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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR266 IGR271 IGR267 IGR272 IGR268 IGR270 IGR273 IGR269 HD0376 ansB, - HD0372 HD0374 luxS, - HD0370 HD0375 HD0371 pyrG, - HD0373 pqiB, - HD0369 HD0376 ansB, - HD0372 HD0374 luxS, - HD0370 HD0375 HD0371 pyrG, - HD0373 pqiB, - HD0369 HD0376 ansB, - HD0372 HD0374 luxS, - HD0370 HD0375 HD0371 pyrG, - HD0373 pqiB, - HD0369
* Calculated from Protein Sequence

Gene ID: HD0372

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
ansB  

Definition:
L-asparaginase II precursor

Gene Start:
291759

Gene Stop:
290710

Gene Length:
1050

Molecular Weight*:
37443

pI*:
6.70

Net Charge*:
-0.88

EC:
3.5.1.1  

Functional Class:
Energy metabolism; Amino acids and amines  

Pathway: pathway table
Alanine and aspartate metabolism
Cyanoamino acid metabolism
Nitrogen metabolism

Secondary Evidence:
Scott S, Busby S, Beacham I.
Transcriptional co-activation at the ansB promoters: involvement of the activating regions of CRP and FNR when bound in tandem.
Mol Microbiol. 1995 Nov;18(3):521-31.
PMID: 8748035

Jennings MP, Scott SP, Beacham IR.
Regulation of the ansB gene of Salmonella enterica.
Mol Microbiol. 1993 Jul;9(1):165-72.
PMID: 8412661

Jennings MP, Beacham IR.
Co-dependent positive regulation of the ansB promoter of Escherichia coli by CRP and the FNR protein: a molecular analysis.
Mol Microbiol. 1993 Jul;9(1):155-64.
PMID: 8412660

Harms E, Wehner A, Jennings MP, Pugh KJ, Beacham IR, Rohm KH.
Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts.
Protein Expr Purif. 1991 Apr-Jun;2(2-3):144-50.
PMID: 1821783

Bonthron DT.
L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene.
Gene. 1990 Jul 2;91(1):101-5.
PMID: 2144836

Jennings MP, Beacham IR.
Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins.
J Bacteriol. 1990 Mar;172(3):1491-8.
PMID: 2407723

Comment:
0

Blast Summary:  PSI-Blast Search
Residues 1 to 349 are 78% ( EScore : 1e-155 ) identical to sp|P43843|ASG2_HAEIN PROBABLE L-ASPARAGINASE PERIPLASMIC PRECURSOR >1074950|pir||A64090 asparaginase between residues 1 and 349 in [Haemophilus influenzae Rd]
Residues 5 to 349 are 64% ( EScore : 1e-125 ) identical to sp|P00805|ASG2_ECOLI L-ASPARAGINASE II PRECURSOR between residues 6 and 348 in [Escherichia coli]
Residues 21 to 349 are 65% ( EScore : 1e-124 ) identical to gb|AAA62276.1| (U06943) chimeric immunoglobulin-L-asparaginase between residues 287 and 615 in [synthetic construct]
Residues 24 to 349 are 66% ( EScore : 1e-124 ) identical to pdb|3ECA|A between residues 1 and 326
Residues 24 to 349 are 65% ( EScore : 1e-123 ) identical to pdb|4ECA|A between residues 1 and 326
Residues 24 to 349 are 65% ( EScore : 1e-116 ) identical to prf||742507A asparaginase between residues 1 and 321 in [Escherichia coli]
Residues 25 to 349 are 50% ( EScore : 7e-88 ) identical to sp|P50286|ASPG_WOLSU L-ASPARAGINASE between residues 4 and 330 in [Wolinella succinogenes]
Residues 21 to 349 are 48% ( EScore : 2e-81 ) identical to sp|Q9ZLB9|ASPG_HELPJ L-ASPARAGINASE between residues 2 and 332 in [Helicobacter pylori J99]
Residues 21 to 349 are 49% ( EScore : 2e-80 ) identical to sp|O25424|ASPG_HELPY L-ASPARAGINASE between residues 2 and 330 in [Helicobacter pylori 26695]
Residues 27 to 349 are 50% ( EScore : 5e-78 ) identical to emb|CAB72522.1| (AL139074) cytoplasmic L-asparaginase between residues 8 and 331 in [Campylobacter jejuni]

COGS Summary:  COGS Search
BeTs to 9 clades of COG0252
COG name: L-asparaginase
Functional Class: E
The phylogenetic pattern of COG0252 is amtKY---EBrhuj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000267 (Asparaginase/glutaminase family) with a combined E-value of 1.5e-91.
    IPB000267A    24-40
    IPB000267B    58-96
    IPB000267C    104-148
    IPB000267D    155-196
    IPB000267E    320-346


ProDom Summary:  Protein Domain Search
Residues 26-92 are 47% similar to a (GLUTAMINASE-ASPARAGINASE PROTEOME) protein domain (PD413140) which is seen in ASPQ_ACIGL.

Residues 27-189 are 84% similar to a (L-ASPARAGINASE HYDROLASE COMPLETE PROTEOME L-ASPARAGINE) protein domain (PD003221) which is seen in ASG2_HAEIN.

Residues 200-346 are 72% similar to a (L-ASPARAGINASE HYDROLASE AMIDOHYDROLASE L-ASPARAGINE) protein domain (PD244538) which is seen in ASG2_HAEIN.



Paralogs:  Local Blast Search
HD0372 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 35 to 344 (E-value = 1.7e-162) place HD0372 in the Asparaginase family which is described as Asparaginase (PF00710)

PDB Hit:
pdb|3ECA|A Chain A, Asparaginase Type Ii (E.C.3.5.1.1) (Eca) >g... 445 4e-126
pdb|4ECA|A Chain A, Asparaginase From E. Coli, Mutant T89v With... 441 6e-125
pdb|1WSA|B Chain B, Structure Of L-Asparaginase Ii Precursor >g... 324 9e-090

Gene Protein Sequence:
MKLTKLALSTLFALGLSTAYANKLPNITILATGGTIAGSGESAVSSAYQA
GQLNIDTLIEAVPEMKKLANIKGEQVVKIGSQDMNDQVWLTLANTINQQC
ASTDGFVITHGTDTMEETAYFLDMTAKCEKPIVLVGAMRPATEKSADGPL
NLYNAIVVAREAKSAKRGVLVAMNDQVLGARDVTKTSTTAVQTFHSPNFG
ALGYIHNSKVDYERNPESKHTTNTPFDVTKLTDLPKVGIIYAYANMPTEP
LKALLDADYQGIVVAGVGNGNMNAENLALLETAAKKGVAVIRSSRVPTGY
TTRDAEIDDSKYGFAASGTLNPQKARVLLQLALTKTKDIHTIQQYFEEF$


Gene Nucleotide Sequence:  Sequence Viewer
ATGAAATTGACTAAATTAGCGCTTTCCACTTTATTTGCATTAGGATTATC
TACCGCTTACGCCAACAAGCTCCCGAATATCACGATCCTAGCCACCGGTG
GCACGATCGCTGGTAGCGGTGAAAGTGCCGTCAGCTCTGCTTATCAAGCT
GGACAACTGAATATTGACACGCTGATTGAAGCGGTTCCAGAAATGAAAAA
ATTAGCAAATATCAAAGGCGAACAAGTGGTTAAAATTGGCTCACAAGATA
TGAATGATCAAGTTTGGTTAACATTAGCCAACACGATCAACCAACAATGT
GCTTCTACTGATGGCTTTGTGATCACACACGGCACAGATACGATGGAAGA
AACCGCTTATTTCCTAGATATGACCGCTAAATGCGAAAAACCGATTGTCT
TAGTTGGCGCTATGCGCCCTGCAACCGAAAAAAGTGCTGATGGCCCACTT
AATTTATATAATGCCATCGTAGTGGCACGAGAAGCTAAATCCGCCAAACG
TGGCGTGTTAGTTGCAATGAATGATCAAGTACTTGGCGCACGAGACGTCA
CTAAAACAAGCACAACGGCTGTCCAAACCTTTCATTCACCAAATTTTGGC
GCTTTAGGTTATATTCATAATAGTAAAGTCGATTATGAACGTAATCCTGA
AAGCAAGCATACAACCAACACACCATTTGATGTAACCAAATTAACTGATT
TGCCTAAAGTCGGCATTATTTACGCCTATGCAAATATGCCAACGGAGCCA
TTAAAAGCATTATTAGATGCTGATTATCAAGGTATTGTGGTTGCGGGAGT
TGGCAATGGTAATATGAATGCCGAAAACTTAGCACTACTCGAAACAGCAG
CTAAAAAAGGCGTTGCCGTTATTCGCTCATCGCGTGTTCCAACCGGTTAT
ACCACACGCGATGCTGAAATTGATGATTCAAAATATGGCTTTGCTGCATC
TGGTACACTTAATCCACAAAAAGCCCGCGTATTGTTACAATTAGCATTAA
CGAAAACAAAAGATATCCATACTATCCAACAATATTTTGAAGAATTTTAA



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