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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0465.2 IGR0462 IGR0463 IGR0461 IGR0465.3 IGR0465 IGR0464 IGR0465.1 IGR0460 IGR0459 NG0557 NG0558 aspA, - NG0556 NG0560 fcuA, - NG0560.1 tpn, - NG0559 NG0554 NG0560.2 NG0555 NG0561 tdfF,tonB, - NG0553 NG0557 NG0558 aspA, - NG0556 NG0560 fcuA, - NG0560.1 tpn, - NG0559 NG0554 NG0560.2 NG0555 NG0561 tdfF,tonB, - NG0553 NG0558 aspA, - NG0556 NG0557 NG0560 fcuA, - NG0560.1 tpn, - NG0559 NG0554 NG0555 NG0561 tdfF,tonB, - NG0553 NG0560.2
* Calculated from Protein Sequence

Gene ID: NG0556

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
aspA  

Definition:
aspartate ammonia-lyase

Gene Start:
535895

Gene Stop:
534501

Gene Length:
1395

Molecular Weight*:
50682

pI*:
5.30

Net Charge*:
-7.99

EC:
4.3.1.1  

Functional Class:
Central intermediary metabolism; Nitrogen metabolism  
Energy metabolism; TCA cycle  

Pathway: pathway table
Alanine and aspartate metabolism
Nitrogen metabolism

Secondary Evidence:
Takagi,J.S., Ida,N., Tokushige,M., Sakamoto,H. and Shimura,Y.
Cloning and nucleotide sequence of the aspartase gene of Escherichia coli W.
Nucleic Acids Res. 13 (6), 2063-2074 (1985)
Medline: 85215599.

Woods,S.A., Miles,J.S., Roberts,R.E. and Guest,J.R.
Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12.
Biochem. J. 237 (2), 547-557 (1986)
Medline: 87099873.

Shi,W., Dunbar,J., Jayasekera,M.M., Viola,R.E. and Farber,G.K.
The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry 36 (30), 9136-9144 (1997)
Medline: 97375637.

Comment:
From GenBANK (gi:114272): AspA is a homotetramer that catalyzes the reaction: L-aspartate = fumarate + NH3.

From Medline (97375637): The enzyme contains three domains, and each domain is composed almost completely of alpha helices. The central domain is composed of five long helices. In the tetramer, these five helices form a 20-helix cluster. Such clusters have also been seen in delta-crystallin and in fumarase. The active site of aspartase has been located in a region that contains side chains from three different subunits.

For other 'asp' genes', see NG1452 (aspC), NG1490 (aspS), and NG1489 (aspS).

Oklahoma ID: NGO.556c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to aspartate ammonia-lyases; e.g. residues 4-463 are 78% similar to gb|AAC22191.1| (U32735) aspartate ammonia-lyase (aspA) of Haemophilus influenzae Rd.

Residues 1-465 are 98% similar to NMB1029 and NMA1459, aspartate ammonia-lyases, of N.meningitidis (11268843, 11268831).

COGS Summary:  COGS Search
BeTs to 4 clades of COG1027
COG name: Aspartate ammonia-lyase
Functional Class:  E
The phylogenetic pattern of COG1027 is ------v-eb-huj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000362 (Fumarate lyase) with a combined E-value of 2.8e-14.
    IPB000362A    186-199
    IPB000362B    318-328


ProDom Summary:  Protein Domain Search
Residues 185-459 are 83% similar to a (LYASE BIOSYNTHESIS ARGININOSUCCINATE FUMARATE HYDRATASE) protein domain (PD000660) which is seen in ASPA_HAEIN.

Residues 24-184 are 67% similar to a (LYASE FUMARATE HYDRATASE FUMARASE) protein domain (PD002097) which is seen in ASPA_HAEIN.



Paralogs:  Local Blast Search


NG0556 is paralogously related to NG1029 (fumarate hydratase (fumarase C)) (1e-101) and NG0219 (argininosuccinate lyase) (6e-13).


Pfam Summary:  Pfam Search
Residues 11 to 343 (E-value = 2.2e-149) place NG0556 in the Lyase_1 family which is described as Lyase (PF00206)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|1JSW|1JSW-A NATIVE L-ASPARTATE AMMONIA LYASE 679.0 0.000000
pdb|2FUS|2FUS-A MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN 327.0 2e-90
pdb|1KQ7|1KQ7-A E315Q MUTANT FORM OF FUMARASE C FROM E.COLI 326.0 4e-90
pdb|1FUR|1FUR-A FU

Gene Protein Sequence:
MTVRIEHDLLGDREIPAEVYWGIHTLRAIENFKISTQKISDVPQFVRSIV
MVKKATAQANGELGAVKPEIAAAIEKACDEVLLNNRCLDQFPSDVYQGGA
GTSVNMNTNEVIANLALEALGYEKGRYDIVNPMDHVNASQSTNDAYPTGF
RLAVYYSIGELLDKLTVLKNAFAAKAEAFKDVLKMGRTQLQDAVPMTAGQ
EFQSFQVLLEEEILNLDRTRQLLLEVNLGATAIGTGVNTPKGYAELVVKK
LSEVSGLPCKLTENLIEATSDCGAYVMVHGALKRTAVKLSKICNDLRLLS
SGPRAGLKEINLPELQAGSSIMPAKVNPVIPEVVNQVCFKVIGNDTTITF
AAESGQLQLNVMEPVIAQCMFETISLLGNAAVNLSDKCVKGITVNREICE
RYVFNSIGLVTYLNPYIGHRNGDLVGKICAQTGKGVREVVLERGLLSEEE
INRILSPENLMNPHL

Gene Nucleotide Sequence:  Sequence Viewer
ATGACTGTCCGTATCGAACACGATTTATTGGGCGACCGCGAGATTCCCGC
CGAAGTGTATTGGGGCATCCACACCCTGCGCGCCATTGAAAACTTTAAAA
TCTCCACACAAAAAATTTCCGACGTGCCGCAGTTTGTCCGCAGTATAGTG
ATGGTGAAAAAAGCAACCGCGCAGGCAAACGGCGAATTGGGTGCAGTAAA
ACCCGAAATCGCCGCCGCCATTGAAAAGGCTTGCGACGAAGTTCTGCTGA
ACAACCGCTGCCTCGACCAATTCCCGTCCGACGTGTATCAGGGCGGGGCG
GGAACTTCGGTCAATATGAACACCAACGAAGTCATCGCCAACCTTGCATT
GGAAGCCTTGGGCTATGAGAAAGGCCGCTACGACATCGTCAATCCGATGG
ATCACGTCAACGCCAGCCAATCCACCAACGATGCCTATCCCACGGGCTTC
CGCCTTGCCGTGTATTACAGCATCGGCGAATTGCTCGACAAACTGACCGT
ATTGAAAAACGCCTTTGCCGCCAAAGCCGAAGCGTTTAAAGACGTTTTGA
AAATGGGTCGCACCCAGCTTCAAGATGCCGTACCGATGACGGCAGGCCAG
GAATTCCAATCTTTCCAAGTATTGTTGGAAGAGGAAATCCTCAACCTTGA
CCGCACCCGCCAACTGCTCTTGGAAGTCAATTTGGGCGCAACGGCAATCG
GCACGGGCGTGAACACGCCCAAAGGCTACGCCGAACTGGTGGTCAAAAAA
CTCTCCGAAGTCAGCGGCTTGCCTTGCAAACTGACTGAAAACCTGATCGA
AGCGACCTCCGACTGCGGTGCATATGTGATGGTACACGGCGCATTGAAAC
GCACGGCCGTCAAACTCTCTAAAATCTGCAACGATTTGCGCCTTCTCTCT
TCCGGTCCGCGCGCCGGTTTGAAAGAAATCAACCTGCCCGAATTGCAGGC
CGGTTCTTCCATCATGCCTGCCAAAGTCAATCCCGTGATTCCCGAAGTCG
TCAACCAAGTCTGCTTCAAAGTCATCGGCAACGATACGACGATTACCTTC
GCCGCCGAATCCGGGCAACTGCAATTAAACGTTATGGAGCCGGTCATCGC
CCAATGTATGTTTGAAACCATTTCCCTCTTGGGCAATGCCGCAGTCAACC
TATCCGACAAATGCGTCAAAGGCATTACGGTCAACCGCGAAATCTGCGAG
CGGTATGTCTTCAACTCCATCGGTTTGGTCACTTATCTGAATCCGTACAT
CGGCCACCGCAACGGCGACTTGGTCGGCAAAATCTGCGCCCAAACCGGCA
AAGGCGTGCGCGAAGTCGTACTGGAGCGCGGCCTGTTAAGCGAAGAAGAA
ATCAACCGCATCCTCTCCCCCGAGAACCTGATGAATCCTCATCTG


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