Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFYYLAEKY-NVELIYNNKYDIYN 81
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316  82 NIYTMYLLREHL-PDSYVIEGDVYICNNFIDPDIKESTYFTLYKENFNNEFIFKFDE--NNKVYDMY------VGDNKGY 152
Cdd:cd02523   81 NIYSLYLARDFLdEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEYVKdlDDAGVLLGiiskakNLEEIQG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500187316 153 ILCGVSYWSLTDGNIIAKKLEETIENGdFESLFWDDVVMKNKDALNMYIQKIDFKDCFEIDNEKDLR 219
Cdd:cd02523  161 EYVGISKFSPEDADRLAEALEELIEAG-RVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLE 226

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 500187316    2 KAIILAAGLGTRLKPLTSECPKPLV-KVNGKPMIETQIECLLEKGIKDIKVAVGY 55
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREIIVILTQ 55

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFYYLAEKY-NVELIYNNKYDIYN 81
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316  82 NIYTMYLLREHL-PDSYVIEGDVYICNNFIDPDIKESTYFTLYKENFNNEFIFKFDE--NNKVYDMY------VGDNKGY 152
Cdd:cd02523   81 NIYSLYLARDFLdEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEYVKdlDDAGVLLGiiskakNLEEIQG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500187316 153 ILCGVSYWSLTDGNIIAKKLEETIENGdFESLFWDDVVMKNKDALNMYIQKIDFKDCFEIDNEKDLR 219
Cdd:cd02523  161 EYVGISKFSPEDADRLAEALEELIEAG-RVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLE 226

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316   2 KAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFY-YLAE--KYNVELIYNNKYD 78
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEeYFGDgsRFGVRITYVDEGE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 500187316  79 IYNNIYTMYLLREHLPDS--YVIEGDVyicnnFIDPDIKE 116
Cdd:COG1208   81 PLGTGGALKRALPLLGDEpfLVLNGDI-----LTDLDLAA 115

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500187316   2 KAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFY-YLAEK-YNVELIY 73
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEaHLGDSrFGLRITI 74

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316   1 MKAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKF 60
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEI 60

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500187316   1 MKAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKE------KFYylAEKYNVELIY 73
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEdmvpflKEY--EKKLGIKITF 77

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316    2 KAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLK----EKFYYLAEKYNVELIYNNKY 77
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTgeeiKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 500187316   78 DIYNNIYTMYLLREHLPDSYVIegdVYICNNFIDPDIKEstyftlYKENFNNE 130
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFV---VYLGDNLIQDGISR------FVKSFEEK 124

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500187316   3 AIILAAGLGTRLKPltsecPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFYYLAEKYNVELIYNNKYD 78
Cdd:COG2068    6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWE 76

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 500187316    2 KAIILAAGLGTRLKPLTSECPKPLV-KVNGKPMIETQIECLLEKGIKDIKVAVGY 55
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREIIVILTQ 55

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500187316   1 MKAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAV 53
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV 53

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500187316   1 MKAIILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEK 59
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ 58

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 500187316   1 MKAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDI 49
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREI 49

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500187316   3 AIILAAG--LGTRLKPLTSECPKPLVKVNGKPMIETQIECLLE-KGIKDIKVAVGYLKEKF--YYLAEK--YNVELIYNN 75
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFsdFISDAQqeFNVPIRYLQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500187316  76 KYDIYNNIYTMYLLREHL----PDS-YVIEGDVyiCNNF 109
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQIlagnPSAfFVLNADV--CCDF 117

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500187316   6 LAAGLGTRLKPltseCPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGYLKEKFYYLAEKYNVELIY 73
Cdd:COG2266    1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKERGVEVIE 64

D-ribitol-5-phosphate cytidylyltransferase;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500187316   3 AIILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLE-KGIKDIKVAV 53
Cdd:PRK00155   6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAhPRIDEIIVVV 54

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500187316   4 IILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLE-KGIKDIKVAV 53
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAhPRIDEIVVVV 48

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500187316   3 AIILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVG 54
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVG 56

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500187316   2 KAIILAAGLGTRLKPLTSECPK---PLVKvngKPMIETQIECLLEKGIKDI 49
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKemlPIVD---KPLIQYVVEEAVAAGIEEI 52

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDI 49
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEV 49

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDIKVAVGY----LKEKF--YYL 63
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYkghvIKEYFlnYFL 67

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500187316   4 IILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLEKGiKDIKVAVGYLKEK 59
Cdd:PRK14359   6 IILAAGKGTRMK---SSLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQKER 57

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 500187316   1 MKAIILAAGLGTRLKpltseCPKPLVKVNGKPMIETQIECL 41
Cdd:cd02503    1 ITGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERL 36

UTP--glucose-1-phosphate uridylyltransferase GalU;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 500187316   2 KAIILAAGLGTRLKPLTSECPKPLVKVNGKPMIETQIECLLEKGIKDI 49
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEI 57

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 500187316   1 MKAIILAAGLGTRLKpltseCPKPLVKVNGKPMIETQIECL 41
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERL 40

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 500187316   1 MKAIILAAGLGTRLKPL-TSECPKPLVKVNG-KPMIE 35
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLGeKSLLQ 39

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGK-PMIETQIECLLEKGIKDIKVAVGY 55
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGVLTQY 54

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 500187316    3 AIILAAGLGTRLKpltSECPKPLVKVNGKPMIETQIECLLEKG-IKDIKVAV 53
Cdd:pfam01128   1 AVIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAV 49

glucose-1-phosphate adenylyltransferase; Provisional

                         10        20
                 ....*....|....*....|....*....
gi 500187316   3 AIILAAGLGTRLKPLTSECPKPLVKVNGK 31
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGK 34