1kam

<table><tr><td colspan='2'>[[1kam]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KAM FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kaq|1kaq]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nadD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinate-nucleotide_adenylyltransferase Nicotinate-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.18 2.7.7.18] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kam OCA], [http://pdbe.org/1kam PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kam RCSB], [http://www.ebi.ac.uk/pdbsum/1kam PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kam ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NADD_BACSU NADD_BACSU]] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).

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== Publication Abstract from PubMed ==

The nadD gene, encoding the enzyme nicotinic acid mononucleotide (NaMN) adenylyltransferase (AT), is essential for the synthesis of NAD and subsequent viability of the cell. The nadD gene in Bacillus subtilis (yqeJ) was identified by sequence homology with other bacterial nadD genes and by biochemical characterization of the gene product. NaMN AT catalyzes the reversible adenylation of both NaMN and the nicotinamide mononucleotide (NMN) but shows specificity for the nicotinate. In contrast to other known NMN ATs, biophysical characterizations reveal it to be a dimer. The NaMN AT crystal structure was determined for both the apo enzyme and product-bound form, to 2.1 and 3.2 A, respectively. The structures reveal a "functional" dimer conserved in both crystal forms and a monomer fold common to members of the nucleotidyl-transferase alpha/beta phosphodiesterase superfamily. A structural comparison with family members suggests a new conserved motif (SXXXX(R/K)) at the N terminus of an alpha-helix, which is not part of the shared fold. Interactions of the nicotinic acid with backbone atoms indicate the structural basis for specificity.

Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase.,Olland AM, Underwood KW, Czerwinski RM, Lo MC, Aulabaugh A, Bard J, Stahl ML, Somers WS, Sullivan FX, Chopra R J Biol Chem. 2002 Feb 1;277(5):3698-707. Epub 2001 Nov 9. PMID:11704676<ref>PMID:11704676</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kam" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Aulabaugh, A]]

[[Category: Bard, J]]

[[Category: Chopra, R]]

[[Category: Czerwinski, R M]]

[[Category: Lo, M C]]

[[Category: Olland, A M]]

[[Category: Somers, W S]]

[[Category: Stahl, M L]]

[[Category: Sullivan, F X]]

[[Category: Underwood, K W]]

[[Category: Transferase]]