTTCCCCCGCGCCAAATTGCTGGAAGGCTA
CGGACTGAGCGAAGCCTCGCCCGTCGTCGCCGTCAATACGCCCGAACGGC
AAAAAGCCCGCAGCGTCGGCATCCCCCTGCCCGGTTTGGAAGCCAAAGCC
GTCGATGAAGAATTGGTCGAAGTGCCGCGCGGCGAAGTGGGCGAACTGAT
CGTCAGGGGCGGTTCGGTGATGCGGGGCTACCTCAATATGCCTGCCGCCA
CCGATGAAACCATCGTCAACGGCTGGTTGAAAACGGGCGATTTCGTTACC
ATAGACGAGGACGGCTTTATCTTTATCGTCGACCGCAAAAAAGATTTGAT
TATTTCCAAAGGTCAAAACGTCTATCCGCGCGAGATCGAAGAAGAAATCC
ACAAACTCGATGCCGTCGAAGCCGCCGCCGTCATCGGCGTGAAAGACCGT
TATGCCGACGAGGAAATCGTCGCCTTCGTCCAATTGAAGGAAGGTATGGA
TTTGGGCGAGGACGAAATCCGCCGCCACCTGCGTACCGTGCTGGCAAATT
TCAAAATCCCCAAACAGATCCACTTTAAAGACGGGCTGCCGCGCAACGCT
ACGGGCAAAGTATTGAAACGGGTGCTGAAGGAGCAGTTTGAAGGAAACAA
A


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy