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Conserved domains on  [gi|1563167965|gb|QAV26187|]
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bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Neobacillus thermocopriae]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 11145907)

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, allowing the repair of both epimers of NAD(P)HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 224-507 2.55e-120

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


:

Pssm-ID: 439833  Cd Length: 280  Bit Score: 354.43  E-value: 2.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 224 RLWSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCs 303
Cdd:COG0063     3 RLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 304 slngcfAGEIDLITL--DVDAIAAGPGMGRTMGAKSVIQKVLCQ-DVPVVLDADALYFWNDYVSIIRDRTEATILTPHPG 380
Cdd:COG0063    82 ------PEEDELLELleRADAVVIGPGLGRDEETRELLRALLEAaDKPLVLDADALNLLAEDPELLAALPAPTVLTPHPG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 381 EMARMLGVSIDDVERDRFGIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDN 460
Cdd:COG0063   156 EFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLD 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 461 IQEAICNAVFVHGKAADALVEKEHSPMdvLATDVIEAIPQTLFSLYK 507
Cdd:COG0063   236 PFEAAAAGVYLHGLAGDLAAEERGRGL--LASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.42e-50

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


:

Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 169.72  E-value: 2.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  24 EESLMENAGQAVAAVLLERIQPA-QRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLWLIPPKEKVKGAAKKALEIYENSG 102
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSPAgPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 103 YEVkNYIGNEKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyAIDVPSGIPADGGAV-ETAIQADV 181
Cdd:pfam03853  81 GKI-VTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVL-AVDIPSGLDADTGAVlGTAVRADH 158


                  ....*....
gi 1563167965 182 TITIQYPKL 190
Cdd:pfam03853 159 TVTFGAPKP 167
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 224-507 2.55e-120

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 354.43  E-value: 2.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 224 RLWSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCs 303
Cdd:COG0063     3 RLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 304 slngcfAGEIDLITL--DVDAIAAGPGMGRTMGAKSVIQKVLCQ-DVPVVLDADALYFWNDYVSIIRDRTEATILTPHPG 380
Cdd:COG0063    82 ------PEEDELLELleRADAVVIGPGLGRDEETRELLRALLEAaDKPLVLDADALNLLAEDPELLAALPAPTVLTPHPG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 381 EMARMLGVSIDDVERDRFGIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDN 460
Cdd:COG0063   156 EFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLD 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 461 IQEAICNAVFVHGKAADALVEKEHSPMdvLATDVIEAIPQTLFSLYK 507
Cdd:COG0063   236 PFEAAAAGVYLHGLAGDLAAEERGRGL--LASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-499 5.04e-96

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 291.44  E-value: 5.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 240 RSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCSSLNgcfAGEIDLITLD 319
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETD---IEELLELLER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 320 VDAIAAGPGMGRTMGAKSVIQKVLCQDVPVVLDADALYFWNDYVSIIRdRTEATILTPHPGEMARMLGVSIDDVERDRFG 399
Cdd:cd01171    78 ADAVVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIK-RYGPVVLTPHPGEFARLLGALVEEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 400 IAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADAL 479
Cdd:cd01171   157 AAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLA 236

                         250       260
                  ....*....|....*....|
gi 1563167965 480 VEKEHSPMdvLATDVIEAIP 499
Cdd:cd01171   237 AKKKGAGL--TAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 20-500 8.58e-92

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 289.27  E-value: 8.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  20 IGMSEESLMENAGQAVAAVLLERIQPAQRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLWLIPPKEKVKGAAKKALEIYE 99
Cdd:PRK10565   34 LGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAWL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 100 NSGYEVknyignEKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyAIDVPSGIPADGGAVETA-IQ 178
Cdd:PRK10565  114 NAGGEI------HAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV-ALDIPSGLLAETGATPGAvIN 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 179 ADVTITIQYPKLSAYTFPTADYYGELIVVDIGIPPLSLEKNAEFRRLwSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRN 258
Cdd:PRK10565  187 ADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRF-DAEQLSQWLKPRRPTSHKGDHGRLLIIGGDHG 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 259 MTGAVIMTAKAALRSGAGL---LTMavPDDVYPVAATHiPEVMYHpcsslngcfagEIDLITLD-----VDAIAAGPGMG 330
Cdd:PRK10565  266 TAGAIRMAGEAALRSGAGLvrvLTR--SENIAPLLTAR-PELMVH-----------ELTPDSLEeslewADVVVIGPGLG 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 331 RTMGAKSVIQKVLCQDVPVVLDADALyfwnDYVSIIRDRTEATILTPHPGEMARMLGVSIDDVERDRFGIAKQIAMNYGV 410
Cdd:PRK10565  332 QQEWGKKALQKVENFRKPMLWDADAL----NLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 411 YLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADALVEKEHSpMDVL 490
Cdd:PRK10565  408 VVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGT-RGML 486

                         490
                  ....*....|
gi 1563167965 491 ATDVIEAIPQ 500
Cdd:PRK10565  487 ATDLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 224-500 1.18e-74

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 236.90  E-value: 1.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 224 RLWSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHpcs 303
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVH--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 304 slngCFAGEIDLITLDV---DAIAAGPGMGRTMGAKSVIQKVLCQDVPVVLDADALYfwndYVSIIRDRTEATILTPHPG 380
Cdd:TIGR00196  78 ----RLMWKVDEDEELLeryDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALN----LLTYNQKREGEVILTPHPG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 381 EMARMLGVSIDdvERDRFGIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDN 460
Cdd:TIGR00196 150 EFKRLLGVNEI--QGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLD 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1563167965 461 IQEAICNAVFVHGKAADaLVEKEHSPMDVLATDVIEAIPQ 500
Cdd:TIGR00196 228 PFDAACNAAFAHGLAGD-LALKNHGAYGLTALDLIEKIPR 266
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 251-499 2.49e-63

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 206.45  E-value: 2.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 251 LVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCSSLNgcfagEIDLITLDVDAIAAGPGMG 330
Cdd:pfam01256   2 LVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETS-----SILEKLSRYDAVVIGPGLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 331 RTMGAKSVIQKVLCQDVPVVLDADALYFWnDYVSIIRDRTEATILTPHPGEMARMLGvSIDDVERDRFGIAKQIAMNYGV 410
Cdd:pfam01256  77 RDEKGKAALEEVLAKDCPLVIDADALNLL-AINNEKPAREGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 411 YLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADALVEKeHSPmDVL 490
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN-HGV-YML 232


                  ....*....
gi 1563167965 491 ATDVIEAIP 499
Cdd:pfam01256 233 PTLLSKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.42e-50

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 169.72  E-value: 2.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  24 EESLMENAGQAVAAVLLERIQPA-QRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLWLIPPKEKVKGAAKKALEIYENSG 102
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSPAgPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 103 YEVkNYIGNEKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyAIDVPSGIPADGGAV-ETAIQADV 181
Cdd:pfam03853  81 GKI-VTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVL-AVDIPSGLDADTGAVlGTAVRADH 158


                  ....*....
gi 1563167965 182 TITIQYPKL 190
Cdd:pfam03853 159 TVTFGAPKP 167
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 1-213 1.01e-47

yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]


Pssm-ID: 272956 [Multi-domain]  Cd Length: 205  Bit Score: 164.12  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   1 MHVVTASEMyAIDRYTIQQIGMSEESLMENAGQAVAAVLLERIQPAQRVAVLSGTGNNGGDGFVVARVLKSYGYttDLWL 80
Cdd:TIGR00197   1 KVVVSPKDM-AIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGV--EVFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  81 IPPKEKVKGA--AKKALEIYENSGYEVK--NYIGNEKEfieqlrhyDVIIDALLGIGINGALRSPYKEIIEKVNEAKELV 156
Cdd:TIGR00197  78 LKKEKRIECTeqAEVNLKALKVGGISIDegNLVKPEDC--------DVIIDAILGTGFKGKLREPFKTIVESINELPAPI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1563167965 157 VyAIDVPSGIPADGGAVE-TAIQADVTITIQYPKlSAYTFPTADYYGELIVVDIGIPP 213
Cdd:TIGR00197 150 V-SVDIPSGLDVDTGAIEgPAVNADLTITFHAIK-PCLLSDRADVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 4-195 3.10e-26

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 107.27  E-value: 3.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   4 VTASEMYAIDRYTIQQIGMSEESLMENAGQAVAAVLLE-----------RIQPaqRVAVLSGTGNNGGDGFVVARVLKSY 72
Cdd:PLN03050    9 LNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEvadgekasnppGRHP--RVLLVCGPGNNGGDGLVAARHLAHF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  73 GYttDLWLIPPKEKVKGAAKKALEIYENSGYEVKNYIGNEKEFIEQLRH-YDVIIDALLGIGINGALRSPYKEIIEKVNE 151
Cdd:PLN03050   87 GY--EVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAIGGTNDSSKPLETtYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQ 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 152 AK--ELVVYAIDVPSGIPADGGAVE-TAIQADVTITIQYPKLSAYTF 195
Cdd:PLN03050  165 QQksPPPIVSVDVPSGWDVDEGDVSgTGMRPDVLVSLTAPKLSAKKF 211
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 224-507 2.55e-120

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 354.43  E-value: 2.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 224 RLWSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCs 303
Cdd:COG0063     3 RLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 304 slngcfAGEIDLITL--DVDAIAAGPGMGRTMGAKSVIQKVLCQ-DVPVVLDADALYFWNDYVSIIRDRTEATILTPHPG 380
Cdd:COG0063    82 ------PEEDELLELleRADAVVIGPGLGRDEETRELLRALLEAaDKPLVLDADALNLLAEDPELLAALPAPTVLTPHPG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 381 EMARMLGVSIDDVERDRFGIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDN 460
Cdd:COG0063   156 EFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLD 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 461 IQEAICNAVFVHGKAADALVEKEHSPMdvLATDVIEAIPQTLFSLYK 507
Cdd:COG0063   236 PFEAAAAGVYLHGLAGDLAAEERGRGL--LASDLIEALPAALRELLE 280
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-498 4.68e-110

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];


Pssm-ID: 439832 [Multi-domain]  Cd Length: 499  Bit Score: 336.07  E-value: 4.68e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   1 MHVVTASEMYAIDRYTIQQIGMSEESLMENAGQAVAAVLLERIQ-PAQRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLW 79
Cdd:COG0062     1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  80 LIPPKEKVKGAAKKALEIYENSGYEVKNYigneKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyA 159
Cdd:COG0062    81 LLGDPEKLSGDAAANLERLKAAGIPILEL----DDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVL-A 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 160 IDVPSGIPADGGAV-ETAIQADVTITIQYPKLSAYTFPTADYYGELIVVDIGIPPLsLEKNAEFRRLWSEAAVARTLPVR 238
Cdd:COG0062   156 VDIPSGLDADTGEVlGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIP-AAAEAPAALLLLADLLALLLPPR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 239 KRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCsslnGCFAGEIDLITL 318
Cdd:COG0062   235 RRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALAL----DDDEELLLLLAA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 319 DVDAIAAGPGMGRTMGAKSVIQKVLCQDVPVVLDADALYFWNDYVSIIRDRTEATILTPHPGEMARMLGVSIDDVERDRF 398
Cdd:COG0062   311 AVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAAL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 399 GIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADA 478
Cdd:COG0062   391 LAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAA 470

                         490       500
                  ....*....|....*....|
gi 1563167965 479 LVEKEHSPMDVLATDVIEAI 498
Cdd:COG0062   471 AAALAAALLAAAAALIALLL 490
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 240-499 5.04e-96

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 291.44  E-value: 5.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 240 RSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCSSLNgcfAGEIDLITLD 319
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETD---IEELLELLER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 320 VDAIAAGPGMGRTMGAKSVIQKVLCQDVPVVLDADALYFWNDYVSIIRdRTEATILTPHPGEMARMLGVSIDDVERDRFG 399
Cdd:cd01171    78 ADAVVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIK-RYGPVVLTPHPGEFARLLGALVEEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 400 IAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADAL 479
Cdd:cd01171   157 AAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLA 236

                         250       260
                  ....*....|....*....|
gi 1563167965 480 VEKEHSPMdvLATDVIEAIP 499
Cdd:cd01171   237 AKKKGAGL--TAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 20-500 8.58e-92

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 289.27  E-value: 8.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  20 IGMSEESLMENAGQAVAAVLLERIQPAQRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLWLIPPKEKVKGAAKKALEIYE 99
Cdd:PRK10565   34 LGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAWL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 100 NSGYEVknyignEKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyAIDVPSGIPADGGAVETA-IQ 178
Cdd:PRK10565  114 NAGGEI------HAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVV-ALDIPSGLLAETGATPGAvIN 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 179 ADVTITIQYPKLSAYTFPTADYYGELIVVDIGIPPLSLEKNAEFRRLwSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRN 258
Cdd:PRK10565  187 ADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRF-DAEQLSQWLKPRRPTSHKGDHGRLLIIGGDHG 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 259 MTGAVIMTAKAALRSGAGL---LTMavPDDVYPVAATHiPEVMYHpcsslngcfagEIDLITLD-----VDAIAAGPGMG 330
Cdd:PRK10565  266 TAGAIRMAGEAALRSGAGLvrvLTR--SENIAPLLTAR-PELMVH-----------ELTPDSLEeslewADVVVIGPGLG 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 331 RTMGAKSVIQKVLCQDVPVVLDADALyfwnDYVSIIRDRTEATILTPHPGEMARMLGVSIDDVERDRFGIAKQIAMNYGV 410
Cdd:PRK10565  332 QQEWGKKALQKVENFRKPMLWDADAL----NLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 411 YLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADALVEKEHSpMDVL 490
Cdd:PRK10565  408 VVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGT-RGML 486

                         490
                  ....*....|
gi 1563167965 491 ATDVIEAIPQ 500
Cdd:PRK10565  487 ATDLFSTLQR 496
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 224-500 1.18e-74

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 236.90  E-value: 1.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 224 RLWSEAAVARTLPVRKRSSHKGTYGKGLVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHpcs 303
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVH--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 304 slngCFAGEIDLITLDV---DAIAAGPGMGRTMGAKSVIQKVLCQDVPVVLDADALYfwndYVSIIRDRTEATILTPHPG 380
Cdd:TIGR00196  78 ----RLMWKVDEDEELLeryDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALN----LLTYNQKREGEVILTPHPG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 381 EMARMLGVSIDdvERDRFGIAKQIAMNYGVYLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDN 460
Cdd:TIGR00196 150 EFKRLLGVNEI--QGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLD 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1563167965 461 IQEAICNAVFVHGKAADaLVEKEHSPMDVLATDVIEAIPQ 500
Cdd:TIGR00196 228 PFDAACNAAFAHGLAGD-LALKNHGAYGLTALDLIEKIPR 266
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 251-499 2.49e-63

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 206.45  E-value: 2.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 251 LVIGGSRNMTGAVIMTAKAALRSGAGLLTMAVPDDVYPVAATHIPEVMYHPCSSLNgcfagEIDLITLDVDAIAAGPGMG 330
Cdd:pfam01256   2 LVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETS-----SILEKLSRYDAVVIGPGLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 331 RTMGAKSVIQKVLCQDVPVVLDADALYFWnDYVSIIRDRTEATILTPHPGEMARMLGvSIDDVERDRFGIAKQIAMNYGV 410
Cdd:pfam01256  77 RDEKGKAALEEVLAKDCPLVIDADALNLL-AINNEKPAREGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 411 YLVLKGPYTIVTTPDGKQYVNTSGNPALAKGGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADALVEKeHSPmDVL 490
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN-HGV-YML 232


                  ....*....
gi 1563167965 491 ATDVIEAIP 499
Cdd:pfam01256 233 PTLLSKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-190 2.42e-50

YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.


Pssm-ID: 427546 [Multi-domain]  Cd Length: 168  Bit Score: 169.72  E-value: 2.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  24 EESLMENAGQAVAAVLLERIQPA-QRVAVLSGTGNNGGDGFVVARVLKSYGYTTDLWLIPPKEKVKGAAKKALEIYENSG 102
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSPAgPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 103 YEVkNYIGNEKEFIEQLRHYDVIIDALLGIGINGALRSPYKEIIEKVNEAKELVVyAIDVPSGIPADGGAV-ETAIQADV 181
Cdd:pfam03853  81 GKI-VTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVL-AVDIPSGLDADTGAVlGTAVRADH 158


                  ....*....
gi 1563167965 182 TITIQYPKL 190
Cdd:pfam03853 159 TVTFGAPKP 167
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 1-213 1.01e-47

yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]


Pssm-ID: 272956 [Multi-domain]  Cd Length: 205  Bit Score: 164.12  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   1 MHVVTASEMyAIDRYTIQQIGMSEESLMENAGQAVAAVLLERIQPAQRVAVLSGTGNNGGDGFVVARVLKSYGYttDLWL 80
Cdd:TIGR00197   1 KVVVSPKDM-AIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGV--EVFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  81 IPPKEKVKGA--AKKALEIYENSGYEVK--NYIGNEKEfieqlrhyDVIIDALLGIGINGALRSPYKEIIEKVNEAKELV 156
Cdd:TIGR00197  78 LKKEKRIECTeqAEVNLKALKVGGISIDegNLVKPEDC--------DVIIDAILGTGFKGKLREPFKTIVESINELPAPI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1563167965 157 VyAIDVPSGIPADGGAVE-TAIQADVTITIQYPKlSAYTFPTADYYGELIVVDIGIPP 213
Cdd:TIGR00197 150 V-SVDIPSGLDVDTGAIEgPAVNADLTITFHAIK-PCLLSDRADVTGELKVGGIGIPP 205
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 4-195 3.10e-26

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 107.27  E-value: 3.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   4 VTASEMYAIDRYTIQQIGMSEESLMENAGQAVAAVLLE-----------RIQPaqRVAVLSGTGNNGGDGFVVARVLKSY 72
Cdd:PLN03050    9 LNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEvadgekasnppGRHP--RVLLVCGPGNNGGDGLVAARHLAHF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  73 GYttDLWLIPPKEKVKGAAKKALEIYENSGYEVKNYIGNEKEFIEQLRH-YDVIIDALLGIGINGALRSPYKEIIEKVNE 151
Cdd:PLN03050   87 GY--EVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAIGGTNDSSKPLETtYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQ 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 152 AK--ELVVYAIDVPSGIPADGGAVE-TAIQADVTITIQYPKLSAYTF 195
Cdd:PLN03050  165 QQksPPPIVSVDVPSGWDVDEGDVSgTGMRPDVLVSLTAPKLSAKKF 211
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 4-236 8.80e-22

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 98.00  E-value: 8.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   4 VTASEMYAIDRYTIQQIGMSEESLMENAGQAVAAVLLERIQPAQ--RVAVLSGTGNNGGDGFVVARVLKSYGYttDLWLI 81
Cdd:PLN03049   15 LSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEyrRVLALCGPGNNGGDGLVAARHLHHFGY--KPSIC 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  82 PPKEKVKGAAKKALEIYENSGYEVKNYIGNEKEFIEQlrhYDVIIDALLGIGINGALRSPYKEIIEK-VNEAKELVVYAI 160
Cdd:PLN03049   93 YPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQ---FDIVVDAMFGFSFHGAPRPPFDDLIQKlVRAAGPPPIVSV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 161 DVPSGIPADGGAVE-TAIQADVTITIQYPKLSAYTF--------------PTAD--------YYGELIVVDIGIPP---- 213
Cdd:PLN03049  170 DIPSGWHVEEGDVNgEGLKPDMLVSLTAPKLCAKMFkgphhflggrfvppAIVEkfklhlppYPGTSMCVRIGKTPsvdi 249

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1563167965 214 LSLEKN----------------AEFRRlWSEAAVARTLP 236
Cdd:PLN03049  250 AALRENyvgpelleeqvnadpiDQFKE-WFDDAVAAGLR 287
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 4-195 2.13e-19

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 91.15  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965   4 VTASEMYAIDRYTIQQIGMSEESLMENAGQAVAAVLLERIQPAQ--RVAVLSGTGNNGGDGFVVARVLKSYGYTTdlWLI 81
Cdd:PLN02918   91 LTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEysRVLAICGPGNNGGDGLVAARHLHHFGYKP--FVC 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965  82 PPKEKVK---GAAKKALEIYENSGYEVKNYIGN-EKEFieqlrhyDVIIDALLGIGINGALRSPYKEIIEKV-------N 150
Cdd:PLN02918  169 YPKRTAKplyTGLVTQLESLSVPFVSVEDLPADlSKDF-------DIIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeQ 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1563167965 151 EAKELVVYAIDVPSGIPADGGAVET-AIQADVTITIQYPKLSAYTF 195
Cdd:PLN02918  242 TLKHPVIVSVDIPSGWHVEEGDHEGgGIKPDMLVSLTAPKLCAKKF 287
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 345-486 2.42e-06

4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 48.69  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 345 QDVPVVLDADAlyfwndyVSIIRDRTEA---TILTPHP-------GEMARMLG--------VSIDDVERDRFGIAKQIAM 406
Cdd:cd01170    78 LGKPVVLDPVG-------VGATSFRTEVakeLLAEGQPtvirgnaSEIAALAGltglgkgvDSSSSDEEDALELAKALAR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 407 NYGVYLVLKGPYTIVTtpDGKQ-YVNTSGNPALAK-GGSGDVLTGIILAFIMQHDNIQEAICNAVFVHGKAADALVEKEH 484
Cdd:cd01170   151 KYGAVVVVTGEVDYIT--DGERvVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGELAAERAK 228


                  ..
gi 1563167965 485 SP 486
Cdd:cd01170   229 GP 230
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 348-473 4.30e-06

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 48.35  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 348 PVVLDADALYFWN-DYVSIIRDRTE--ATILTPHPGEMARMLGVSIDDVErDRFGIAKQIAMNYGVYLVLKGP------- 417
Cdd:cd01173   110 PVMGDNGKLYVVAeEIVPVYRDLLVplADIITPNQFELELLTGKKINDLE-DAKAAARALHAKGPKTVVVTSVeladddr 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1563167965 418 -YTIVTTPDGKQYVNTsgnPALAKG----GSGDVLTGIILAFIMQHDNIQEAICNAV-FVHG 473
Cdd:cd01173   189 iEMLGSTATEAWLVQR---PKIPFPayfnGTGDLFAALLLARLLKGKSLAEALEKALnFVHE 247
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 345-455 3.80e-03

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 39.40  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563167965 345 QDVPVVLD---ADALYFWNDY---------VSIIR-DRTE-ATILtphpGEMARMLGVSIDDVERDRFGIAKQIAMNYGV 410
Cdd:PRK09355   83 AGKPVVLDpvgVGATSYRTEFalellaevkPAVIRgNASEiAALA----GEAAETKGVDSTDGSADAVEIAKAAAKKYGT 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1563167965 411 YLVLKGPYTIVTtpDGKQ-YVNTSGNPALAK-GGSGDVLTGIILAFI 455
Cdd:PRK09355  159 VVVVTGEVDYIT--DGERvVSVHNGHPLMTKvTGTGCLLSAVVAAFA 203
 
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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