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Conserved domains on  [gi|1195004357|gb|ARS39632|]
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radical SAM protein [Sphingobacteriaceae bacterium GW460-11-11-14-LB5]

Protein Classification

menaquinone biosynthetic enzyme MqnA/MqnD family protein( domain architecture ID 10003665)

menaquinone biosynthetic enzyme MqnA/MqnD family protein similar to Campylobacter jejuni MqnA which catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
3-241 1.07e-83

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 441036  Cd Length: 268  Bit Score: 250.52  E-value: 1.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDIINKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPL-VPNANIVADYCIGSDGGVNS 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARhADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  82 VFIFSEVPAREI--KTVRLDSHSRTSNNLAKVLLKFHWKKEVEFTTDPT------AKTDAFVLIGDRTFG--KKDDFAYA 151
Cdd:COG1427    81 VLLFSRVPLEELdgKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPdleamlEGADAALLIGDRALRaaARGRFPYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 152 YDMGEEWKNFTGLPFMYAAWVANKEI-----SQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYLyHRLQFDV 223
Cdd:COG1427   161 YDLGEEWKELTGLPFVFAVWAVRRDAaeanpVAELHEALLEAKERGLAHLDEIAEEAARRLGLPpelLEDYL-RNLRYDL 239
                         250
                  ....*....|....*...
gi 1195004357 224 TDDRRKALKLFLGYIEEL 241
Cdd:COG1427   240 GEEERKGLRLFYEYAAEL 257
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
3-241 1.07e-83

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441036  Cd Length: 268  Bit Score: 250.52  E-value: 1.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDIINKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPL-VPNANIVADYCIGSDGGVNS 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARhADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  82 VFIFSEVPAREI--KTVRLDSHSRTSNNLAKVLLKFHWKKEVEFTTDPT------AKTDAFVLIGDRTFG--KKDDFAYA 151
Cdd:COG1427    81 VLLFSRVPLEELdgKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPdleamlEGADAALLIGDRALRaaARGRFPYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 152 YDMGEEWKNFTGLPFMYAAWVANKEI-----SQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYLyHRLQFDV 223
Cdd:COG1427   161 YDLGEEWKELTGLPFVFAVWAVRRDAaeanpVAELHEALLEAKERGLAHLDEIAEEAARRLGLPpelLEDYL-RNLRYDL 239
                         250
                  ....*....|....*...
gi 1195004357 224 TDDRRKALKLFLGYIEEL 241
Cdd:COG1427   240 GEEERKGLRLFYEYAAEL 257
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
3-237 1.63e-73

The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein fold; This group includes the SCO4506 protein from Streptomyces coelicolor and related hypothetical proteins. SCO4506 is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. SCO4506 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270352  Cd Length: 256  Bit Score: 224.35  E-value: 1.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDIINKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIP-LVPNANIVADYCIGSDGGVNS 81
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGKVPPGFELVLGVPSELNRMLLEGELDVGLVSSIEYArNADDYLILPDLSISSDGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  82 VFIFSEVPA--REIKTVRLDSHSRTSNNLAKVLLKFHWKKEVEFTT------DPTAKTDAFVLIGDRTFG--KKDDFAYA 151
Cdd:cd13634    81 VLLFSKVPLeeLEGKRVALTTESATSVALLKILLEEFYGLEPEYVPappdldEMLADADAALLIGDDALRarASGRGPYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 152 YDMGEEWKNFTGLPFMYAAWVANKEI------SQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYlYHRLQFD 222
Cdd:cd13634   161 YDLGEEWKELTGLPFVFAVWAVRRDAaerpeeLAELVQALLESKRYGLANLEEIIAEAAERLGLSeefLRDY-FTNLRYD 239
                         250
                  ....*....|....*
gi 1195004357 223 VTDDRRKALKLFLGY 237
Cdd:cd13634   240 LGEEELEGLELFYRY 254
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-240 1.31e-48

Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine. These enzymes comprise two domains with alpha/beta structures, a large domain and a small domain. A pocket between the two domains may form the active site, a conserved histidine located within this pocket could be the catalytic base.


Pssm-ID: 426881  Cd Length: 252  Bit Score: 160.41  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   4 IKISAVAYTNTKAFIYGLTHSDIINkIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPLVPNA-NIVADYCIGSDGGVNSV 82
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALVHDEGLD-FEIVLGDPETLNRMLLEGELDVSAISSAAYARNADDyVLLPDLSGSALGRVYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  83 FIFSEVP--AREIKTVRLDSHSRTSNNLAKVLLKFHWKKeVEFTTDPT-------AKTDAFVLIGDRTFGKKD-DFAYAY 152
Cdd:pfam02621  80 LLVSRVPelDGDGKRVALPGESTTSVLLLRLLLPERYGK-PRYVPMPDeimaavlEGEDAGLLIGDSALTYAErGLKKVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 153 DMGEEWKNFTGLPFMYAAWVANK----EISQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYlYHRLQFDVTD 225
Cdd:pfam02621 159 DLGEWWKELTGLPMPFGLWVVRRdlalETAKELEEALRASKEYALAHPDEIAEYAAEHAQEMeefLRLY-VNELSYDLGE 237
                         250
                  ....*....|....*
gi 1195004357 226 DRRKALKLFLGYIEE 240
Cdd:pfam02621 238 EGRAGLEEFYERAAE 252
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
3-241 1.07e-83

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441036  Cd Length: 268  Bit Score: 250.52  E-value: 1.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDIINKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPL-VPNANIVADYCIGSDGGVNS 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARhADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  82 VFIFSEVPAREI--KTVRLDSHSRTSNNLAKVLLKFHWKKEVEFTTDPT------AKTDAFVLIGDRTFG--KKDDFAYA 151
Cdd:COG1427    81 VLLFSRVPLEELdgKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPdleamlEGADAALLIGDRALRaaARGRFPYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 152 YDMGEEWKNFTGLPFMYAAWVANKEI-----SQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYLyHRLQFDV 223
Cdd:COG1427   161 YDLGEEWKELTGLPFVFAVWAVRRDAaeanpVAELHEALLEAKERGLAHLDEIAEEAARRLGLPpelLEDYL-RNLRYDL 239
                         250
                  ....*....|....*...
gi 1195004357 224 TDDRRKALKLFLGYIEEL 241
Cdd:COG1427   240 GEEERKGLRLFYEYAAEL 257
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
3-237 1.63e-73

The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein fold; This group includes the SCO4506 protein from Streptomyces coelicolor and related hypothetical proteins. SCO4506 is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. SCO4506 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270352  Cd Length: 256  Bit Score: 224.35  E-value: 1.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDIINKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIP-LVPNANIVADYCIGSDGGVNS 81
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGKVPPGFELVLGVPSELNRMLLEGELDVGLVSSIEYArNADDYLILPDLSISSDGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  82 VFIFSEVPA--REIKTVRLDSHSRTSNNLAKVLLKFHWKKEVEFTT------DPTAKTDAFVLIGDRTFG--KKDDFAYA 151
Cdd:cd13634    81 VLLFSKVPLeeLEGKRVALTTESATSVALLKILLEEFYGLEPEYVPappdldEMLADADAALLIGDDALRarASGRGPYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 152 YDMGEEWKNFTGLPFMYAAWVANKEI------SQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYlYHRLQFD 222
Cdd:cd13634   161 YDLGEEWKELTGLPFVFAVWAVRRDAaerpeeLAELVQALLESKRYGLANLEEIIAEAAERLGLSeefLRDY-FTNLRYD 239
                         250
                  ....*....|....*
gi 1195004357 223 VTDDRRKALKLFLGY 237
Cdd:cd13634   240 LGEEELEGLELFYRY 254
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-240 1.31e-48

Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine. These enzymes comprise two domains with alpha/beta structures, a large domain and a small domain. A pocket between the two domains may form the active site, a conserved histidine located within this pocket could be the catalytic base.


Pssm-ID: 426881  Cd Length: 252  Bit Score: 160.41  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   4 IKISAVAYTNTKAFIYGLTHSDIINkIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPLVPNA-NIVADYCIGSDGGVNSV 82
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALVHDEGLD-FEIVLGDPETLNRMLLEGELDVSAISSAAYARNADDyVLLPDLSGSALGRVYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  83 FIFSEVP--AREIKTVRLDSHSRTSNNLAKVLLKFHWKKeVEFTTDPT-------AKTDAFVLIGDRTFGKKD-DFAYAY 152
Cdd:pfam02621  80 LLVSRVPelDGDGKRVALPGESTTSVLLLRLLLPERYGK-PRYVPMPDeimaavlEGEDAGLLIGDSALTYAErGLKKVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357 153 DMGEEWKNFTGLPFMYAAWVANK----EISQEFKAEFNAALKFGLKHRKDVLKELPEVQNFD---LEDYlYHRLQFDVTD 225
Cdd:pfam02621 159 DLGEWWKELTGLPMPFGLWVVRRdlalETAKELEEALRASKEYALAHPDEIAEYAAEHAQEMeefLRLY-VNELSYDLGE 237
                         250
                  ....*....|....*
gi 1195004357 226 DRRKALKLFLGYIEE 240
Cdd:pfam02621 238 EGRAGLEEFYERAAE 252
PBP2_MqnD_like cd13534
Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 ...
3-214 2.76e-10

Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 periplasmic-binding protein fold; This family represents MqnD, an enzyme within the alternative menaquinone biosynthetic pathway, and related conserved hypothetical proteins. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. The members include Ttha1568, MqnD from Thermus thermophiles HB8, and the conserved hypothetical proteins SCO4506 from Streptomyces coelicolor, Af1704 from Archaeoglobus DSM 4304, Dr0370 from Deinococcus radiodurans, and Ca3427 from candida albicans. They all have significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270252 [Multi-domain]  Cd Length: 261  Bit Score: 58.97  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357   3 KIKISAVAYTNTKAFIYGLTHSDI---INKIDLSLDIPSDCAAKVINGQVDIGLMPVAAIPLVPNaNIVA--DYCIGSDG 77
Cdd:cd13534     1 TIRVGHSPDADDLFLFYALKHGWVketDLIFENVKEDVETLNELALKNELDVSAISFAAYPKIAD-DYVIlpTGAVFGDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195004357  78 GVNSVFIFSEVPAREIKTVRLDSHSRTSNNLAKVLLKfhwkKEVEFTTDP---------TAKTDAFVLIGDRTFgkKDDF 148
Cdd:cd13534    80 YGPVLVAKSPLDDKQGKRVAVSGRNTTAYLLLKLLAP----QYFRPIVVRfddiedavlEGEVDAGVLIHESIL--MTYP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195004357 149 AYA----YDMGEEWKNFTGLPFMYAAWVANKEISQE----FKAEFNAALKFGLKHRKDVLKELpeVQNFDLEDY 214
Cdd:cd13534   154 RYGlkvvRDLWDLWKESTNLPLPLGVVAIRRDLGEDliraFKEAVLLSKAYALAHPDEAIEYM--LQEAREIRL 225
MqnD COG2107
1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) [Coenzyme ...
153-201 1.16e-04

1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; 1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441710  Cd Length: 276  Bit Score: 42.43  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1195004357 153 DMGEEWKNFTGLPFMYAAWVANKEISQEFKAEFNAAL----KFGLKHRKDVLK 201
Cdd:COG2107   165 DLGEWWEEETGLPLPLGGNVIRRDLGEEVARKIEEALrksiKYALAHPDEALE 217
 
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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