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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0543 IGR0538 IGR0542 IGR0540 IGR0539 IGR0545 IGR0537 IGR0544 IGR0541 NG0643 truB, - NG0642 argD, - NG0646 rhlE, - NG0650 mod, - NG0641 NG0649 NG0647 NG0648 NG0651 clpX, - NG0645 NG0643 truB, - NG0642 argD, - NG0646 rhlE, - NG0650 mod, - NG0641 NG0649 NG0647 NG0648 NG0651 clpX, - NG0645 Type: tandem, Name:  - 31 Type: tandem, Name:  - 32 truB, - NG0642 argD, - NG0646 rhlE, - NG0650 mod, - NG0641 rbfA, - NG0644 NG0643 rbfA, - NG0644 NG0647 NG0648 NG0651 clpX, - NG0645 NG0649
* Calculated from Protein Sequence

Gene ID: NG0646

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
argD  

Definition:
acetylornithine aminotransferase (acetylornitine delta-aminotransferase) / succinylornithine transaminase (succinylornithine aminotransferase) (carbon starvation protein c)

Gene Start:
637171

Gene Stop:
635981

Gene Length:
1191

Molecular Weight*:
42672

pI*:
7.30

Net Charge*:
2.00

EC:
2.6.1.11  

Functional Class:
Amino acid biosynthesis; Glutamate family/nitrogen assimilation  

Pathway: pathway table
Urea cycle and metabolism of amino groups

Secondary Evidence:
Fraley,C.D., Kim,J.H., McCann,M.P. and Matin,A.
The Escherichia coli starvation gene cstC is involved in amino acid catabolism.
J. Bacteriol. 180 (16): 4287-4290 (1998)
[Medline: 98361921].

Schneider,B.L., Kiupakis,A.K. and Reitzer,L.J.
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
J. Bacteriol. 180 (16): 4278-4286 (1998)
[Medline: 98361920].

Heimberg,H., Boyen,A., Crabeel,M. and Glansdorff,N.
Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithineaminotransferase.
Gene 90 (1): 69-78 (1990)
[Medline: 9033734].

Velasco AM, Leguina JI, Lazcano A.
Molecular evolution of the lysine biosynthetic pathways.
J Mol Evol. 2002 Oct;55(4):445-59.
PMID: 12355264

Miyazaki J, Kobashi N, Nishiyama M, Yamane H.
Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through alpha-aminoadipate.
J Bacteriol. 2001 Sep;183(17):5067-73.
PMID: 11489859

Ledwidge R, Blanchard JS.
The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis.
Biochemistry. 1999 Mar;38(10):3019-24.
PMID: 10074354

Comment:
This protein was strongly similar to both acetylornithine aminotransferases and succinylornithine transaminases.

See also: ArgA, NG0027; ArgB, NG0844; ArgC, NG0118; ArgF, NG1232; ArgG, NG1961; ArgH, NG0219; ArgJ, NG1194.

For other aminotransferases, see NG0082 (avtA), NG0308 (bioA), NG0460, NG2045 (glmS), NG1047 (aat), NG1241 (hisC), NG1283 (serC), NG1329 (tyrB), NG1452 (aspC).

Oklahoma ID: NGO.646c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to acetylornithine aminotransferase; e.g. residues 4-390 are 57% similar to AE004524 of Pseudomonas aeruginosa.

NG0646 is orthologous to L162756, N. meningitidis Z2491 acetylornithine aminotransferase residues 1-397 have 96% similarity to residues 1-397 in NG0646.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0160
COG name: PLP-dependent aminotransferases
Functional Class:  E
The phylogenetic pattern of COG0160 is AmtKYqvcEBRh---------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000954 (Aminotransferase class-III pyridoxal-phosphate) with a combined E-value of 8.9e-54.
    IPB000954A    26-55
    IPB000954B    185-224
    IPB000954C    233-248
    IPB000954D    269-287


ProDom Summary:  Protein Domain Search
Residues 165-277 are 40% similar to a (FISSION YEAST) protein domain (PD200245) which is seen in P78766_SCHPO.

Residues 323-381 are 49% similar to a (AMINOTRANSFERASE TRANSFERASE PYRIDOXAL PHOSPHATE) protein domain (PD001337) which is seen in Q9ZC66_YERPE.

Residues 214-260 are 55% similar to a (AMINOTRANSFERASE TRANSFERASE PYRIDOXAL PHOSPHATE) protein domain (PD000465) which is seen in O57878_PYRHO.

Residues 54-307 are 61% similar to a (PYRIDOXAL PHOSPHATE AMINOTRANSFERASE TRANSFERASE PROTEIN) protein domain (PD000087) which is seen in O30508_PSEAE.

Residues 4-45 are 64% similar to a (AMINOTRANSFERASE PYRIDOXAL PHOSPHATE TRANSFERASE) protein domain (PD000493) which is seen in ARGM_ECOLI.

Residues 18-171 are 31% similar to a (PROBABLE AMINOTRANSFERASE C27F1.05C EC) protein domain (PD104185) which is seen in YAV5_SCHPO.

Residues 13-141 are 31% similar to a (AMINOTRANSFERASE TRANSFERASE DNTP-HEXOSE DEDUCED) protein domain (PD032384) which is seen in O52565_BBBBB.

Residues 46-200 are 32% similar to a (HYPOTHETICAL 22.7 KD PROTEIN) protein domain (PD082173) which is seen in P71890_MYCTU.



Paralogs:  Local Blast Search


NG0646 is paralogously related to NG0308 (adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (7e-29) and NG0040 (glutamate 1-semialdehyde 2,1-aminotransferase) (7e-27).


Pfam Summary:  Pfam Search
Residues 3 to 392 (E-value = 1.6e-169) place NG0646 in the Aminotran_3 family which is described as Aminotransferase class-III (PF00202)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
356  
372

PDB Hit:
pdb|1GBN|1GBN-A HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 228.0 2e-60
pdb|2OAT|2OAT-A 228.0 2e-60
pdb|1DKA|1DKA 2,2-DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE) 183.0 3e-47
pdb|1DGD|1DGD DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE) (DGD) 183.

Gene Protein Sequence:
MQNYLTPNFAFAPMIPERASGSRVWDTEGREYIDFSGGIAVNALGHCHPA
LVDALNAQMHKLWHISNIYTTRPAQELAQKLVKHSFADKVFFCNSGAEAN
EAALKLARKYARDRFGGGKSEIVACINSFHGRTLFTVSVGGQPKYSKDYA
PLPQGITHVPFNDIAALEAAVGEQTCAVIIEPIQGESGILPATAEYLQAA
RRLCDRHNALLILDEVQTGMGHTGRLFAYEHYGVVPDILSSAKALGCGFP
IGTMLATEKIAAAFQPGTHGSTFGGNPMACAVGSRAFDIINAPETLHNVR
SQGQKLQTALLDLGRKTGLFSQVRGMGLLLGCALDTPYRGRSSEIAATSL
KHGVMILVAGADVLRFAPSLLLNDEDIAEGLRRLEHVLTEFAAANRP

Gene Nucleotide Sequence:  Sequence Viewer
ATGCAAAACTATCTGACCCCCAATTTCGCCTTTGCCCCGATGATTCCCGA
ACGCGCTTCAGGCAGCCGCGTTTGGGATACGGAAGGGCGTGAATATATTG
ATTTTTCAGGCGGCATCGCCGTTAACGCTCTGGGGCACTGCCACCCTGCC
CTTGTCGATGCTTTAAACGCGCAGATGCACAAGCTGTGGCACATTTCCAA
TATCTATACGACGCGGCCGGCGCAGGAATTGGCGCAAAAATTGGTGAAAC
ACAGTTTTGCCGACAAGGTTTTTTTCTGCAACTCGGGCGCGGAAGCGAAT
GAGGCGGCGTTAAAGCTGGCAAGGAAATATGCGCGCGACCGTTTCGGCGG
AGGCAAAAGCGAAATCGTCGCCTGTATCAACAGTTTCCACGGACGCACGC
TGTTTACCGTGTCCGTCGGCGGACAGCCGAAATACAGTAAGGATTATGCA
CCGCTGCCGCAAGGCATTACGCACGTTCCGTTCAACGATATTGCCGCGCT
GGAAGCTGCCGTCGGCGAACAGACCTGCGCGGTCATCATCGAGCCGATAC
AGGGCGAAAGCGGCATCCTGCCCGCCACTGCGGAATATTTGCAGGCGGCG
CGCCGTCTGTGCGACCGGCACAATGCGTTGTTGATTTTGGACGAAGTTCA
AACCGGGATGGGGCATACGGGCAGGCTGTTTGCCTATGAACATTACGGCG
TTGTTCCCGATATTTTGAGTTCGGCAAAAGCCTTGGGCTGCGGCTTTCCG
ATCGGCACGATGCTGGCGACAGAAAAGATTGCCGCCGCCTTCCAACCGGG
CACGCACGGCTCGACTTTCGGCGGCAACCCGATGGCGTGTGCGGTCGGCA
GCCGCGCCTTCGACATCATCAACGCGCCGGAAACCTTGCACAACGTCCGC
AGTCAGGGGCAGAAACTTCAGACGGCATTGCTGGATTTGGGCAGGAAAAC
AGGCTTGTTCTCACAGGTTCGCGGGATGGGGCTGCTGCTCGGCTGCGCGT
TGGACACGCCTTATCGCGGACGCTCATCCGAAATCGCCGCTACCTCCTTG
AAACACGGCGTGATGATCTTAGTTGCGGGTGCGGACGTATTGCGTTTCGC
GCCTTCGCTGCTGTTGAACGATGAGGATATTGCGGAAGGTTTGCGGCGTT
TGGAACACGTGCTGACGGAATTTGCCGCCGCAAACCGCCCC


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