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Conserved domains on  [gi|501039518|ref|WP_012091464|]
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MULTISPECIES: 1-deoxy-D-ribulose 5-phosphate reductoisomerase [Brucella/Ochrobactrum group]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 11467855)

NAD(P)H-dependent oxidoreductase which catalyzes the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+, such as 1-deoxy-D-ribulose 5-phosphate reductoisomerase, which catalyzes the NADPH-dependent production of the methylerythritol 4-phosphate (MEP) for isoprenoid biosynthesis in bacteria

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
9-436 0e+00

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


:

Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 644.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   9 GLARDLAARAETGKPIRIGLIGAGEMGTDIVTQVARMQGIEVGALSARRLPNTFKAVRTAYGDEENAREARTESAMTSAI 88
Cdd:COG4091    1 NLDRLLAARAAEGRPIRVGLIGAGQMGRGLLAQIRRMPGMEVVAIADRNPERARAALREAGIPEEDIRVVDTAAEADAAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518  89 ESGKIAVTDDNDLILSNPLLDVIIDATGIPEVGAQTGIKAIRNGKHLVMMNVEADVTIGPYLKAEADKHGVIYSLGAGDE 168
Cdd:COG4091   81 AAGKTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGVVYTGADGDQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 169 PSSCMELIEFVSAMGHKVVAAGKGKNNPLNFDAIPDDYQEEADRRNMNVRLLVEFVDGSKTMVEMAAIANATGLVPDIAG 248
Cdd:COG4091  161 PGLIMELYDFARALGFEVVAAGKGKNNPLDDYATPDTQAEEAERKGMNPKMLASFADGTKTMVEMAAVANATGLVPDVRG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 249 MHGPKAAIDELNRTLIPKEDGGVLNKTGVVDYSIGRGVSPGVFVIAKMEHPRLVERLEDLKMGKGPYFTFHRPFHLTSLE 328
Cdd:COG4091  241 MHGPPARVDELPDVFRPKEDGGILERGGVVDYVVGLSVAPGVFVIVTADDPYVRHCLNYYKLGDGPYYSLYRPYHLCGLE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 329 VPLTVARVVLHGKTDMVPLPKPVAEVCAVAKKDLQPGDHLDAIGQYCYRSWIMTTPEAHAAKAIPCGLLQNGTVIAPIRK 408
Cdd:COG4091  321 TPLSVARAVLRGEATGAPLGRPVAEVVAVAKRDLKAGEVLDGIGGYTVYGKLEPAEVARAENLLPIGLAEGCRLKRDVKK 400
                        410       420
                 ....*....|....*....|....*...
gi 501039518 409 GELITYANAAPQPGSKIAELRALQDKMI 436
Cdd:COG4091  401 GEVITYDDVELDEGSLIVRLRREQDALF 428
 
Name Accession Description Interval E-value
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
9-436 0e+00

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 644.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   9 GLARDLAARAETGKPIRIGLIGAGEMGTDIVTQVARMQGIEVGALSARRLPNTFKAVRTAYGDEENAREARTESAMTSAI 88
Cdd:COG4091    1 NLDRLLAARAAEGRPIRVGLIGAGQMGRGLLAQIRRMPGMEVVAIADRNPERARAALREAGIPEEDIRVVDTAAEADAAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518  89 ESGKIAVTDDNDLILSNPLLDVIIDATGIPEVGAQTGIKAIRNGKHLVMMNVEADVTIGPYLKAEADKHGVIYSLGAGDE 168
Cdd:COG4091   81 AAGKTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGVVYTGADGDQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 169 PSSCMELIEFVSAMGHKVVAAGKGKNNPLNFDAIPDDYQEEADRRNMNVRLLVEFVDGSKTMVEMAAIANATGLVPDIAG 248
Cdd:COG4091  161 PGLIMELYDFARALGFEVVAAGKGKNNPLDDYATPDTQAEEAERKGMNPKMLASFADGTKTMVEMAAVANATGLVPDVRG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 249 MHGPKAAIDELNRTLIPKEDGGVLNKTGVVDYSIGRGVSPGVFVIAKMEHPRLVERLEDLKMGKGPYFTFHRPFHLTSLE 328
Cdd:COG4091  241 MHGPPARVDELPDVFRPKEDGGILERGGVVDYVVGLSVAPGVFVIVTADDPYVRHCLNYYKLGDGPYYSLYRPYHLCGLE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 329 VPLTVARVVLHGKTDMVPLPKPVAEVCAVAKKDLQPGDHLDAIGQYCYRSWIMTTPEAHAAKAIPCGLLQNGTVIAPIRK 408
Cdd:COG4091  321 TPLSVARAVLRGEATGAPLGRPVAEVVAVAKRDLKAGEVLDGIGGYTVYGKLEPAEVARAENLLPIGLAEGCRLKRDVKK 400
                        410       420
                 ....*....|....*....|....*...
gi 501039518 409 GELITYANAAPQPGSKIAELRALQDKMI 436
Cdd:COG4091  401 GEVITYDDVELDEGSLIVRLRREQDALF 428
SAF_DH_OX_like cd11616
SAF domain of putative dehydrogenases or oxidoreductases; C-terminal SAF domain of an ...
354-433 6.92e-26

SAF domain of putative dehydrogenases or oxidoreductases; C-terminal SAF domain of an uncharacterized family of putative dehydrogenases or oxidoreductases, which are otherwise members of the NAD(P)-dependent Rossmann-fold superfamily.


Pssm-ID: 212161  Cd Length: 80  Bit Score: 99.88  E-value: 6.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 354 VCAVAKKDLQPGDHLDAIGQYCYRSWIMTTPEAHAAKAIPCGLLQNGTVIAPIRKGELITYANAAPQPGSKIAELRALQD 433
Cdd:cd11616    1 VVAVAKRDLKAGEVLDGIGGYTVYGGLEPAADARAENALPIGLATGARLKRDVKKGELITYDDVELDEGSLAVRLRREQD 80
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
30-161 1.25e-07

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 50.00  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   30 GAGEMGTDIVTQVARMQ---GIEVGALSARRLPntfkavrtaygDEENAREARTEsamtsaiesgkiAVTDDNDLILSNP 106
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQseiPLELVAVADRDLL-----------SKDPLALLPDE------------PLTLDLDDLIAHP 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 501039518  107 LLDVIIDATGiPEVGAQTGIKAIRNGKHLVMMNVEA--DVTIGPYLKAEADKHGVIY 161
Cdd:pfam03447  58 DPDVVVECAS-SEAVAELVLDALKAGKDVVTASKGAlaDLALYEELREAAEANGARI 113
 
Name Accession Description Interval E-value
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
9-436 0e+00

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 644.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   9 GLARDLAARAETGKPIRIGLIGAGEMGTDIVTQVARMQGIEVGALSARRLPNTFKAVRTAYGDEENAREARTESAMTSAI 88
Cdd:COG4091    1 NLDRLLAARAAEGRPIRVGLIGAGQMGRGLLAQIRRMPGMEVVAIADRNPERARAALREAGIPEEDIRVVDTAAEADAAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518  89 ESGKIAVTDDNDLILSNPLLDVIIDATGIPEVGAQTGIKAIRNGKHLVMMNVEADVTIGPYLKAEADKHGVIYSLGAGDE 168
Cdd:COG4091   81 AAGKTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGVVYTGADGDQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 169 PSSCMELIEFVSAMGHKVVAAGKGKNNPLNFDAIPDDYQEEADRRNMNVRLLVEFVDGSKTMVEMAAIANATGLVPDIAG 248
Cdd:COG4091  161 PGLIMELYDFARALGFEVVAAGKGKNNPLDDYATPDTQAEEAERKGMNPKMLASFADGTKTMVEMAAVANATGLVPDVRG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 249 MHGPKAAIDELNRTLIPKEDGGVLNKTGVVDYSIGRGVSPGVFVIAKMEHPRLVERLEDLKMGKGPYFTFHRPFHLTSLE 328
Cdd:COG4091  241 MHGPPARVDELPDVFRPKEDGGILERGGVVDYVVGLSVAPGVFVIVTADDPYVRHCLNYYKLGDGPYYSLYRPYHLCGLE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 329 VPLTVARVVLHGKTDMVPLPKPVAEVCAVAKKDLQPGDHLDAIGQYCYRSWIMTTPEAHAAKAIPCGLLQNGTVIAPIRK 408
Cdd:COG4091  321 TPLSVARAVLRGEATGAPLGRPVAEVVAVAKRDLKAGEVLDGIGGYTVYGKLEPAEVARAENLLPIGLAEGCRLKRDVKK 400
                        410       420
                 ....*....|....*....|....*...
gi 501039518 409 GELITYANAAPQPGSKIAELRALQDKMI 436
Cdd:COG4091  401 GEVITYDDVELDEGSLIVRLRREQDALF 428
SAF_DH_OX_like cd11616
SAF domain of putative dehydrogenases or oxidoreductases; C-terminal SAF domain of an ...
354-433 6.92e-26

SAF domain of putative dehydrogenases or oxidoreductases; C-terminal SAF domain of an uncharacterized family of putative dehydrogenases or oxidoreductases, which are otherwise members of the NAD(P)-dependent Rossmann-fold superfamily.


Pssm-ID: 212161  Cd Length: 80  Bit Score: 99.88  E-value: 6.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518 354 VCAVAKKDLQPGDHLDAIGQYCYRSWIMTTPEAHAAKAIPCGLLQNGTVIAPIRKGELITYANAAPQPGSKIAELRALQD 433
Cdd:cd11616    1 VVAVAKRDLKAGEVLDGIGGYTVYGGLEPAADARAENALPIGLATGARLKRDVKKGELITYDDVELDEGSLAVRLRREQD 80
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
30-161 1.25e-07

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 50.00  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   30 GAGEMGTDIVTQVARMQ---GIEVGALSARRLPntfkavrtaygDEENAREARTEsamtsaiesgkiAVTDDNDLILSNP 106
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQseiPLELVAVADRDLL-----------SKDPLALLPDE------------PLTLDLDDLIAHP 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 501039518  107 LLDVIIDATGiPEVGAQTGIKAIRNGKHLVMMNVEA--DVTIGPYLKAEADKHGVIY 161
Cdd:pfam03447  58 DPDVVVECAS-SEAVAELVLDALKAGKDVVTASKGAlaDLALYEELREAAEANGARI 113
MviM COG0673
Predicted dehydrogenase [General function prediction only];
22-164 5.08e-06

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 48.00  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518  22 KPIRIGLIGAGEMGTDIVTQVARMQGIEVGALSARrlpntfkavrtaygDEENAREARTESamtsaiesgKIAVTDDNDL 101
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR--------------DPERAEAFAEEY---------GVRVYTDYEE 58
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501039518 102 ILSNPLLDVIIDATgIPEVGAQTGIKAIRNGKHLVM-----MNV-EADVtigpyLKAEADKHGVIYSLG 164
Cdd:COG0673   59 LLADPDIDAVVIAT-PNHLHAELAIAALEAGKHVLCekplaLTLeEARE-----LVAAAEEAGVVLMVG 121
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
24-158 2.79e-04

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 42.48  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518  24 IRIGLIGAGEMGTDIVTQVArMQGIEVGALSARrlpntfkavrtaygdeeNAREARTESAMTSAiesgkIAVTDDNDLIL 103
Cdd:COG1712    1 MRIGLIGCGAIGSEVAEALA-DAGVELVAVYDR-----------------DPERAEALLASLGA-----RVVSDVDELLA 57
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501039518 104 SNPllDVIIDATGIPEVgAQTGIKAIRNGKHLVMMNVEA--DVTIGPYLKAEADKHG 158
Cdd:COG1712   58 ADP--DLVVEAASQAAV-REHGPAVLEAGKDLMIMSVGAlaDEELLERLEAAAREGG 111
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
24-164 8.60e-03

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 36.03  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039518   24 IRIGLIGAGEMGTDIVTQVARMQ-GIEVGALSARRLPNtFKAVRTAYGdeenareartesamtsaiesgkIAVTDDNDLI 102
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQpGAELVAILDPNSER-AEAVAESFG----------------------VEVYSDLEEL 57
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501039518  103 LSNPLLDVIIDATGiPEVGAQTGIKAIRNGKHLVM-----MNVEADVTigpyLKAEADKHGVIYSLG 164
Cdd:pfam01408  58 LNDPEIDAVIVATP-NGLHYDLAIAALEAGKHVLCekplaTTVEEAKE----LVELAKKKGVRVSVG 119
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
355-416 9.77e-03

SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.


Pssm-ID: 430140 [Multi-domain]  Cd Length: 63  Bit Score: 34.45  E-value: 9.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501039518  355 CAVAKKDLQPGDHLDAIGQYCYRswiMTTPEAHAAKAIPCGLLQNGTVIAPIRKGELITYAN 416
Cdd:pfam08666   3 VVVAARDLPAGEVITADDLTLVR---PPLALPPGLFPIAYGEVIGKVARRDIAAGEPLTASD 61
 
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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