Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1912983799  10 NGERTIVQLIHDGEVDLIVNTPYGTGGRLDGYDIRTAAVARSVPCLTTVQALAAAVQ 66
Cdd:cd01424    54 EGRPNIVDLIKNGEIQLVINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1912983799  11 GERTIVQLIHDGEVDLIVNTPYG--TGGRLDGYDIRTAAVARSVPCLT 56
Cdd:smart00851 44 GIPQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRRAAENIDIPGPT 91

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1912983799  10 NGERTIVQLIHDGEVDLIVNTPYGTGGRLDGYDIRTAAVARSVPCLTTVQALAAAVQ 66
Cdd:cd01424    54 EGRPNIVDLIKNGEIQLVINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 1912983799  9 PNGERTIVQLIHDGEVDLIVNTPYG-TGGRLDGYDIRTAAVARSVPCLT 56
Cdd:pfam02142 45 PGGRVQIGDLIKNGEIDLVINTLYPfKATVHDGYAIRRAAENIDIPGPT 93

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1912983799   11 GERTIVQLIHDGEVDLIVNTPY-GTGGRLDGYDIRTAAVARSVPCLTTVQ 59
Cdd:TIGR01369  992 GRPNILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPLITTLN 1041

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1912983799  10 NGERTIVQLIHDGEVDLIVNTP-YGTGGRLD-GYDIRTAAVARSVPCLTTVQ 59
Cdd:cd01423    58 NDKPSLRELLAEGKIDLVINLPsNRGKRVLDnDYVMRRAADDFAVPLITNPK 109