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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR703 IGR707 IGR706 IGR704 IGR702 IGR700 IGR705 IGR701 IGR698 IGR699 HD0977 fstE, - HD0982 fstX, - HD0981 ftsY, - HD0984 mfd, - HD0975 HD0986 folQ,folA, - HD0978 hpaB, - HD0987 HD0985 cda,cdd, - HD0979 pepN, - HD0976 HD0977 fstE, - HD0982 fstX, - HD0981 ftsY, - HD0984 mfd, - HD0975 HD0986 folQ,folA, - HD0978 hpaB, - HD0987 HD0985 cda,cdd, - HD0979 pepN, - HD0976 HD0977 fstE, - HD0982 fstX, - HD0981 ftsY, - HD0984 mfd, - HD0975 folQ,folA, - HD0978 hpaB, - HD0987 HD0985 cda,cdd, - HD0979 pepN, - HD0976 HD0986
* Calculated from Protein Sequence

Gene ID: HD0979

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
cda  cdd  

Definition:
cytidine deaminase

Gene Start:
776340

Gene Stop:
777239

Gene Length:
900

Molecular Weight*:
32464

pI*:
6.60

Net Charge*:
-2.74

EC:
3.5.4.5  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Salvage of nucleosides and nucleotides  

Pathway: pathway table
Pyrimidine metabolism

Secondary Evidence:
Petersen-Mahrt SK, Harris RS, Neuberger MS.
AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification.
Nature. 2002 Jul 4;418(6893):99-103.
PMID: 12097915

Betts,L., Xiang,S., Short,S.A., Wolfenden,R. and Carter,C.W. Jr.
Cytidine deaminase. The 2.3 A crystal structure of an enzyme:
transition-state analog complex
J. Mol. Biol. 235 (2), 635-656 (1994)
M:94118314

Xiang,S., Short,S.A., Wolfenden,R. and Carter,C.W. Jr.
Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis
Biochemistry 35 (5), 1335-1341 (1996)
M:96223623


Comment:
0

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to cytidine deaminase protein; e.g. residues 20-299 are 48% similar to (U32814) cytidine deaminase of Haemophilus influenzae, residues 10-272 are 49% similar to (M60916) cytidine deaminase of Escherichia coli, residues 87-251 are 67% similar to [95735] cytidine deaminase of Escherichia coli.

COGS Summary:  COGS Search
BeTs to 7 clades of COG0295
COG name: Cytidine deaminase
Functional Class:  F
The phylogenetic pattern of COG0295 is ----y-v-ebrh--gpo----
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 147-299 are 41% similar to a (CYTIDINE DEAMINASE HYDROLASE COMPLETE) protein domain (PD021108) which is seen in Q9CP11_PASMU.

Residues 65-147 are 74% similar to a (CYTIDINE HYDROLASE DEAMINASE ZINC) protein domain (PD081080) which is seen in CDD_HAEIN.

Residues 69-146 are 58% similar to a (CYTIDINE DEAMINASE HYDROLASE PROTEOME) protein domain (PD003466) which is seen in Q9KSM5_VIBCH.



Paralogs:  Local Blast Search
HD0979 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 56 to 157 (E-value = 2.9e-19) place HD0979 in the dCMP_cyt_deam family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region (PF00383)

PDB Hit:
pdb|1CTT| Cytidine Deaminase (Cda) (E.C.3.5.4.5) Complexed Wi... 235 7e-063

Gene Protein Sequence:
MTMPTLSALQHRLAQLAEQKNEPLTLAIIEQLKQQSYQGALSAPLVQQFC
QQFSLSKIELGLGCVPIAACYALTPVSHFCVGAVAIGLSGSFYFGANQEF
AGIAMQQTVHAEQSAISHAWLAGEGAISDMVVNCTPCGHCRQFMNELNTA
TTLQIHLPHRQHNTLQQYLIDAFGPKDLNIANVLFDQQHIVLPLQGDALV
QATIKEAQQAYAPYSQAVSAVALQVGEQIICGRYAENAAFNPSLLPLQSA
LNYRRFLGLSDVAVSRVVMVEKRAVLSHYHMSKALAETALGLTLEYIAV$


Gene Nucleotide Sequence:  Sequence Viewer
ATGACTATGCCAACTTTATCTGCACTTCAACATCGATTAGCGCAGTTAGC
AGAACAGAAAAATGAACCGCTTACATTAGCAATTATTGAACAGCTTAAAC
AGCAATCTTATCAAGGTGCATTATCCGCACCACTAGTGCAACAATTTTGT
CAGCAATTTTCGTTATCTAAAATTGAATTAGGCTTAGGTTGTGTACCTAT
TGCAGCTTGTTACGCATTGACACCCGTGTCACATTTTTGTGTGGGGGCTG
TTGCTATAGGGCTATCAGGCAGTTTTTATTTTGGCGCTAACCAAGAATTT
GCAGGGATCGCAATGCAACAAACTGTACACGCCGAACAAAGTGCGATCTC
ACATGCTTGGCTTGCTGGCGAAGGGGCAATCAGTGATATGGTGGTAAATT
GCACCCCTTGTGGGCATTGCCGTCAGTTTATGAATGAATTAAACACCGCT
ACAACATTGCAAATTCACTTACCACATCGGCAACACAATACATTACAACA
ATATTTAATTGATGCCTTTGGGCCGAAAGATCTAAATATTGCCAATGTAT
TGTTTGATCAACAACACATAGTGCTACCTTTACAAGGCGATGCACTAGTC
CAAGCGACGATCAAGGAAGCACAACAGGCTTATGCACCTTATAGTCAAGC
AGTCAGTGCAGTCGCATTACAAGTAGGGGAGCAAATAATTTGTGGTCGTT
ATGCAGAAAATGCGGCGTTTAATCCCAGTTTGTTACCATTACAAAGTGCA
TTAAATTATCGCCGATTTTTAGGTTTATCTGATGTGGCGGTCAGTCGTGT
CGTGATGGTGGAAAAACGAGCAGTGCTAAGCCATTATCATATGAGTAAAG
CCTTAGCTGAAACAGCATTGGGATTAACGCTAGAGTACATAGCGGTTTAA



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