{PDOC51855}
{PS51855; MGS}
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* MGS-like domain profile *
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Methylglyoxal synthase  (MGS,  EC  4.2.3.3) (see <PDOC01037>), which catalyzes
the conversion  of dihydroxyacetone phosphate (DHAP) to methylglyoxal (MG) and
inorganic phosphate,  has  been  found  in  many  organisms, including enteric
bacteria, some  gram-positive  bacteria,  a  number of archaebacteria, several
yeast species and goat liver [1,2]. A domain similar to the full-length MGS is
found in [3]:

 - Bifunctional    purine   biosynthesis   protein   PurH,   also   known   as
   aminoimidazole-4-carboxamide ribonucleotide  (AICAR)  transformylase (AICAR
   Tfase)/inosine 50-monophosphate   (IMP)   cyclohydrolase   (IMPCH)   (ATIC)
   (EC 2.1.2.3).  In  bacteria  and  eukaryotes, the last two steps of de novo
   purine biosynthesis  are  catalyzed  by  PurH,  which  is  composed  of two
   functionally independent  domains  linked  by  a  flexible  region.  The N-
   terminal MGS-like domain possesses IMPCH activity and the C-terminal domain
   possesses AICAR  Tfase  activity.  The  MGS-like domain with IMPCH activity
   catalyzes the  intramolecular cyclization of 5-formyl-AICAR (FAICAR) to IMP
   [4,5,6,7].
 - Carbamoyl  phosphate  synthetase (CPS) catalyzes the formation of carbamoyl
   phosphate from  one molecule of bicarbonate, two molecules of Mg(2+)ATP and
   one molecule  of glutamine or ammonia depending upon the particular form of
   the enzyme.  The  enzyme is an alpha,beta-heterodimer consisting of a small
   subunit that  hydrolyzes  glutamine  and a large subunit that catalyzes the
   two required  phosphorylation  events.  The  large subunit consists of four
   structural units:    the    carboxyphosphate   synthetic   component,   the
   oligomerization domain, the carbamoyl phosphate synthetic component and the
   MGS-like allosteric  domain. The binding of various ligands by the MGS-like
   domain allosterically regulates CPS [8,9].

The main  core  of  the  MGS-like  domain,  a  modified  'Rossmann'  fold,  is
characterized by a five stranded parallel beta-sheet flanked on either side by
three and  five  alpha-helices,  respectively (see <PDB:1PKX>) [6,8]. MGS-like
domains share a conserved phosphate binding site [3,7].

The profile we developed covers the entire MGS-like domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2018 / First entry.

[ 1] Falahati H., Pazhang M., Zareian S., Ghaemi N., Rofougaran R.,
     Hofer A., Rezaie A.R., Khajeh K.
     "Transmitting the allosteric signal in methylglyoxal synthase."
     Protein Eng. Des. Sel. 26:445-452(2013).
     PubMed=23592737; DOI=10.1093/protein/gzt014
[ 2] Huang K., Rudolph F.B., Bennett G.N.
     "Characterization of methylglyoxal synthase from Clostridium
     acetobutylicum ATCC 824 and its use in the formation of 1,
     2-propanediol."
     Appl. Environ. Microbiol. 65:3244-3247(1999).
     PubMed=10388730
[ 3] Murzin A.G.
     "Structure classification-based assessment of CASP3 predictions for
     the fold recognition targets."
     Proteins 0:88-103(1999).
     PubMed=10526357
[ 4] Qiu X., Yuan Y., Gao Y.
     "Expression, purification, crystallization and preliminary X-ray
     diffraction crystallographic study of PurH from Escherichia coli."
     Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 67:1590-1594(2011).
     PubMed=22139174; DOI=10.1107/S1744309111039960
[ 5] Axelrod H.L., McMullan D., Krishna S.S., Miller M.D., Elsliger M.-A.,
     Abdubek P., Ambing E., Astakhova T., Carlton D., Chiu H.-J.,
     Clayton T., Duan L., Feuerhelm J., Grzechnik S.K., Hale J., Han G.W.,
     Haugen J., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W.,
     Koesema E., Morse A.T., Nigoghossian E., Okach L., Oommachen S.,
     Paulsen J., Quijano K., Reyes R., Rife C.L., van den Bedem H.,
     Weekes D., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J.,
     Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.
     "Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249)
     from Thermotoga maritima at 1.88 A resolution."
     Proteins 71:1042-1049(2008).
     PubMed=18260100; DOI=10.1002/prot.21967
[ 6] Wolan D.W., Cheong C.-G., Greasley S.E., Wilson I.A.
     "Structural insights into the human and avian IMP cyclohydrolase
     mechanism via crystal structures with the bound XMP inhibitor."
     Biochemistry 43:1171-1183(2004).
     PubMed=14756553; DOI=10.1021/bi030162i
[ 7] Verma P., Kar B., Varshney R., Roy P., Sharma A.K.
     "Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC)
     from Staphylococcus lugdunensis."
     FEBS J. 284:4233-4261(2017).
     PubMed=29063699; DOI=10.1111/febs.14303
[ 8] Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.
     "The structure of carbamoyl phosphate synthetase determined to 2.1 A
     resolution."
     Acta Crystallogr. D 55:8-24(1999).
     PubMed=10089390; DOI=10.1107/S0907444998006234
[ 9] de Cima S., Polo L.M., Diez-Fernandez C., Martinez A.I., Cervera J.,
     Fita I., Rubio V.
     "Structure of human carbamoyl phosphate synthetase: deciphering the
     on/off switch  of human ureagenesis."
     Sci. Rep. 5:16950-16950(2015).
     PubMed=26592762; DOI=10.1038/srep16950

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