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 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMFEYLKEKL-GVTLVHNPEYDRKN 86
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427  87 NHSSIYAVREYL-HNTYICCADNYFNENPFEKMADGSFYSALYAEGETNEWCM--------QENEEGIITSVVIGGRDSW 157
Cdd:cd02523    81 NIYSLYLARDFLdEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDeyvkdlddAGVLLGIISKAKNLEEIQG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427 158 YMNGPAFWTEEYTRQFLEILDEAYGKPETaEKLWENIYLENIEKLPMKLKKCDERNIYEFDSLEELREFD 227
Cdd:cd02523   161 EYVGISKFSPEDADRLAEALEELIEAGRV-NLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLERAE 229

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731130427   7 NAVILAAGLSSRfapisyeM--PKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKA-EMFEYLKEKLGVTLVHNPEY 82
Cdd:TIGR03310   1 DAIILAAGLSSR-------MgqNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEAdELVALLANHSNITLVHNPQY 72

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 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMFEYLKEKL-GVTLVHNPEYDRKN 86
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAETN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427  87 NHSSIYAVREYL-HNTYICCADNYFNENPFEKMADGSFYSALYAEGETNEWCM--------QENEEGIITSVVIGGRDSW 157
Cdd:cd02523    81 NIYSLYLARDFLdEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDeyvkdlddAGVLLGIISKAKNLEEIQG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427 158 YMNGPAFWTEEYTRQFLEILDEAYGKPETaEKLWENIYLENIEKLPMKLKKCDERNIYEFDSLEELREFD 227
Cdd:cd02523   161 EYVGISKFSPEDADRLAEALEELIEAGRV-NLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDLERAE 229

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 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMF-EYLKE--KLGVTLVHNPEYDR 84
Cdd:COG1208     2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIeEYFGDgsRFGVRITYVDEGEP 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1731130427  85 KNNHSSIYAVREYLHNTYICC--ADNYFNENpFEKMAD 120
Cdd:COG1208    82 LGTGGALKRALPLLGDEPFLVlnGDILTDLD-LAALLA 118

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731130427   8 AVILAAGLSSRFapisyEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMFEYLKEKLGVTLVHNPEYDR 84
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEE 77

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMF-EYLKE--KLGVTLVHNPEYDR 84
Cdd:cd04189     3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIkEALGDgsRFGVRITYILQEEP 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1731130427  85 KNNHSSIYAVREYLHNT--YICCADNYFNE 112
Cdd:cd04189    83 LGLAHAVLAARDFLGDEpfVVYLGDNLIQE 112

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731130427   8 AVILAAGLSSRFApisyeMPKALIPVRGEVLIERQICQLREAGiDEVIVVTGYKAEMFEYlkEKLGVTLVHNPEYDR 84
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAAL--AGLGVPVVPDPDPGQ 69

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731130427   7 NAVILAAGLSSRfapisyeM--PKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKA-EMFEYLKEKLGVTLVHNPEY 82
Cdd:TIGR03310   1 DAIILAAGLSSR-------MgqNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEAdELVALLANHSNITLVHNPQY 72

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTG-YKAEMFE-YLK--EKLGVTL 76
Cdd:COG1209     3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFErLLGdgSQLGIKI 75

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 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVT 58
Cdd:cd04198     3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV 53

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 1731130427   7 NAVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAE-MFEYLKE---KLGVTLV 77
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEdMVPFLKEyekKLGIKIT 76

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731130427   8 AVILAAGLSSRfapisyeM----PKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMFEYLKEKLGVTLVHNPE 81
Cdd:cd02540     1 AVILAAGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEE 71

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        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731130427   7 NAVILAAGLSSRFApisyeMPKALIPVRGEVLIERQICQLREAgIDEVIVVTGYKAEMFeylkEKLGVTLV 77
Cdd:cd02503     2 TGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERY----ALLGVPVI 62

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        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731130427   8 AVILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTG-YKAEMFEYLK 69
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCsHSDQIKEYIE 65

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731130427   7 NAVILAAGLSSRfapisyeM----PKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMfeyLKEKLG 73
Cdd:COG1207     4 AVVILAAGKGTR-------MksklPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ---VRAALA 64

D-ribitol-5-phosphate cytidylyltransferase;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731130427   8 AVILAAGLSSRFAPisyEMPKALIPVRGEVLIERQICQLREAG-IDEVIVVTGykAEMFEYLKEKL 72
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP--PDDRPDFAELL 66

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1731130427   9 VILAAGLSSRFAPISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVT 58
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC 51

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427   7 NAVILAAGLSSRfapISYEMPKALIPVRGEVLIERQICQLREAGIDEVIVVTGYKAEMFEYLKEKLGVTL 76
Cdd:PRK14358    9 DVVILAAGQGTR---MKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF 75

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 1731130427   8 AVILAAGLS--SRFAPISYEMPKALIPVRGEVLIERQICQLRE-AGIDEVIVVTGYKAEMF----EYLKEKLGVTLVHNP 80
Cdd:cd06428     1 AVILVGGPQkgTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFsdfiSDAQQEFNVPIRYLQ 80

                  ..
gi 1731130427  81 EY 82
Cdd:cd06428    81 EY 82

molybdenum cofactor guanylyltransferase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1731130427   8 AVILAAGLSSRfapisyeM--PKALIPVRGEVLIERqICQLREAGIDEVIVVT 58
Cdd:PRK02726   10 ALILAGGKSSR-------MgqDKALLPWQGVPLLQR-VARIAAACADEVYIIT 54

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731130427   8 AVILAAGLSSRFapiSYEMPKALIPVRGEVLIERQICQLREAG-IDEVIVVTGYKAE--MFEYLKEKLGVTLVH 78
Cdd:PRK09382    8 LVIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIayMKKALPEIKFVTLVT 78

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731130427   8 AVILAAGL-SSRFapisyemP-KALIPVRGEVLIERQICQLREA-GIDEVIVVTGYKAE--MFEYLKEKLGVTLVHNPEY 82
Cdd:cd02518     1 VAIIQARMgSTRL-------PgKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATSTNEEddPLEALAKKLGVKVFRGSEE 73

                  .
gi 1731130427  83 D 83
Cdd:cd02518    74 D 74