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Conserved domains on  [gi|521042270|ref|WP_020374294|]
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molybdenum cofactor guanylyltransferase [Sulfobacillus thermosulfidooxidans]

Protein Classification

molybdenum cofactor guanylyltransferase( domain architecture ID 10002369)

molybdenum cofactor guanylyltransferase (MobA) catalyzes the guanylation of the molybdenum cofactor using GTP as the source for the GMP moiety to form molybdopterin guanine dinucleotide

EC:  2.7.7.77
Gene Symbol:  mobA
Gene Ontology:  GO:0061603|GO:0005525|GO:0006777|GO:0046872
PubMed:  12719427|10978347|9445404|12691742|10521532
SCOP:  4000697|4000697

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 9-129 5.44e-14

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: 68.30  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   9 AIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRNSgrVNPIIVVGPPHL---GLHDVIWADVHDDM--LEN 82
Cdd:COG0746    7 GVILAG----GRsRRMGQDK---ALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPEryaALGVPVVPDDPPGAgpLAG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521042270  83 VLSGLNAVDEPTVLIATADIPLLTGYIVNAFLDQADPRYDVVYPVIE 129
Cdd:COG0746   78 ILAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRSG 124
 
Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 9-129 5.44e-14

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: 68.30  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   9 AIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRNSgrVNPIIVVGPPHL---GLHDVIWADVHDDM--LEN 82
Cdd:COG0746    7 GVILAG----GRsRRMGQDK---ALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPEryaALGVPVVPDDPPGAgpLAG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521042270  83 VLSGLNAVDEPTVLIATADIPLLTGYIVNAFLDQADPRYDVVYPVIE 129
Cdd:COG0746   78 ILAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRSG 124
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 7-129 7.00e-13

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: 64.90  E-value: 7.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   7 RPAIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRnsGRVNPIIVVGPPHL----GLHDVIWADVHDDM-- 79
Cdd:cd02503    1 ITGVILAG----GKsRRMGGDK---ALLELGGKPLLEHVLERLK--PLVDEVVISANRDQeryaLLGVPVIPDEPPGKgp 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 521042270  80 LENVLSGLNAVDEPTVLIATADIPLLTGYIVNAFLDQADPRYDVVYPVIE 129
Cdd:cd02503   72 LAGILAALRAAPADWVLVLACDMPFLPPELLERLLAAAEEGADAVVPKSG 121
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 9-127 1.30e-12

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: 63.75  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270    9 AIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRNSGRvnPIIVVGPP--------HLGLHDVIWADVHDDM 79
Cdd:pfam12804   1 AVILAG----GRsSRMGGDK---ALLPLGGKPLLERVLERLRPAGD--EVVVVANDeevlaalaGLGVPVVPDPDPGQGP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 521042270   80 LENVLSGLNAVDEPT-VLIATADIPLLTGYIVNAFLDQADP-RYDVVYPV 127
Cdd:pfam12804  72 LAGLLAALRAAPGADaVLVLACDMPFLTPELLRRLLAAAEEsGADIVVPV 121
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-126 2.06e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 45.13  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   3 PLNQRPAIVLAGqhndGKLRTISDKEwEAEILLQGRPMVEYVVEALRNsgRVNPII--VVGPPHL--GLHDVI--WADVH 76
Cdd:PRK14489   2 QISQIAGVILAG----GLSRRMNGRD-KALILLGGKPLIERVVDRLRP--QFARIHlnINRDPARyqDLFPGLpvYPDIL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521042270  77 DDM---LENVLSGLNAVDEPTVLIATADIPLLTGYIV----NAFLDQAdprYDVVYP 126
Cdd:PRK14489  75 PGFqgpLSGILAGLEHADSEYLFVVACDTPFLPENLVkrlsKALAIEG---ADIAVP 128
 
Name Accession Description Interval E-value
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 9-129 5.44e-14

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: 68.30  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   9 AIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRNSgrVNPIIVVGPPHL---GLHDVIWADVHDDM--LEN 82
Cdd:COG0746    7 GVILAG----GRsRRMGQDK---ALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPEryaALGVPVVPDDPPGAgpLAG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521042270  83 VLSGLNAVDEPTVLIATADIPLLTGYIVNAFLDQADPRYDVVYPVIE 129
Cdd:COG0746   78 ILAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRSG 124
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 7-129 7.00e-13

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: 64.90  E-value: 7.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   7 RPAIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRnsGRVNPIIVVGPPHL----GLHDVIWADVHDDM-- 79
Cdd:cd02503    1 ITGVILAG----GKsRRMGGDK---ALLELGGKPLLEHVLERLK--PLVDEVVISANRDQeryaLLGVPVIPDEPPGKgp 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 521042270  80 LENVLSGLNAVDEPTVLIATADIPLLTGYIVNAFLDQADPRYDVVYPVIE 129
Cdd:cd02503   72 LAGILAALRAAPADWVLVLACDMPFLPPELLERLLAAAEEGADAVVPKSG 121
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 9-127 1.30e-12

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: 63.75  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270    9 AIVLAGqhndGK-LRTISDKeweAEILLQGRPMVEYVVEALRNSGRvnPIIVVGPP--------HLGLHDVIWADVHDDM 79
Cdd:pfam12804   1 AVILAG----GRsSRMGGDK---ALLPLGGKPLLERVLERLRPAGD--EVVVVANDeevlaalaGLGVPVVPDPDPGQGP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 521042270   80 LENVLSGLNAVDEPT-VLIATADIPLLTGYIVNAFLDQADP-RYDVVYPV 127
Cdd:pfam12804  72 LAGLLAALRAAPGADaVLVLACDMPFLTPELLRRLLAAAEEsGADIVVPV 121
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 37-120 1.08e-08

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 53.35  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  37 GRPMVEYVVEALRNSGRVNPIIVVGP--P----HLGLHDVIWAD------VHDdmlenVLSGLNAVDEPtVLIATADIPL 104
Cdd:COG2266   21 GKPMIDRVIDALEESCIDKIYVAVSPntPktreYLKERGVEVIEtpgegyVED-----LNEALESISGP-VLVVPADLPL 94

                         90
                 ....*....|....*.
gi 521042270 105 LTGYIVNAFLDQADPR 120
Cdd:COG2266   95 LTPEIIDDIIDAYLES 110
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 35-127 2.93e-07

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: 49.48  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  35 LQGRPMVEYVVEALRNSGrVNPIIVVGPPH-------LGLHDVIWADVHD---DMLENVLSGLNAVDEPT--VLIATADI 102
Cdd:cd04182   23 LDGKPLLRHALDAALAAG-LSRVIVVLGAEadavraaLAGLPVVVVINPDweeGMSSSLAAGLEALPADAdaVLILLADQ 101

                         90       100
                 ....*....|....*....|....*.
gi 521042270 103 PLLTGYIVNAFLDQAD-PRYDVVYPV 127
Cdd:cd04182  102 PLVTAETLRALIDAFReDGAGIVAPV 127
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 33-128 9.09e-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: 9.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  33 ILLQGRPMVEYVVEALRNSGRVNPIIVVGPP-HLGLHDVIWADVHDDML-----------ENVLSGLNAVDEPT--VLIA 98
Cdd:COG1211   20 LPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPdDIEYFEELLAKYGIDKPvrvvaggatrqDSVRNGLEALPDDDdwVLVH 99

                         90       100       110
                 ....*....|....*....|....*....|
gi 521042270  99 TADIPLLTGYIVNAFLDQADpRYDVVYPVI 128
Cdd:COG1211  100 DAARPLVSPELIDRVIEAAR-EYGAAIPAL 128
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 37-115 1.73e-05

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: 45.40  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  37 GRPMVEYVVEALRNSGRVNPIIVVG------PPHLGLHDVIWAdVHDDML---ENVLSGLNAV--DEPTVLIATADIPLL 105
Cdd:COG1207   29 GKPMLEHVLDAARALGPDRIVVVVGhgaeqvRAALADLDVEFV-LQEEQLgtgHAVQQALPALpgDDGTVLVLYGDVPLI 107

                         90
                 ....*....|
gi 521042270 106 TGYIVNAFLD 115
Cdd:COG1207  108 RAETLKALLA 117
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-126 2.06e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 45.13  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270   3 PLNQRPAIVLAGqhndGKLRTISDKEwEAEILLQGRPMVEYVVEALRNsgRVNPII--VVGPPHL--GLHDVI--WADVH 76
Cdd:PRK14489   2 QISQIAGVILAG----GLSRRMNGRD-KALILLGGKPLIERVVDRLRP--QFARIHlnINRDPARyqDLFPGLpvYPDIL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521042270  77 DDM---LENVLSGLNAVDEPTVLIATADIPLLTGYIV----NAFLDQAdprYDVVYP 126
Cdd:PRK14489  75 PGFqgpLSGILAGLEHADSEYLFVVACDTPFLPENLVkrlsKALAIEG---ADIAVP 128
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 33-128 7.86e-05

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: 42.51  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  33 ILLQGRPMVEYVVEALRNSGRVNPIIVVGPPH----------LGLHDVIW-----ADVHDdmleNVLSGLNAV---DEPT 94
Cdd:cd02516   23 LELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDdidlakelakYGLSKVVKiveggATRQD----SVLNGLKALpdaDPDI 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 521042270  95 VLIATADIPLLTGYIVNAFLDQADpRYDVVYPVI 128
Cdd:cd02516   99 VLIHDAARPFVSPELIDRLIDALK-EYGAAIPAV 131
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
33-97 1.08e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 42.43  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521042270  33 ILLQGRPMVEYVVEALRNSGRVNPIIVVGPPHLG--LHDVIWADVHDDML--------ENVLSGLNAV-DEPTVLI 97
Cdd:PRK00155  26 LPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpdFAELLLAKDPKVTVvaggaerqDSVLNGLQALpDDDWVLV 101
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 37-106 2.77e-04

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: 40.96  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521042270  37 GRPMVEYVVEALRNSGRVNPIIVVGPP------HLGLHDVIWAdVHDDML---ENVLSGLNAVDEP--TVLIATADIPLL 105
Cdd:cd02540   25 GKPMLEHVLDAARALGPDRIVVVVGHGaeqvkkALANPNVEFV-LQEEQLgtgHAVKQALPALKDFegDVLVLYGDVPLI 103


                 .
gi 521042270 106 T 106
Cdd:cd02540  104 T 104
 
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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