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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR103 IGR97 IGR102 IGR105 IGR106 IGR100 IGR101 IGR98 IGR107 IGR99 IGR108 IGR104 CT120 adk, - CT128 incA, - CT119 ydhO, - CT127 CT117 rs9, - CT126 CT116 rl13, - CT125 accB, - CT123 CT118 glnP, - CT129 rpe,araD, - CT121 glnQ, - CT130 accC, - CT124 CT120 adk, - CT128 incA, - CT119 ydhO, - CT127 CT117 rs9, - CT126 CT116 rl13, - CT125 accB, - CT123 CT118 glnP, - CT129 rpe,araD, - CT121 glnQ, - CT130 accC, - CT124 CT120 adk, - CT128 incA, - CT119 ydhO, - CT127 rs9, - CT126 CT116 rl13, - CT125 accB, - CT123 CT118 glnP, - CT129 rpe,araD, - CT121 glnQ, - CT130 accC, - CT124 efp1, - CT122 efp1, - CT122 CT117
* Calculated from Protein Sequence

Gene ID: CT124

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
accC  

Definition:
biotin carboxylase

Gene Start:
139898

Gene Stop:
141268

Gene Length:
1371

Molecular Weight*:
50190

pI*:
7.41

Net Charge*:
2.02

EC:
 

Functional Class:
fatty acid and phospholipid metabolism  

Pathway: pathway table

Comment:
Active in the first step of long-chain fatty acid synthesis.
See CT123, CT265, and CT293.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to biotin carboxylase proteins, e.g., 54% similarity to ACCC_METJA, 51% similarity to ACCC_ANASP.
CT124 is weakly similar to TP0695 in T.pallidum, a predicted phosphoribosylglycinamide formyltransferase. No similarity to
M.genitalium.

CT124 is orthologous to CPn0182: residues 1-450 are 88% similar to CPn0182.

COGS Summary:  COGS Search
BeTs to 12 clades of COG0439
COG name: Biotin carboxylase
Functional Class:  I
The phylogenetic pattern of COG0439 is amt-YQ-CeBRhuj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 6-19, 109-122, 327-340, 197-242, 284-307 are significantly matched to blocks BL00866A,B,C, concerned with Carbamoyl-phosphate synthase subdomain proteins, e.g. ACCC_METJA.
Residues 206-242, 259-295 are significantly matched to blocks BL00188, concerned with biotin-requiring enzymes attachment site proteins, e.g. BCCA_MYCTU.


ProDom Summary:  Protein Domain Search
Residues 332-431 are 60% similar to a carboxylase domain as observed in ACCC_HAEIN. Residues 16-90 are consistent with this observation.
Residues 191-317 are 59% similar to a carbamoyl-phosphate carboxylase domain as seen in ACCC_METJA.

Paralogs:  Local Blast Search
CT124 is paralogously related to CT762, a MUR-NAc-L-alanine and D-alanine-D-alanine ligase(fusion protein?): residues 74-289 are 23% similar to CT762.

Pfam Summary:  Pfam Search
Residues 1 to 112 (E-value = 1.1e-46) place CT124 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain (PF00289)
Residues 114 to 328 (E-value = 5.9e-99) place CT124 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786)
Residues 335 to 441 (E-value = 1.5e-64) place CT124 in the Biotin_carb_C family which is described as Biotin carboxylase C-terminal domain (PF02785)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
113  
190

PDB Hit:
gi|1127198|pdb|1BNC|A Chain A, Mol_id: 1; Molecule: Biotin Carboxylase; Chain: A, B; Ec: 6.3.4.14

Gene Protein Sequence:
MKKVLIANRGEIAIRIIRACHDLGLATVAVYSMADQEALHVLLADEAVCI
GEAQAAKSYLKIANILAACEITGVDAVHPGYGFLSENANFASICESCGLT
FIGPSAESIATMGDKVAAKQLAKKIKCPVIPGSEGVVKDEVEGIRIAEKI
GFPIVIKAVAGGGGRGIRIVREKDEFYRAFTAARAEAEAGFNNPDVYIEK
FIENPRHLEVQVIGDKHGNYVYLGERDCTVQRRRQKLIEETPSPILTPEM
RAKVGKVAVDLARSAGYFSVGTVEFLLDKEKRFYFMEMNTRIQVEHTITE
EVTGIDLLKAQISVAKGEKLPWKQKNIKFKGHVIQCRINAEDPINNFTPS
PGRLDYYLPPAGPAVRVDGACYSGYAIPPYYDSMIAKVITKGKNREEAIA
IMKRALKEFHIGGVHSTIPFHQFMLDNPKFLLSDYDINYVDQLLASGSTF
LNLADGS

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAGAAAGTATTGATTGCAAATAGAGGCGAGATAGCTATTCGGATTAT
TCGAGCATGTCATGATCTAGGATTAGCTACTGTTGCTGTATATTCTATGG
CGGATCAAGAAGCTTTGCATGTGCTTCTTGCTGACGAAGCTGTTTGTATT
GGAGAAGCTCAGGCAGCAAAATCCTACCTAAAGATCGCCAATATTTTAGC
TGCTTGTGAGATTACTGGGGTAGATGCTGTGCATCCTGGTTATGGTTTCT
TAAGTGAAAATGCAAACTTTGCTTCTATTTGTGAAAGTTGTGGGCTCACA
TTTATCGGTCCTAGTGCTGAGTCGATAGCGACTATGGGAGATAAAGTCGC
AGCTAAGCAGTTGGCTAAAAAGATTAAGTGCCCTGTAATCCCTGGATCTG
AAGGTGTAGTGAAGGATGAGGTGGAAGGGATTAGAATTGCAGAAAAGATC
GGATTCCCCATCGTCATCAAAGCTGTTGCTGGAGGCGGTGGACGAGGAAT
ACGGATTGTTAGAGAAAAAGACGAATTCTACAGGGCTTTTACTGCCGCTC
GGGCTGAAGCAGAAGCGGGATTTAATAATCCTGACGTGTATATTGAAAAA
TTTATTGAAAATCCAAGACATTTAGAAGTTCAAGTAATTGGAGATAAGCA
CGGAAATTACGTGTATCTTGGAGAACGAGATTGTACAGTACAAAGGCGTC
GGCAAAAATTAATAGAAGAGACTCCAAGTCCTATTTTAACTCCAGAAATG
CGAGCTAAAGTTGGAAAAGTAGCAGTGGATTTAGCTCGGAGTGCCGGGTA
TTTCTCTGTTGGAACAGTAGAATTTCTGTTAGATAAGGAGAAGCGTTTTT
ATTTCATGGAGATGAATACGCGTATCCAAGTGGAACATACTATTACGGAA
GAAGTGACAGGGATCGATTTGTTAAAGGCTCAGATTAGTGTCGCTAAGGG
AGAAAAACTGCCTTGGAAGCAAAAGAATATAAAGTTTAAAGGGCACGTGA
TTCAATGCCGAATCAATGCAGAGGATCCAATTAATAACTTTACTCCTTCC
CCTGGTAGATTAGATTATTATCTCCCTCCTGCAGGTCCTGCTGTGCGAGT
AGACGGGGCTTGCTACAGTGGTTATGCGATACCTCCTTATTATGATTCCA
TGATTGCTAAGGTAATCACAAAAGGAAAGAATCGAGAGGAAGCGATAGCC
ATTATGAAAAGAGCTTTAAAAGAGTTCCATATTGGTGGGGTGCATTCTAC
AATTCCTTTTCATCAGTTCATGTTGGATAATCCGAAGTTTCTTCTTTCTG
ATTATGATATTAATTACGTGGACCAGCTTTTAGCGTCTGGTAGCACCTTT
TTAAATTTAGCTGATGGCAGC


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