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

Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR609 IGR607 IGR608 IGR604 IGR603 IGR602 IGR605 IGR606 nudE, - HD0841 recF, - HD0849 dnaN, - HD0850 asd, - HD0847 lpxB, - HD0846 dnaA, - HD0851 hslR, - HD0842 sodC, - HD0848 hslO,hsp33, - HD0843 nudE, - HD0841 recF, - HD0849 dnaN, - HD0850 asd, - HD0847 lpxB, - HD0846 dnaA, - HD0851 hslR, - HD0842 sodC, - HD0848 hslO,hsp33, - HD0843 nudE, - HD0841 recF, - HD0849 dnaN, - HD0850 asd, - HD0847 lpxB, - HD0846 dnaA, - HD0851 sohB, - HD0845 sohB, - HD0845 hslR, - HD0842 sodC, - HD0848 hslO,hsp33, - HD0843
* Calculated from Protein Sequence

Gene ID: HD0847

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
asd  

Definition:
aspartate semialdehyde dehydrogenase

Gene Start:
675329

Gene Stop:
674211

Gene Length:
1119

Molecular Weight*:
40996

pI*:
5.40

Net Charge*:
-4.54

EC:
1.2.1.11  

Functional Class:
Amino acid biosynthesis; Aspartate family  

Pathway: pathway table
Glycine, serine and threonine metabolism
Lysine biosynthesis

Primary Evidence:
Langford,P.R. and Kroll,J.S.
Distribution, cloning, characterisation and mutagenesis of sodC,
the gene encoding copper/zinc superoxide dismutase, a potential
determinant of virulence, in Haemophilus ducreyi
FEMS Immunol. Med. Microbiol. 17 (4), 235-242 (1997)
MEDLINE: 97288949


Secondary Evidence:
Haziza,C., Stragier,P. and Patte,J.C.
Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal
EMBO J. 1 (3), 379-384 (1982)
M:84182485

Karsten,W.E. and Viola,R.E.
Identification of an essential cysteine in the reaction catalyzed
by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli
Biochim. Biophys. Acta 1121 (1-2), 234-238 (1992)
M:92287957

James CL, Viola RE.
Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway.
Biochemistry. 2002 Mar 19;41(11):3726-31.
PMID: 11888290

James CL, Viola RE.
Production and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate
pathway.
Biochemistry. 2002 Mar 19;41(11):3720-5.
PMID: 11888289


Comment:


Blast Summary:  PSI-Blast Search
Thie sequence corresponds to the previously reported gi 1418710 in GenBank.

Many significant hits using gapped BLAST to aspartate semialdehyde dehydrogenase from H. influenzae (1169296), Salmonella typhimurium (3121984), E. coli (118510), among others. HD0847 is 83% similar to residues 1-369 from DHAS_HAEIN.

No similarities to C. trachomatis, C. pneumoniae, U. urealyticum, T. pallidum, M. genitalium, or M. pneumoniae.


COGS Summary:  COGS Search
BeTs to 12 clades of COG0136
COG name: Aspartate-semialdehyde dehydrogenase
Functional Class: E
The phylogenetic pattern of COG0136 is amtkyqvcEbrHuj----inx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB000319 (Aspartate-semialdehyde dehydrogenase) with a combined E-value of 1.1e-53.
    IPB000319A    4-15
    IPB000319C    65-81
    IPB000319D    95-116
    IPB000319E    159-169
    IPB000319F    243-256
    IPB000319G    264-284
    IPB000319H    319-338
    IPB000319I    352-366
***** IPB000534 (Semialdehyde dehydrogenase) with a combined E-value of 2e-06.
    IPB000534A    68-85
    IPB000534B    267-279
    IPB000534A    131-148
    IPB000534B    352-364


ProDom Summary:  Protein Domain Search
Residues 135-299 are 64% similar to a (DEHYDROGENASE BIOSYNTHESIS) protein domain (PD002095) which is seen in DHAS_NEIMB.

Residues 4-134 are 82% similar to a (DEHYDROGENASE BIOSYNTHESIS) protein domain (PD011448) which is seen in DHAS_HAEIN.

Residues 135-301 are 82% similar to a (DEHYDROGENASE BIOSYNTHESIS) protein domain (PD376765) which is seen in DHAS_HAEIN.

Residues 302-366 are 90% similar to a (DEHYDROGENASE BIOSYNTHESIS) protein domain (PD240221) which is seen in DHAS_HAEIN.



Paralogs:  Local Blast Search
HD0847 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 1 to 132 (E-value = 1.1e-44) place HD0847 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain (PF01118)
Residues 145 to 356 (E-value = 5.3e-77) place HD0847 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain (PF02774)

PDB Hit:
pdb|1BRM|C Chain C, Aspartate Beta-Semialdehyde Dehydrogenase F... 534 6e-153

Gene Protein Sequence:
MQNVGFIGWRGMVGSVLMDRMVQENDFANINPIFFTTSQVGQKAPYLADK
ETGDLKNAFDIEELKKLDIIVTCQGGDYTTEVYPKLRATGWNGCWIDAAS
TLRMQDDAVIVLDPVNQQVITENLKKGIKTFVGGNCTVSLMLMAIGGLFE
KGLVEWVSVATYQAASGAGARNMRELLTQMGILEKTVQTTLADPATCILA
IERKVTDIMRDDSFPIEHFGAPLAGSLIPWIDKLLPETGQTREEWKGYAE
TNKILGLTNQPIAVDGLCVRIGALRCHSQAFTIKLKKDLPLAEIEQIIAQ
HNEWVKVIPNDKEATLRELTPTKVTGTLAVPVGRLRKLAMGPEYLSAFTV
GDQLLWGAAEPIRRMLVQLTNN$

Gene Nucleotide Sequence:  Sequence Viewer
ATGCAAAATGTTGGTTTTATTGGTTGGCGTGGTATGGTCGGCTCAGTTTT
AATGGATCGTATGGTCCAAGAAAACGACTTTGCAAACATTAATCCCATTT
TTTTCACGACCTCACAAGTCGGTCAAAAAGCGCCTTATTTAGCTGATAAA
GAAACAGGCGACTTAAAAAATGCGTTTGATATTGAAGAACTTAAAAAGTT
AGACATTATCGTCACGTGCCAAGGTGGTGATTACACCACTGAAGTTTACC
CTAAATTACGTGCAACAGGTTGGAATGGCTGTTGGATTGATGCCGCGTCA
ACACTACGTATGCAAGATGATGCAGTTATCGTGTTAGACCCTGTTAACCA
ACAAGTTATTACAGAAAATCTAAAAAAAGGAATAAAAACTTTTGTTGGTG
GTAACTGTACCGTTAGCTTAATGCTAATGGCAATCGGCGGTTTATTCGAA
AAAGGCTTAGTGGAATGGGTCTCTGTTGCAACCTATCAGGCAGCCTCAGG
GGCCGGTGCGCGGAATATGCGTGAATTACTGACACAAATGGGTATTCTAG
AAAAAACTGTTCAGACGACGTTAGCAGATCCCGCCACGTGTATTTTAGCA
ATTGAGCGAAAAGTAACAGATATAATGCGTGATGATAGCTTTCCTATTGA
GCATTTTGGTGCACCATTAGCAGGCAGTCTAATTCCTTGGATTGATAAAT
TATTACCAGAAACGGGGCAAACTAGAGAAGAATGGAAAGGCTATGCCGAA
ACAAATAAAATTCTTGGCTTAACGAATCAACCTATTGCAGTAGATGGCTT
ATGTGTACGAATTGGTGCTTTACGTTGTCACAGCCAAGCATTTACCATCA
AACTCAAAAAAGATTTACCATTAGCTGAAATTGAGCAAATCATTGCCCAA
CATAATGAATGGGTAAAAGTGATTCCAAATGATAAAGAAGCCACACTACG
TGAATTAACGCCAACCAAAGTGACAGGCACATTAGCTGTTCCTGTAGGGC
GGCTACGTAAATTAGCAATGGGGCCTGAATATTTATCCGCATTCACGGTT
GGCGATCAATTATTGTGGGGAGCAGCAGAACCTATTCGCCGGATGTTAGT
ACAATTAACCAATAATTAA


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