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Conserved domains on  [gi|1327850588|ref|NP_001346676|]
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cytokine-like nuclear factor N-PAC isoform 3 [Mus musculus]

Protein Classification

PWWP and MmsB domain-containing protein( domain architecture ID 11638485)

PWWP and MmsB domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 198-475 1.45e-101

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 305.50  E-value: 1.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 271
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 272 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 351
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 352 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 431
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327850588 432 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PWWP super family cl02554
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 1-21 4.42e-03

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


The actual alignment was detected with superfamily member cd05836:

Pssm-ID: 470613 [Multi-domain]  Cd Length: 86  Bit Score: 36.43  E-value: 4.42e-03
                          10        20
                  ....*....|....*....|.
gi 1327850588   1 MIKINKGKRFQQAVDAVEEFL 21
Cdd:cd05836    66 MLKSKKSAGFKDAVEAIEEYI 86
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 198-475 1.45e-101

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 305.50  E-value: 1.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 271
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 272 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 351
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 352 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 431
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327850588 432 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 198-475 6.65e-52

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 177.55  E-value: 6.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE------KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 271
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEavaeviAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 272 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 351
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 352 GEV--GNAAKM--MLIVNMVqgsfMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYI 427
Cdd:PRK11559  163 GDIgaGNVTKLanQVIVALN----IAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLH 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1327850588 428 QKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:PRK11559  239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 199-352 1.40e-48

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 164.18  E-value: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPsGVL 272
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKveelvaAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 273 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 352
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 199-475 8.84e-45

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 158.51  E-value: 8.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 272
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVadellaAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 273 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 352
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 353 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLR 432
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1327850588 433 LAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 140-263 3.60e-03

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 39.56  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 140 VKDAdphfhhFLLSQTEKPA------VCYQAIT--KKLKiceEET----GSTSI-QAADSTAVNGSITPTDKKIGFLGLG 206
Cdd:cd05213   117 VKNA------YKLAKEAGTSgkllnrLFQKAIKvgKRVR---TETgisrGAVSIsSAAVELAEKIFGNLKGKKVLVIGAG 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850588 207 LMGSGIVSNLLKMGHT-VTVWNRTAEKEGARLGRTPAEVVS---------TCDITFACVSDPKAAKD 263
Cdd:cd05213   188 EMGELAAKHLAAKGVAeITIANRTYERAEELAKELGGNAVPldellellnEADVVISATGAPHYAKI 254
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 1-21 4.42e-03

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 36.43  E-value: 4.42e-03
                          10        20
                  ....*....|....*....|.
gi 1327850588   1 MIKINKGKRFQQAVDAVEEFL 21
Cdd:cd05836    66 MLKSKKSAGFKDAVEAIEEYI 86
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 198-475 1.45e-101

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 305.50  E-value: 1.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 271
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 272 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 351
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 352 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 431
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327850588 432 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 198-475 6.65e-52

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 177.55  E-value: 6.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE------KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 271
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEavaeviAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 272 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 351
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 352 GEV--GNAAKM--MLIVNMVqgsfMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYI 427
Cdd:PRK11559  163 GDIgaGNVTKLanQVIVALN----IAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLH 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1327850588 428 QKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:PRK11559  239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 199-352 1.40e-48

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 164.18  E-value: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPsGVL 272
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKveelvaAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 273 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 352
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 199-475 8.84e-45

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 158.51  E-value: 8.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 272
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVadellaAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 273 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 352
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 353 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLR 432
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1327850588 433 LAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
199-472 9.38e-35

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 131.52  E-value: 9.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWN------RTAEKEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 272
Cdd:PRK15461    3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDvnpqavDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 273 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 352
Cdd:PRK15461   83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 353 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNqGQLASI--FLDQKCQNILQGNFKPDFYLKYIQKD 430
Cdd:PRK15461  163 GPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMS-GTAAGKghFTTTWPNKVLKGDLSPAFMIDLAHKD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1327850588 431 LRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVY 472
Cdd:PRK15461  242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
199-474 4.48e-29

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 115.89  E-value: 4.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHT--VTVWNRTAE---KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQ 273
Cdd:PRK15059    2 KLGFIGLGIMGTPMAINLARAGHQlhVTTIGPVADellSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 274 GIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGE 353
Cdd:PRK15059   82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 354 VGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRL 433
Cdd:PRK15059  162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLNL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1327850588 434 AIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRA 474
Cdd:PRK15059  242 ALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQA 282
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 355-475 7.20e-23

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 93.36  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 355 GNAAKMmlIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKC-QNILQGNFKPDFYLKYIQKDLRL 433
Cdd:pfam14833   3 GQAVKA--ANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFpQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1327850588 434 AIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 196-475 2.48e-22

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 100.70  E-value: 2.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  196 TDKKIGFLGLGLMGSGIVSNLLKMGHTVT---VWNRTA---EKEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPS 269
Cdd:PLN02858   323 PVKRIGFIGLGAMGFGMASHLLKSNFSVCgydVYKPTLvrfENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDL 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  270 GVLQGIRPGKCYVDMSTVDADTVTELAQVI--VSRGGRFLEAPVSGNQQLSNDGMLVILAAG-DRGLyEDCSSCFQAMGK 346
Cdd:PLN02858   403 GAVSALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGtDEAL-KSAGSVLSALSE 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  347 TSFFLGEVGNAAKMMLIVN-MVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLK 425
Cdd:PLN02858   482 KLYVIKGGCGAGSGVKMVNqLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALD 561

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327850588  426 YIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:PLN02858   562 IFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVY 611
PLN02858 PLN02858
fructose-bisphosphate aldolase
 196-475 1.85e-19

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 91.84  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  196 TDKKIGFLGLGLMGSGIVSNLLKMGHTVTVW-------NRTAEKEGARLGrTPAEVVSTCDITFACVSDPKAAKDLVLGP 268
Cdd:PLN02858     3 SAGVVGFVGLDSLSFELASSLLRSGFKVQAFeistplmEKFCELGGHRCD-SPAEAAKDAAALVVVLSHPDQVDDVFFGD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  269 SGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGR--FLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGK 346
Cdd:PLN02858    82 EGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588  347 TSFFL-GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLK 425
Cdd:PLN02858   162 KLYTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLN 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327850588  426 YIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 475
Cdd:PLN02858   242 VLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVW 291
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
199-246 1.16e-06

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 50.13  E-value: 1.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNR------TAEKEGARLGRTPAEVVS 246
Cdd:PRK09599    2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRnpeaveALAEEGATGADSLEELVA 55
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 196-277 1.97e-06

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 49.29  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 196 TDKKIGFLGLGLMGSGIVSNLLKMGHT---VTVWNRTAEK-------EGARLGRTPAEVVSTCDITFACVsDPKAAKDlv 265
Cdd:COG0345     1 MSMKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERlealaerYGVRVTTDNAEAAAQADVVVLAV-KPQDLAE-- 77

                          90
                  ....*....|..
gi 1327850588 266 lgpsgVLQGIRP 277
Cdd:COG0345    78 -----VLEELAP 84
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
200-274 7.79e-06

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 46.70  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 200 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK---------EGARlGRTPAEVVSTCDITFACVsDPKAAKDLVLGPSG 270
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKaaalaaelgPGAR-AGTNAEAAAAADVVVLAV-PYEAVPDVLESLGD 78


                  ....
gi 1327850588 271 VLQG 274
Cdd:COG2085    79 ALAG 82
PRK07680 PRK07680
late competence protein ComER; Validated
 199-255 1.76e-05

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 46.50  E-value: 1.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 199 KIGFLGLGLMG-----SGIVSNLLKMGHtVTVWNRTAEKE--------GARLGRTPAEVVSTCDITFACV 255
Cdd:PRK07680    2 NIGFIGTGNMGtilieAFLESGAVKPSQ-LTITNRTPAKAyhikerypGIHVAKTIEEVISQSDLIFICV 70
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 200-232 4.57e-05

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 45.83  E-value: 4.57e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1327850588 200 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK 232
Cdd:COG0362     5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEK 37
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 200-232 3.82e-04

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 42.85  E-value: 3.82e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1327850588 200 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK 232
Cdd:PTZ00142    4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEK 36
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 199-257 1.40e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 40.57  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850588 199 KIGFLGLGLMGSGIVSNLLKMGHTVT-VWNRT---AEKEGARLGRTPA----EVVSTCDITFACVSD 257
Cdd:COG5495     5 KIGIIGAGRVGTALAAALRAAGHEVVgVYSRSpasAERAAALLGAVPAldleELAAEADLVLLAVPD 71
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
201-285 2.10e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 37.21  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 201 GFLGLGLMGSGIVSNLLKMG-HTVTVWNR--------TAEKEGARL-GRTPAEVVSTCDITFACVSdPKAAKDLVlgpsG 270
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSrnpekaeeLAEEYGVGAtAVDNEEAAEEADVVFLAVK-PEDAPDVL----S 75

                          90
                  ....*....|....*
gi 1327850588 271 VLQGIRPGKCYVDMS 285
Cdd:pfam03807  76 ELSDLLKGKIVISIA 90
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 200-266 2.15e-03

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 38.37  E-value: 2.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850588 200 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE-----KEGARLGRTPAEVVSTCDITFACVSDPKAAkDLVL 266
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAElaaikKNGLRLTSPGGERIVPPPAVTSASESLGPI-DLVI 71
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 140-263 3.60e-03

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 39.56  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 140 VKDAdphfhhFLLSQTEKPA------VCYQAIT--KKLKiceEET----GSTSI-QAADSTAVNGSITPTDKKIGFLGLG 206
Cdd:cd05213   117 VKNA------YKLAKEAGTSgkllnrLFQKAIKvgKRVR---TETgisrGAVSIsSAAVELAEKIFGNLKGKKVLVIGAG 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850588 207 LMGSGIVSNLLKMGHT-VTVWNRTAEKEGARLGRTPAEVVS---------TCDITFACVSDPKAAKD 263
Cdd:cd05213   188 EMGELAAKHLAAKGVAeITIANRTYERAEELAKELGGNAVPldellellnEADVVISATGAPHYAKI 254
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 1-21 4.42e-03

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 36.43  E-value: 4.42e-03
                          10        20
                  ....*....|....*....|.
gi 1327850588   1 MIKINKGKRFQQAVDAVEEFL 21
Cdd:cd05836    66 MLKSKKSAGFKDAVEAIEEYI 86
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 197-255 8.43e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.20  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850588 197 DKKIGFLGLGLMGSGIVSNLLKMG---HTVTVWNRTAEKE-------GARLGRTPAEVVSTCDITFACV 255
Cdd:PRK11880    2 MKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRaalaeeyGVRAATDNQEAAQEADVVVLAV 70
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 194-230 9.41e-03

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 37.86  E-value: 9.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1327850588 194 TPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTA 230
Cdd:cd12164   129 PAAERRVGVLGLGELGAAVARRLAALGFPVSGWSRSP 165
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 198-306 9.80e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 37.80  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850588 198 KKIGFLGLGLMGSGIVSNLLKMG--HTVTVWNR------TAEKEGA--RLGRTPAEVVSTCDITFACVSdPKAAKDLVlg 267
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRspetleRALELGVidRAATDLEEAVADADLVVLAVP-VGATIEVL-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1327850588 268 pSGVLQGIRPGKCYVDMSTVDADTVTELAQVIvSRGGRF 306
Cdd:COG0287    79 -AELAPHLKPGAIVTDVGSVKGAVVEAAEALL-PDGVRF 115
 
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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