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Treponema pallidum Search Results

Record: 1 of 1  
MiniMap tRNA-Leu-1 IGR115 IGR114 IGR113 IGR112 TP0149 TP0143 amy1, - TP0147 dat, - TP0141 chrA, - TP0146 TP0145 TP0149 TP0143 amy1, - TP0147 dat, - TP0141 chrA, - TP0146 TP0145 Type: tandem, Name:  - 49 Type: tandem, Name:  - 46 Type: tandem, Name:  - 51 Type: tandem, Name:  - 47 Type: tandem, Name:  - 48 Type: tandem, Name:  - 50 Type: tandem, Name:  - 233 TP0143 amy1, - TP0147 TP0148 TP0142 tbpA, - TP0144 TP0142 tbpA, - TP0144 TP0149 TP0148 dat, - TP0141 chrA, - TP0146 TP0145
* Calculated from Protein Sequence

Gene ID: TP0145

DNA Molecule Name:
1  

Genbank ID:
3322408

Gene Name:


Definition:
long-chain-fatty-acid--CoA ligase

Gene Start:
165904

Gene Stop:
167871

Gene Length:
1968

Molecular Weight*:
72215

pI*:
7.69

Net Charge*:
5.00

EC:
6.2.1.3  

Functional Class:
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Miscellaneous Enzymes

Secondary Evidence:
Weimar JD, DiRusso CC, Delio R, Black PN.
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. 2002 Aug;277(33):29369-76.
PMID: 12034706

Yoo JH, Cheng OH, Gerber GE.
Determination of the native form of FadD, the Escherichia coli fatty acyl-CoA synthetase, and characterization of limited proteolysis by outer membrane protease OmpT.
Biochem J. 2001 Dec;360(Pt 3):699-706.
PMID: 11736662

Comment:
In E. coli this protein is involved in esterification, concomitant with
transport, of exogenous long-chain fatty acids into metabolically active
CoA thioesters for subsequent degradation or incorporation into
phosopholipids. This enzyme requires magnesium as a cofactor.

Reaction:
ATP + A LONG-CHAIN CARBOXYLIC ACID + COA =
AMP + PYROPHOSPHATE + AN ACYL-COA.

Blast Summary:  PSI-Blast Search
There are many significant hits to both prokaryotic and eukaryotic
long-chain-fatty-acid CoA ligases in the database both after gapped
BLAST and several iterations of PSI-BLAST. For example residues
15-656 are 37% similar to the long-chain-fatty-acid CoA ligase of
Borrelia burgdorferi, (accession# AE001161).

COGS Summary:  COGS Search
BeTs to 8 clades of COG1022
COG name: Long-chain acyl-CoA synthetases (AMP-forming)
Functional Class:? I
The phylogenetic pattern of COG1022 is a---Yq-c--Rh----Ol---
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
Residues 213-224 represent a significant (99%) hit to blocks (BL00455),
Putative AMP-binding domain proteins.

ProDom Summary:  Protein Domain Search
Residues 213-312 are 38% similar to LONG-CHAIN-FATTY-ACID--COA LIGASE 1
of LCFA_HUMAN. Residues 374-402, 380-457, 460-511, 481-536, 550-655
and 199-260 also match CoA ligases.

Paralogs:  Local Blast Search
There is no evidence of paralogs in T. pallidum.

Pfam Summary:  Pfam Search
Residues 48 to 550 (E-value = 7.4e-89) place TP0145 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
361  
379

PDB Hit:
gi|2098485|pdb|1LCI| Firefly Luciferase Oxidoreductase, Monooxygenase, Photoprotein, Luminescence Mol_id: 1; Molecule: Luciferase; Chain: Null; Ec: 1.13.12.7; Engineered: Yes

Gene Protein Sequence:
MSVCCTSSEERIERSKNLVHLVAQVAGAYAQLPAQYAKSSSGVFEITSFS
SFYEHVCLFAAGLASIGCGRGDCIGLISDNRVEWLHASFGIQALGAADVP
RGSDATERDLVQILGAVEARTVIVENDAQLKKLARCFDALPSVSQIVLLD
AGGAYQAMKDEFVQNEDGSARKCSFFTYQDILAHGTQFRVHHPGRIEDEI
GRTTRADVATIIFTSGTTGTPKGVVLSHENFLCQLIDISRRLTVCPGDIA
LSVLPVWHVFERISEYVVLSHAGGVAYSKPVGSVMLADLAKLNPHFLPSV
PRIWEAIHDGIFKNVRKKGGVAAALFHFFLAAGKAYAYFYRSVFGLRTHT
TRRAQFCAPLFACVPWLLLVPLHFLGNVLVFRKVRKKFGTSFKTAISGGG
ALPPNVDEFLYAIGVRVLEGYGLTETAPVIAMRSERRPVFGSVGTPCAYN
EVKIVDDTGAQLPVGYKGIVLVRGKNIMQGYYKNPELTAQVLDADGWFNT
GDIGYRCVGGQIVLRGRKKDTVVLRGGENVEPVPLEMSMQESRFIARAVV
VGQDERYLAALIVPDEAELRLWAEAQELRTECMEELLVNPAVVKFFEQEI
AKRISLENGFKIFERINRFVLLPKVFEVGVELSAKQEVMRHRVADLYAKE
IAQLFS

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTGTGTGTTGTACGTCCTCCGAAGAGCGGATTGAACGGAGCAAGAA
TCTCGTTCACCTTGTCGCGCAGGTTGCTGGTGCGTACGCGCAGCTGCCTG
CTCAGTATGCTAAAAGTAGCTCAGGAGTCTTTGAAATTACTTCTTTTTCC
TCGTTTTACGAGCATGTTTGCCTGTTTGCCGCGGGTCTGGCCAGCATTGG
GTGTGGTCGTGGTGATTGCATTGGTTTGATTTCCGACAATCGGGTTGAGT
GGCTCCACGCGAGCTTTGGTATTCAGGCGCTTGGTGCAGCAGACGTCCCG
CGTGGCTCTGACGCTACCGAGCGTGATCTTGTGCAGATTCTCGGTGCGGT
AGAGGCACGCACCGTAATTGTGGAGAATGACGCGCAGTTGAAAAAACTCG
CGCGGTGTTTTGATGCGTTGCCGAGCGTGTCGCAGATCGTGTTGTTGGAT
GCGGGCGGTGCGTACCAGGCGATGAAGGATGAGTTTGTCCAGAATGAGGA
CGGTTCTGCGCGGAAGTGCTCTTTTTTCACCTACCAGGACATACTCGCGC
ATGGGACACAGTTTCGGGTGCACCATCCAGGCAGGATAGAGGATGAGATT
GGGCGTACCACGCGCGCGGACGTTGCTACTATTATTTTCACATCCGGTAC
CACGGGCACCCCGAAGGGAGTGGTGCTTTCGCACGAGAATTTTCTTTGTC
AGTTAATCGATATCTCCCGCAGGCTGACCGTGTGTCCGGGGGATATCGCG
TTGTCAGTGTTGCCTGTGTGGCACGTTTTTGAGCGAATTAGCGAGTATGT
GGTACTGTCCCACGCAGGGGGCGTTGCTTACTCCAAGCCGGTAGGGTCGG
TGATGCTTGCGGATTTGGCAAAGCTTAATCCTCACTTTTTGCCTTCTGTG
CCTCGCATCTGGGAGGCCATTCACGATGGCATTTTCAAGAATGTGCGTAA
GAAAGGGGGTGTTGCTGCAGCACTTTTCCATTTCTTTTTGGCAGCAGGCA
AAGCGTACGCTTACTTTTACCGCAGCGTGTTTGGGCTGCGTACGCATACC
ACGCGTCGTGCGCAGTTTTGTGCGCCGCTGTTTGCCTGTGTGCCGTGGCT
CCTTTTAGTTCCTCTGCACTTTCTTGGAAATGTCTTGGTGTTCCGCAAGG
TACGGAAGAAGTTTGGTACCTCCTTTAAGACTGCTATCTCAGGGGGGGGC
GCGCTTCCTCCAAATGTGGATGAGTTTTTGTACGCTATTGGCGTGAGAGT
GCTTGAGGGGTACGGTCTGACGGAAACGGCGCCGGTAATTGCCATGCGCA
GTGAGCGCAGGCCAGTGTTCGGTTCCGTGGGTACACCCTGCGCGTACAAT
GAAGTGAAGATTGTGGATGACACTGGCGCCCAGCTTCCGGTGGGGTATAA
GGGGATAGTGCTTGTACGCGGCAAAAATATAATGCAGGGGTACTATAAAA
ATCCTGAGCTTACCGCGCAGGTGTTAGATGCAGACGGTTGGTTTAATACG
GGGGATATTGGCTACCGCTGCGTGGGTGGACAGATTGTGTTACGGGGACG
TAAGAAGGATACGGTTGTGCTGCGTGGTGGAGAGAACGTGGAGCCAGTTC
CCCTCGAAATGAGTATGCAGGAGTCCCGTTTTATTGCGCGTGCAGTGGTA
GTCGGGCAAGATGAGCGGTATTTGGCGGCGTTGATAGTTCCGGACGAGGC
AGAGCTGCGGCTGTGGGCAGAGGCGCAGGAACTCCGCACAGAGTGCATGG
AAGAATTGCTAGTAAATCCTGCAGTGGTGAAGTTTTTCGAGCAGGAAATA
GCAAAGCGGATATCACTCGAGAACGGGTTTAAGATATTCGAGCGGATTAA
CCGTTTTGTGCTTCTGCCGAAGGTCTTTGAAGTGGGAGTGGAGCTTTCCG
CAAAGCAGGAGGTAATGCGCCACCGGGTCGCCGACCTGTACGCAAAGGAG
ATCGCGCAGCTCTTTTCC


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