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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0515.1 IGR0517 IGR0510 IGR0511 IGR0515 IGR0516 IGR0509 IGR0512 IGR0514 IGR0513 NG0616 NG0613 NG0618 eno, - NG0617 mltD, - NG0608 NG0615.1 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0616 NG0613 NG0618 eno, - NG0617 mltD, - NG0608 NG0615.1 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0616 NG0613 NG0618 eno, - NG0617 mltD, - NG0608 NG0615.1 NG0609 plsC, - NG0611 fpg, - NG0610 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614
* Calculated from Protein Sequence

Gene ID: NG0614

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
rir1  nrdA  

Definition:
ribonucleotide reductase I alpha chain (ribonucleotide reductase 1) (B1 protein) (R1 protein)

Gene Start:
600309

Gene Stop:
602585

Gene Length:
2277

Molecular Weight*:
85162

pI*:
6.10

Net Charge*:
-8.65

EC:
1.17.4.1  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; 2'-Deoxyribonucleotide metabolism  

Pathway: pathway table
Purine metabolism
Pyrimidine metabolism

Secondary Evidence:
Nilsson,O., Aberg,A., Lundqvist,T. and Sjoberg,B.M. Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction. Nucleic Acids Res. 16 (9): 4174 (1988) [Medline: 88234023].

Carlson,J., Fuchs,J.A. and Messing,J. Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proc. Natl. Acad. Sci. U.S.A. 81 (14): 4294-4297 (1984) [Medline: 84272624].

Sjoberg,B.M., Eriksson,S., Jornvall,H., Carlquist,M. and Eklund,H. Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotidesequence of the Escherichia coli nrdA gene. Eur. J. Biochem. 150 (3): 423-427 (1985) [Medline: 85257670].

Aberg,A., Hahne,S., Karlsson,M., Larsson,A., Ormo,M., Ahgren,A. and Sjoberg,B.M. Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 264 (21): 12249-12252 (1989) [Medline: 89308645].

Uhlin,U. and Eklund,H. Structure of ribonucleotide reductase protein R1 . Nature 370 (6490): 533-539 (1994) [Medline: 94329174].

Eriksson,M., Uhlin,U., Ramaswamy,S., Ekberg,M., Regnstrom,K., Sjoberg,B.M. and Eklund,H. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 5 (8): 1077-1092 (1997) [Medline: 97454793].

Comment:
From GenBANK (gi:2507304): In E. coli, this protein catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides, precursors that are necessary for DNA synthesis. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. Catalytic activity: 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O = ribonucleoside diphosphate + reduced thioredoxin, the first reaction in the DNA replication pathway. This protein is a tetramer of two alpha and two beta chains. the B1 protein is a dimer of alpha chains. E.coli produces two separate class I enzymes; this one is the functional enzyme during growth. R1 belongs to the ribonucleoside diphosphate reductase large chain family.

See also NG0615, ribonucleoside diphosphate reductase I beta chain.

Oklahoma ID: NGO.614

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to ribonucleotide reductase I alpha chain; e.g. residues 7-759 are 78% similar to P43754 of H.influenzae.

Residues 1-759 are 98% similar to NMA1501 and NMB1291, both ribonucleotide reductase I alpha chain of N.meningitidis (11256441, 11256443).


COGS Summary:  COGS Search
BeTs to 15 clades of COG0209
COG name: Ribonucleotide reductase alpha subunit
Functional Class:  F
The phylogenetic pattern of COG0209 is a-tKYqvcEBRhujgp-linx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000788 (Ribonucleotide reductase large subunit) with a combined E-value of 9.9e-116.
    IPB000788A    14-24
    IPB000788B    147-158
    IPB000788C    199-229
    IPB000788D    249-285
    IPB000788E    300-322
    IPB000788F    376-385
    IPB000788G    433-452
    IPB000788H    551-579
    IPB000788I    601-639
    IPB000788J    724-733


ProDom Summary:  Protein Domain Search
Residues 300-426 are 77% similar to a (REDUCTASE RIBONUCLEOTIDE OXIDOREDUCTASE) protein domain (PD001074) which is seen in RIR1_HAEIN.

Residues 488-578 are 80% similar to a (REDUCTASE RIBONUCLEOTIDE OXIDOREDUCTASE DNA REPLICATION) protein domain (PD000706) which is seen in RIR1_HAEIN.

Residues 125-234 are 30% similar to a (RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE ALPHA CHAIN EC) protein domain (PD076574) which is seen in RIR1_SYNY3.

Residues 133-179 are 76% similar to a (REDUCTASE OXIDOREDUCTASE DNA REPLICATION) protein domain (PD002419) which is seen in Q47412_ECOLI.

Residues 187-299 are 78% similar to a (REDUCTASE B1 RIBONUCLEOSIDE-DIPHOSPHATE) protein domain (PD012935) which is seen in RIR1_SALTY.

Residues 62-182 are 28% similar to a (RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE ALPHA CHAIN EC) protein domain (PD207516) which is seen in RIR1_TREPA.

Residues 427-486 are 80% similar to a (REDUCTASE B1 RIBONUCLEOSIDE-DIPHOSPHATE) protein domain (PD013963) which is seen in RIR1_HAEIN.

Residues 640-759 are 75% similar to a (REDUCTASE B1 RIBONUCLEOSIDE-DIPHOSPHATE) protein domain (PD013964) which is seen in RIR1_HAEIN.

Residues 7-122 are 77% similar to a (REDUCTASE RIBONUCLEOSIDE-DIPHOSPHATE ALPHA CHAIN) protein domain (PD008187) which is seen in RIR1_SALTY.

Residues 595-639 are 88% similar to a (REDUCTASE RIBONUCLEOTIDE OXIDOREDUCTASE) protein domain (PD005031) which is seen in RIR1_HAEIN.



Paralogs:  Local Blast Search


NG0614 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 7 to 96 (E-value = 6.7e-20) place NG0614 in the ATP-cone family which is described as ATP cone domain (PF03477)
Residues 143 to 222 (E-value = 4.8e-25) place NG0614 in the Ribonuc_red_lgN family which is described as Ribonucleotide reductase, all-alpha domain (PF00317)
Residues 224 to 738 (E-value = 3.4e-230) place NG0614 in the Ribonuc_red_lgC family which is described as Ribonucleotide reductase, barrel domain (PF02867)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
443  
527

PDB Hit:
pdb|2R1R|2R1R-A RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP 1191.0 0.000000
pdb|6R1R|6R1R-A RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN1190.0 0.000000
pdb|7R1R|7R1R-A RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN1190.0 0.000000
pdb|1R1R|1R1

Gene Protein Sequence:
MNTPTDLKVTKRDGRLEAIDLDKIHRVVTWAAEGLENVSVSQVELKSHIQ
FYNGIRTDDIHETIIKAAADLISEDTPDYQYLAARLAIFHLRKIAYGEYE
PPHLYNHVKKLTDAGKYDRHILEDYSREEFDELNAYIDHERDMSFSYAAV
KQLEGKYLVQNRVTRQIYETPQFLYVLVAMCLFSKYPKEARLDYVKRFYD
AVSTFKVSLPTPIMSGVRTPTRQFSSCVLIECDDSLDSINATTSAIVKYV
SQRAGIGINAGRIRGLDSEIRGGEARHTGCIPFFKMFQAAVKSCSQGGVR
GGAATLFYPLWHIEAESLLVLKNNRGVEDNRIRQLDYGVQINRLLYTRLI
KGGNITLFSPNEVSGLYEAFFADQDEFERLYTKYEQDPNIRKRIIPAADL
FSTLMQERAGTGRIYIQNVDHCNTHSPFDPRVAPVHQSNLCMEIALPTKP
LDNINDPDGEIALCTLSAFNLGALNSLDELEGLADLTVRALDALLDYQGY
PVEAARTSTMDRRSLGIGVINYAYYLAKNGVRYSDGSALGLTHRTFEAIQ
YYLLKASANLAKEYGACTLFNQTVYSQGKLPIDTYKKDLDAVCGEPLHYD
WESLRADIVKYGLRNSTLTALMPSETSSQIANATNGIEPPRGLVTVKASK
DGILKQVVPEFETLKNAYETLWQLPGNEGYLKLVGVMQKFVDQAISANTA
YDPGKFEGNKVSMKQMLKDLLTAYKYGVKTLYYHNTRDGADDTQTDIQDD
GCAGGACKI

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATACACCGACTGATTTAAAAGTAACCAAACGAGACGGAAGATTGGA
AGCCATTGATTTGGATAAGATTCACCGTGTCGTTACTTGGGCGGCGGAAG
GATTGGAAAATGTTTCCGTGTCGCAGGTCGAGTTGAAATCGCACATCCAG
TTCTACAACGGCATCCGCACCGACGACATCCACGAAACCATCATCAAAGC
CGCTGCAGATTTAATTTCGGAAGATACCCCGGACTACCAATACCTTGCCG
CACGTTTGGCGATTTTCCATCTTCGTAAAATAGCCTACGGCGAATACGAG
CCGCCGCACCTTTACAACCATGTTAAAAAGCTCACCGATGCCGGAAAATA
CGACAGGCATATCCTTGAGGATTACAGCCGCGAAGAATTTGACGAACTGA
ACGCCTATATCGACCACGAACGCGATATGTCCTTTTCCTATGCCGCCGTC
AAACAGCTCGAAGGCAAATATCTGGTACAGAACCGCGTTACCCGCCAGAT
TTACGAAACGCCGCAGTTTTTATATGTTTTGGTGGCGATGTGCCTTTTCA
GCAAATACCCGAAAGAGGCGCGCTTGGATTACGTCAAACGGTTTTACGAT
GCCGTTTCCACATTCAAAGTATCGTTGCCCACGCCGATTATGAGCGGCGT
GCGTACGCCTACGCGCCAGTTCTCAAGCTGTGTGCTGATTGAATGCGACG
ATAGTTTGGATTCCATCAATGCCACTACCAGCGCGATTGTGAAATACGTT
TCCCAACGCGCGGGCATCGGCATCAATGCCGGACGTATCCGCGGGCTGGA
CAGCGAAATCCGGGGCGGTGAAGCCCGGCATACCGGCTGCATTCCCTTCT
TTAAGATGTTTCAGGCGGCGGTCAAATCTTGTTCGCAAGGTGGCGTGCGC
GGCGGCGCGGCAACCTTGTTCTACCCCTTGTGGCATATTGAAGCCGAAAG
CCTGCTGGTGTTGAAAAACAACCGGGGCGTGGAAGACAACCGTATCCGCC
AGCTTGATTATGGCGTGCAAATCAACCGCCTGCTGTACACCCGCCTGATT
AAGGGCGGCAACATTACGCTGTTTTCGCCCAACGAGGTTTCGGGGTTGTA
CGAAGCGTTTTTTGCCGACCAAGACGAATTTGAGCGGCTCTATACGAAAT
ACGAGCAAGACCCGAACATACGCAAGCGTATCATTCCGGCTGCCGACCTG
TTTTCCACGCTGATGCAGGAGCGTGCCGGGACCGGGCGCATCTACATTCA
AAACGTCGATCACTGCAATACGCACAGCCCGTTCGATCCGCGCGTTGCGC
CTGTTCATCAGTCCAACTTGTGTATGGAAATCGCCCTGCCGACCAAACCG
CTGGACAACATCAACGACCCTGACGGCGAAATAGCCCTGTGTACACTGTC
CGCCTTCAACTTGGGTGCATTAAACAGCTTGGACGAATTGGAAGGGCTTG
CCGATTTGACCGTGCGCGCACTCGATGCACTTTTAGATTATCAGGGATAT
CCGGTAGAAGCCGCGCGTACCTCTACTATGGACCGCCGTTCGCTCGGCAT
CGGTGTCATCAACTACGCCTACTATCTGGCGAAAAACGGTGTCCGCTACA
GCGACGGTTCCGCGCTCGGTCTGACCCACCGTACCTTTGAAGCCATACAG
TATTACCTGCTCAAAGCATCGGCAAACCTTGCCAAAGAATACGGAGCGTG
CACGCTCTTTAACCAAACCGTTTATTCGCAAGGCAAACTGCCCATCGACA
CCTACAAAAAAGATTTGGATGCCGTCTGCGGCGAGCCTTTGCATTACGAC
TGGGAAAGCCTGCGTGCCGACATCGTCAAATACGGCCTGCGCAACTCTAC
TCTGACCGCGCTCATGCCGTCTGAAACCAGCTCGCAAATCGCCAACGCCA
CCAACGGCATCGAGCCGCCGCGCGGATTGGTAACGGTCAAAGCATCGAAA
GACGGCATTTTGAAACAAGTCGTGCCGGAGTTTGAAACCTTGAAAAATGC
CTACGAAACCCTGTGGCAGCTTCCGGGCAACGAAGGCTACCTGAAACTTG
TCGGCGTAATGCAAAAATTCGTCGATCAGGCGATTTCCGCCAACACTGCT
TACGACCCGGGCAAATTCGAAGGTAACAAAGTTTCTATGAAACAAATGCT
CAAAGACCTGCTGACTGCCTACAAATACGGCGTCAAAACCCTGTACTACC
ACAACACCCGCGACGGCGCGGACGACACGCAGACCGATATTCAAGATGAC
GGCTGCGCTGGTGGGGCTTGTAAGATT


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