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Conserved domains on  [gi|1889466166|ref|WP_182673593|]
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MULTISPECIES: nucleotidyltransferase family protein [unclassified Pseudoalteromonas]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 10135460)

nucleotidyltransferase family protein similar to MobA protein (molybdopterin-guanine dinucleotide biosynthesis protein A) and Paenarthrobacter nicotinovorans nicotine blue oxidoreductase, which catalyzes the reduction of nicotine blue and other quinones to their hydroquinone forms

PubMed:  9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-189 5.92e-56

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


:

Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 175.06  E-value: 5.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   3 IAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQWSQGLGH 82
Cdd:cd04182     1 IAAIILAAGRSSRMGGNKLLLPLD-GKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL-PVVVVINPDWEEGMSS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  83 SIATASQTVfkNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSRW-CANYGERLGVPAIFPAVDLSQLASLTSDRGAQ 161
Cdd:cd04182    79 SLAAGLEAL--PADADAVLILLADQPLVTAETLRALIDAFREDGAGIvAPVYQGRRGHPVLFPRSLFPELLALSGDKGAR 156

                         170       180
                  ....*....|....*....|....*....
gi 1889466166 162 QLLRS-SSEVVNTISLRSASLDIDTQKQL 189
Cdd:cd04182   157 SLLRAhPDRVVVEVDDPGVLIDIDTPEDL 185
 
Name Accession Description Interval E-value
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-189 5.92e-56

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 175.06  E-value: 5.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   3 IAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQWSQGLGH 82
Cdd:cd04182     1 IAAIILAAGRSSRMGGNKLLLPLD-GKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL-PVVVVINPDWEEGMSS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  83 SIATASQTVfkNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSRW-CANYGERLGVPAIFPAVDLSQLASLTSDRGAQ 161
Cdd:cd04182    79 SLAAGLEAL--PADADAVLILLADQPLVTAETLRALIDAFREDGAGIvAPVYQGRRGHPVLFPRSLFPELLALSGDKGAR 156

                         170       180
                  ....*....|....*....|....*....
gi 1889466166 162 QLLRS-SSEVVNTISLRSASLDIDTQKQL 189
Cdd:cd04182   157 SLLRAhPDRVVVEVDDPGVLIDIDTPEDL 185
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-195 1.16e-53

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 169.57  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   1 MLIAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQWSQGL 80
Cdd:COG2068     2 SKVAAIILAAGASSRMGRPKLLLPLG-GKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGL-GVRVVVNPDWEEGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  81 GHSIATASQTVfkNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSRW-CANYGERLGVPAIFPAVDLSQLASLTSDRG 159
Cdd:COG2068    80 SSSLRAGLAAL--PADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIvAPTYDGRRGHPVLFSRRLFPELLALTGDQG 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889466166 160 AQQLLRSSSEVVNTISL--RSASLDIDTQKQLSNFIAK 195
Cdd:COG2068   158 ARALLRRHPDRVRLVPVddPGVLLDIDTPEDLARLLAR 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-170 3.41e-33

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.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 116.14  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDtPVYVVTGawHKEVAQALAGYkNIELIENKQWSQGLGHSIA 85
Cdd:pfam12804   2 VILAGGRSSRMGGDKALLPLG-GKPLLERVLERLRPAGD-EVVVVAN--DEEVLAALAGL-GVPVVPDPDPGQGPLAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  86 TAsqtVFKNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSR-WCANYGERLGVPAIFPAVDLSQLASLTSDRGAQQLL 164
Cdd:pfam12804  77 AA---LRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADiVVPVYDGGRGHPLLYRRRLLPALEALLGDRGLRRLL 153


                  ....*.
gi 1889466166 165 RSSSEV 170
Cdd:pfam12804 154 RRLDEV 159
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 6-185 1.45e-29

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.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 107.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGCKLTADIgFGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYKNIELIENKQWSQGLGHSI- 84
Cdd:TIGR03310   3 IILAAGLSSRMGQNKLLLPY-KGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLVHNPQYAEGQSSSIk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  85 ---ATASQTvfknksfDGILFMLADQVELKVAHLSELVTGFTRNPSR-WCANYGERLGVPAIFPAVDLSQLASLTSDRGA 160
Cdd:TIGR03310  82 lglELPVQS-------DGYLFLLGDQPFVTPDIIQLLLEAFALKNDEiVVPLYKGKRGHPVLFPRKLFPELLALTGDTGG 154

                         170       180
                  ....*....|....*....|....*..
gi 1889466166 161 QQLLRSSSEVVNTISLRSAS--LDIDT 185
Cdd:TIGR03310 155 RQILRELPHEVKYVEVKDPGilFDIDT 181
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-87 3.57e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.31  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   4 AKVVLAAGQSSRFNGC--KLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGY-KNIELIENKQwSQGL 80
Cdd:PRK14353    7 LAIILAAGEGTRMKSSlpKVLHPVA-GRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIaPDAEIFVQKE-RLGT 84


                  ....*..
gi 1889466166  81 GHSIATA 87
Cdd:PRK14353   85 AHAVLAA 91
 
Name Accession Description Interval E-value
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-189 5.92e-56

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 175.06  E-value: 5.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   3 IAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQWSQGLGH 82
Cdd:cd04182     1 IAAIILAAGRSSRMGGNKLLLPLD-GKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL-PVVVVINPDWEEGMSS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  83 SIATASQTVfkNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSRW-CANYGERLGVPAIFPAVDLSQLASLTSDRGAQ 161
Cdd:cd04182    79 SLAAGLEAL--PADADAVLILLADQPLVTAETLRALIDAFREDGAGIvAPVYQGRRGHPVLFPRSLFPELLALSGDKGAR 156

                         170       180
                  ....*....|....*....|....*....
gi 1889466166 162 QLLRS-SSEVVNTISLRSASLDIDTQKQL 189
Cdd:cd04182   157 SLLRAhPDRVVVEVDDPGVLIDIDTPEDL 185
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-195 1.16e-53

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 169.57  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   1 MLIAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQWSQGL 80
Cdd:COG2068     2 SKVAAIILAAGASSRMGRPKLLLPLG-GKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGL-GVRVVVNPDWEEGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  81 GHSIATASQTVfkNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSRW-CANYGERLGVPAIFPAVDLSQLASLTSDRG 159
Cdd:COG2068    80 SSSLRAGLAAL--PADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIvAPTYDGRRGHPVLFSRRLFPELLALTGDQG 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889466166 160 AQQLLRSSSEVVNTISL--RSASLDIDTQKQLSNFIAK 195
Cdd:COG2068   158 ARALLRRHPDRVRLVPVddPGVLLDIDTPEDLARLLAR 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-170 3.41e-33

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.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 116.14  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDtPVYVVTGawHKEVAQALAGYkNIELIENKQWSQGLGHSIA 85
Cdd:pfam12804   2 VILAGGRSSRMGGDKALLPLG-GKPLLERVLERLRPAGD-EVVVVAN--DEEVLAALAGL-GVPVVPDPDPGQGPLAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  86 TAsqtVFKNKSFDGILFMLADQVELKVAHLSELVTGFTRNPSR-WCANYGERLGVPAIFPAVDLSQLASLTSDRGAQQLL 164
Cdd:pfam12804  77 AA---LRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADiVVPVYDGGRGHPLLYRRRLLPALEALLGDRGLRRLL 153


                  ....*.
gi 1889466166 165 RSSSEV 170
Cdd:pfam12804 154 RRLDEV 159
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 6-185 1.45e-29

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.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 107.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGCKLTADIgFGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYKNIELIENKQWSQGLGHSI- 84
Cdd:TIGR03310   3 IILAAGLSSRMGQNKLLLPY-KGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLVHNPQYAEGQSSSIk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166  85 ---ATASQTvfknksfDGILFMLADQVELKVAHLSELVTGFTRNPSR-WCANYGERLGVPAIFPAVDLSQLASLTSDRGA 160
Cdd:TIGR03310  82 lglELPVQS-------DGYLFLLGDQPFVTPDIIQLLLEAFALKNDEiVVPLYKGKRGHPVLFPRKLFPELLALTGDTGG 154

                         170       180
                  ....*....|....*....|....*..
gi 1889466166 161 QQLLRSSSEVVNTISLRSAS--LDIDT 185
Cdd:TIGR03310 155 RQILRELPHEVKYVEVKDPGilFDIDT 181
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-106 5.57e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 56.79  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGckLTAD-------IGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYK-NIELIENKQWS 77
Cdd:COG1213     3 VILAAGRGSRLGP--LTDDipkclveIG-GKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGpDVTFVYNPDYD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1889466166  78 Q-GLGHSIATAsqtvfKNKSFDGILFMLAD 106
Cdd:COG1213    80 EtNNIYSLWLA-----REALDEDFLLLNGD 104
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-76 3.28e-08

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.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 51.85  E-value: 3.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889466166   6 VVLAAGQSSRFNgcKLTADIG------FGKTMIEHAVNTLHALDDTPVYVVTGawHKE--VAQALAGYKNIELIENKQW 76
Cdd:cd02523     2 IILAAGRGSRLR--PLTEDRPkclleiNGKPLLERQIETLKEAGIDDIVIVTG--YKKeqIEELLKKYPNIKFVYNPDY 76
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-69 2.59e-07

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.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 48.73  E-value: 2.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889466166   6 VVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDtPVYVVTGawHKEVAQALAGYKNIE 69
Cdd:cd02503     4 VILAGGKSRRMGGDKALLELG-GKPLLEHVLERLKPLVD-EVVISAN--RDQERYALLGVPVIP 63
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-72 5.81e-07

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 48.20  E-value: 5.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889466166   6 VVLAAGQSSRFNG--CKLTADIGfGKTMIEHAVNTLHALDD-TPVYVVTGA-WHKEVAQALAGY---KNIELIE 72
Cdd:COG1211     1 IIPAAGSGSRMGAgiPKQFLPLG-GKPVLEHTLEAFLAHPRiDEIVVVVPPdDIEYFEELLAKYgidKPVRVVA 73
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-51 1.73e-06

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 46.34  E-value: 1.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1889466166   1 MLIAKVVLAAGQSSRFNGCKLTADIGfGKTMIEHAVNTLHALDDtPVYVVT 51
Cdd:COG0746     3 MPITGVILAGGRSRRMGQDKALLPLG-GRPLLERVLERLRPQVD-EVVIVA 51
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 6-87 1.91e-06

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 47.33  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNGC--KLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGawHK--EVAQALAGYkNIELIENKQwsQ-GL 80
Cdd:COG1207     6 VILAAGKGTRMKSKlpKVLHPLA-GKPMLEHVLDAARALGPDRIVVVVG--HGaeQVRAALADL-DVEFVLQEE--QlGT 79


                  ....*..
gi 1889466166  81 GHSIATA 87
Cdd:COG1207    80 GHAVQQA 86
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-87 8.93e-06

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.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 44.81  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNG------CKLtadigFGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYkNIELIENKQwSQG 79
Cdd:cd02540     2 VILAAGKGTRMKSdlpkvlHPL-----AGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-NVEFVLQEE-QLG 74


                  ....*...
gi 1889466166  80 LGHSIATA 87
Cdd:cd02540    75 TGHAVKQA 82
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-87 3.57e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.31  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   4 AKVVLAAGQSSRFNGC--KLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGY-KNIELIENKQwSQGL 80
Cdd:PRK14353    7 LAIILAAGEGTRMKSSlpKVLHPVA-GRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIaPDAEIFVQKE-RLGT 84


                  ....*..
gi 1889466166  81 GHSIATA 87
Cdd:PRK14353   85 AHAVLAA 91
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-110 1.51e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.45  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   1 MLiAKVVLAAGQSSRFNGC--KLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYKNIELIENKQWSq 78
Cdd:PRK14360    1 ML-AVAILAAGKGTRMKSSlpKVLHPLG-GKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGLEFVEQQPQL- 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1889466166  79 GLGHSIATASQTVfknKSFDGILFMLADQVEL 110
Cdd:PRK14360   78 GTGHAVQQLLPVL---KGFEGDLLVLNGDVPL 106
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-72 1.49e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 38.19  E-value: 1.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889466166   1 MLIAkVVLAAGQSSRFN-GC-KLTADIGfGKTMIEHAVNTLHALDDTP-VYVVTGA-WHKEVAQ-ALAGYKNIELIE 72
Cdd:PRK00155    3 MVYA-IIPAAGKGSRMGaDRpKQYLPLG-GKPILEHTLEAFLAHPRIDeIIVVVPPdDRPDFAElLLAKDPKVTVVA 77
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-127 1.63e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 38.38  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   4 AKVVLAAGQSSRF--NGCKLTADIGfGKTMIEHAVNTLHALDDTPVYVVTGAWHKEVAQALAGYKNIELIENKQWSQGLG 81
Cdd:PRK14352    6 AVIVLAAGAGTRMrsDTPKVLHTLA-GRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVDIAVQDEQPGTG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1889466166  82 HSIATASQTVfkNKSFDGILFMLADQVELKVAH-LSELVTGFTRNPS 127
Cdd:PRK14352   85 HAVQCALEAL--PADFDGTVVVTAGDVPLLDGEtLADLVATHTAEGN 129
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-71 2.68e-03

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 37.50  E-value: 2.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889466166   6 VVLAAGQSSRFNGC--KLTADIGfGKTMIEHAVNTLHALDD-TPVYVVTGAWHKEVAQALAGYKNIELI 71
Cdd:cd02516     4 IILAAGSGSRMGADipKQFLELG-GKPVLEHTLEAFLAHPAiDEIVVVVPPDDIDLAKELAKYGLSKVV 71
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 6-39 2.84e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.09  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1889466166   6 VVLAAGQSSRFNGC-KLTADIGfGKTMIEHAVNTL 39
Cdd:PRK00317    7 VILAGGRSRRMGGVdKGLQELN-GKPLIQHVIERL 40
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-106 4.18e-03

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 36.79  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889466166   6 VVLAAGQSSRFNgcKLTAD-------IGfGKTMIEHAVNTLHALDDTPVYVVTGaWHKEVAQALAG-----YKNIELI-E 72
Cdd:cd04181     2 VILAAGKGTRLR--PLTDTrpkpllpIA-GKPILEYIIERLARAGIDEIILVVG-YLGEQIEEYFGdgskfGVNIEYVvQ 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1889466166  73 NKQWsqGLGHSIATAsqtvfKNKSFDG-ILFMLAD 106
Cdd:cd04181    78 EEPL--GTAGAVRNA-----EDFLGDDdFLVVNGD 105
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-72 5.29e-03

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 36.75  E-value: 5.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889466166   3 IAKVVLAAGQSSRFN-GCK---LTadIGfGKTMIEHAVNTL-HALDDTPVYVVTGA-WHKEVAQALAGYKNIELIE 72
Cdd:PRK09382    6 ISLVIVAAGRSTRFSaEVKkqwLR--IG-GKPLWLHVLENLsSAPAFKEIVVVIHPdDIAYMKKALPEIKFVTLVT 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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