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Conserved domains on  [gi|446394150|ref|WP_000472005|]
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MULTISPECIES: glycerol-3-phosphate responsive antiterminator [Bacillus]

Protein Classification

glycerol-3-phosphate responsive antiterminator( domain architecture ID 10005001)

glycerol-3-phosphate responsive antiterminator similar to Bacillus subtilis GlpP, which binds to glpD leader mRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlpP COG1954
Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];
1-178 7.20e-75

Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];


:

Pssm-ID: 441557  Cd Length: 178  Bit Score: 222.66  E-value: 7.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150   1 MFKEPYIAMIKDWKG-YKAYKQLPKTVFLMTGSMLELPERVYELQKHGHDVFLHCDFIQGLnTNTEEALLYIQDVIGAQG 79
Cdd:COG1954    1 LAENPIIPAVRDLKDlEKALKSDVEVIFLLNGDIGNLKSIVKRLKQAGKKVFVHIDLIEGL-SNDEYGIEYLKQEIKPDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150  80 IISTKGSTIRNANKIGLKTIQRIFIVDTLSLTKSIENCKTTKPNAVEIMPGIMPSIIKQLAEEIEFPIIAGGLIQTREDA 159
Cdd:COG1954   80 IISTKSNLIKAAKKEGLLTIQRLFLIDSSALETGIKLIEKSKPDAIEILPGIMPKVIKEIKKETGIPIIAGGLIRTKEDV 159

                        170
                 ....*....|....*....
gi 446394150 160 EIAIRAGASAISTSHYEVW 178
Cdd:COG1954  160 EAALAAGAIAVSTSNKELW 178
 
Name Accession Description Interval E-value
GlpP COG1954
Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];
1-178 7.20e-75

Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];


Pssm-ID: 441557  Cd Length: 178  Bit Score: 222.66  E-value: 7.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150   1 MFKEPYIAMIKDWKG-YKAYKQLPKTVFLMTGSMLELPERVYELQKHGHDVFLHCDFIQGLnTNTEEALLYIQDVIGAQG 79
Cdd:COG1954    1 LAENPIIPAVRDLKDlEKALKSDVEVIFLLNGDIGNLKSIVKRLKQAGKKVFVHIDLIEGL-SNDEYGIEYLKQEIKPDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150  80 IISTKGSTIRNANKIGLKTIQRIFIVDTLSLTKSIENCKTTKPNAVEIMPGIMPSIIKQLAEEIEFPIIAGGLIQTREDA 159
Cdd:COG1954   80 IISTKSNLIKAAKKEGLLTIQRLFLIDSSALETGIKLIEKSKPDAIEILPGIMPKVIKEIKKETGIPIIAGGLIRTKEDV 159

                        170
                 ....*....|....*....
gi 446394150 160 EIAIRAGASAISTSHYEVW 178
Cdd:COG1954  160 EAALAAGAIAVSTSNKELW 178
G3P_antiterm pfam04309
Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to ...
 7-178 1.37e-72

Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to glycerol-3-phosphate in an ATP-requiring phosphorylation reaction catalyzed by glycerol kinase (GlpK) glycerol-3-phosphate activates the antiterminator GlpP.


Pssm-ID: 427855  Cd Length: 173  Bit Score: 216.50  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150    7 IAMIKDWKGY-KAYKQLPKTVFLMTGSMLELPERVYELQKHGHDVFLHCDFIQGLnTNTEEALLYIQDVIGAQGIISTKG 85
Cdd:pfam04309   2 IAAVRDEKDLeKALESDVEVVFLLNGDIGNLKSIVERLKAAGKKVFVHIDLIEGL-SRDEAAVDFLKKYIGPDGIISTKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150   86 STIRNANKIGLKTIQRIFIVDTLSLTKSIENCKTTKPNAVEIMPGIMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRA 165
Cdd:pfam04309  81 NLIKRAKKLGLLTIQRLFLIDSSALENGLKQIESSKPDAVEILPGLMPKVIKEIKEELGIPIIAGGLIRTKEDVEEALKA 160

                         170
                  ....*....|...
gi 446394150  166 GASAISTSHYEVW 178
Cdd:pfam04309 161 GAIAVSTSNKELW 173
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 130-175 2.19e-05

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 43.97  E-value: 2.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446394150 130 GIMPSIIKQLAEEIEFPIIAGGlIQTREDAEIAIRAGASAISTSHY 175
Cdd:cd04737  207 KLSPADIEFIAKISGLPVIVKG-IQSPEDADVAINAGADGIWVSNH 251
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 131-172 4.81e-04

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 39.66  E-value: 4.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446394150  131 IMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAIST 172
Cdd:TIGR00735  61 TMIDVVERTAETVFIPLTVGGGIKSIEDVDKLLRAGADKVSI 102
 
Name Accession Description Interval E-value
GlpP COG1954
Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];
1-178 7.20e-75

Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];


Pssm-ID: 441557  Cd Length: 178  Bit Score: 222.66  E-value: 7.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150   1 MFKEPYIAMIKDWKG-YKAYKQLPKTVFLMTGSMLELPERVYELQKHGHDVFLHCDFIQGLnTNTEEALLYIQDVIGAQG 79
Cdd:COG1954    1 LAENPIIPAVRDLKDlEKALKSDVEVIFLLNGDIGNLKSIVKRLKQAGKKVFVHIDLIEGL-SNDEYGIEYLKQEIKPDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150  80 IISTKGSTIRNANKIGLKTIQRIFIVDTLSLTKSIENCKTTKPNAVEIMPGIMPSIIKQLAEEIEFPIIAGGLIQTREDA 159
Cdd:COG1954   80 IISTKSNLIKAAKKEGLLTIQRLFLIDSSALETGIKLIEKSKPDAIEILPGIMPKVIKEIKKETGIPIIAGGLIRTKEDV 159

                        170
                 ....*....|....*....
gi 446394150 160 EIAIRAGASAISTSHYEVW 178
Cdd:COG1954  160 EAALAAGAIAVSTSNKELW 178
G3P_antiterm pfam04309
Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to ...
 7-178 1.37e-72

Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to glycerol-3-phosphate in an ATP-requiring phosphorylation reaction catalyzed by glycerol kinase (GlpK) glycerol-3-phosphate activates the antiterminator GlpP.


Pssm-ID: 427855  Cd Length: 173  Bit Score: 216.50  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150    7 IAMIKDWKGY-KAYKQLPKTVFLMTGSMLELPERVYELQKHGHDVFLHCDFIQGLnTNTEEALLYIQDVIGAQGIISTKG 85
Cdd:pfam04309   2 IAAVRDEKDLeKALESDVEVVFLLNGDIGNLKSIVERLKAAGKKVFVHIDLIEGL-SRDEAAVDFLKKYIGPDGIISTKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150   86 STIRNANKIGLKTIQRIFIVDTLSLTKSIENCKTTKPNAVEIMPGIMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRA 165
Cdd:pfam04309  81 NLIKRAKKLGLLTIQRLFLIDSSALENGLKQIESSKPDAVEILPGLMPKVIKEIKEELGIPIIAGGLIRTKEDVEEALKA 160

                         170
                  ....*....|...
gi 446394150  166 GASAISTSHYEVW 178
Cdd:pfam04309 161 GAIAVSTSNKELW 173
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 130-175 2.19e-05

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 43.97  E-value: 2.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446394150 130 GIMPSIIKQLAEEIEFPIIAGGlIQTREDAEIAIRAGASAISTSHY 175
Cdd:cd04737  207 KLSPADIEFIAKISGLPVIVKG-IQSPEDADVAINAGADGIWVSNH 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 131-171 1.55e-04

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 40.91  E-value: 1.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446394150 131 IMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAIS 171
Cdd:cd04731   58 TMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGADKVS 98
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 131-172 4.81e-04

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 39.66  E-value: 4.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446394150  131 IMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAIST 172
Cdd:TIGR00735  61 TMIDVVERTAETVFIPLTVGGGIKSIEDVDKLLRAGADKVSI 102
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 130-171 6.75e-04

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 39.24  E-value: 6.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446394150 130 GIMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAIS 171
Cdd:COG0107   59 KTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVS 100
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 88-170 8.77e-04

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238 [Multi-domain]  Cd Length: 344  Bit Score: 39.12  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394150  88 IRNANKIGLKTIqrIFIVD-----------------TLSLTKSIENCKTTKPNAVEIMPGIMPS-----IIKQLAEEIEF 145
Cdd:cd02922  137 LKRAEKLGAKAI--FLTVDapvlgkrerderlkaeeAVSDGPAGKKTKAKGGGAGRAMSGFIDPtltwdDIKWLRKHTKL 214

                         90       100
                 ....*....|....*....|....*
gi 446394150 146 PIIAGGlIQTREDAEIAIRAGASAI 170
Cdd:cd02922  215 PIVLKG-VQTVEDAVLAAEYGVDGI 238
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 129-170 9.40e-04

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 38.95  E-value: 9.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446394150  129 PGIMPSIIK---QLAEEIEFPIIAGGLIQTREDAEIAIRAGASAI 170
Cdd:TIGR01037 216 PAIKPIALRmvyDVYKMVDIPIIGVGGITSFEDALEFLMAGASAV 260
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 129-170 1.33e-03

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 38.30  E-value: 1.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446394150 129 PGIMP---SIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAI 170
Cdd:cd04740  213 PAIKPialRMVYQVYKAVEIPIIGVGGIASGEDALEFLMAGASAV 257
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 130-171 1.59e-03

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 37.84  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446394150  130 GIMPSIIKQLAEEIEFPIIAGGLIQTREDAEIAIRAGASAIS 171
Cdd:pfam00977  59 PVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVI 100
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 136-170 2.40e-03

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 37.80  E-value: 2.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446394150 136 IKQLAEEIEFPIIAGGlIQTREDAEIAIRAGASAI 170
Cdd:COG1304  217 IAWLRERWPGPLIVKG-VLSPEDARRAVDAGVDGI 250
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 136-174 6.81e-03

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 36.27  E-value: 6.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446394150 136 IKQLAEEIEFPIIAGGlIQTREDAEIAIRAGASAISTSH 174
Cdd:cd02809  164 LAWLRSQWKGPLILKG-ILTPEDALRAVDAGADGIVVSN 201
FMN_dh pfam01070
FMN-dependent dehydrogenase;
136-170 8.17e-03

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 35.97  E-value: 8.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446394150  136 IKQLAEEIEFPIIAGGlIQTREDAEIAIRAGASAI 170
Cdd:pfam01070 210 LAWLRERWKGPLVVKG-ILSPEDAKRAVEAGVDGI 243
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 111-170 9.64e-03

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 35.82  E-value: 9.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446394150 111 TKSIE-NCKTTKPNAVEIM-----PGIMP---SIIKQLAEE--IEFPIIAGGLIQTREDAEIAIRAGASAI 170
Cdd:COG0167  192 TLGRAiDLETRRPVLANEAgglsgPALKPialRMVREVAQAvgGDIPIIGVGGISTAEDALEFILAGASAV 262
 
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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