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Conserved domains on  [gi|1993152036|ref|WP_204805539|]
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NAD(P)H-hydrate dehydratase [Oscillibacter valericigenes]

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 ...
 227-512 6.65e-104

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: 312.44  E-value: 6.65e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 227 RAQTVERDFVRTALPPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFP 306
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 307 LPDKhgklspkakEEILKRAAGCDAVALGPGLGRGDGVTELVLELLREIRQPVVLDADGINALAGHMDVLDARQDRvTVL 386
Cdd:COG0063    81 LPEE---------DELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAP-TVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 387 TPHDGEFARIGGDLSA---GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLL 463
Cdd:COG0063   151 TPHPGEFARLLGCSVAeiqADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1993152036 464 AQGASPVQAAAGGVWLHGRAGDLAAERLTaYGMTPEDVVSALPAAIGEV 512
Cdd:COG0063   231 AQGLDPFEAAAAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALREL 278
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-196 4.41e-47

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: 161.24  E-value: 4.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  24 SIDLMERAAEGVARAALDLLPqrPGRCRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFLVGDYEKLTPDALEETRRLSE 103
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLS--PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 104 CGVELERFDPaDASQRAWVLGCDVVIDAVFGVGLSRPIAAgsPFAAAVDWMNESRAAVVAADIASGVAADTGDVLGRAVR 183
Cdd:pfam03853  79 LGGKIVTDNP-DEDLEKLLSPVDLIIDALLGTGLSGPLRG--EYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVR 155

                         170
                  ....*....|...
gi 1993152036 184 ADRTVTFTLPKIG 196
Cdd:pfam03853 156 ADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 227-512 6.65e-104

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: 312.44  E-value: 6.65e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 227 RAQTVERDFVRTALPPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFP 306
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 307 LPDKhgklspkakEEILKRAAGCDAVALGPGLGRGDGVTELVLELLREIRQPVVLDADGINALAGHMDVLDARQDRvTVL 386
Cdd:COG0063    81 LPEE---------DELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAP-TVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 387 TPHDGEFARIGGDLSA---GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLL 463
Cdd:COG0063   151 TPHPGEFARLLGCSVAeiqADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1993152036 464 AQGASPVQAAAGGVWLHGRAGDLAAERLTaYGMTPEDVVSALPAAIGEV 512
Cdd:COG0063   231 AQGLDPFEAAAAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 246-506 7.48e-80

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: 249.84  E-value: 7.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 246 DGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFPLPDKhgklspkAKEEILKR 325
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLET-------DIEELLEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 326 AAGCDAVALGPGLGRGDGVTELVLELLREiRQPVVLDADGINALAGHMDVLDARQDrvTVLTPHDGEFARIGGDL---SA 402
Cdd:cd01171    75 LERADAVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLIKRYGP--VVLTPHPGEFARLLGALveeIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 403 GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGVWLHGR 482
Cdd:cd01171   152 ADRLAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGL 231

                         250       260
                  ....*....|....*....|....
gi 1993152036 483 AGDLAAERLtAYGMTPEDVVSALP 506
Cdd:cd01171   232 AGDLAAKKK-GAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 6-506 1.63e-76

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 249.59  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   6 ASQMKELDRQAIEERGIPSIDLMERAAEgvarAALDLLPQR-PGRCRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFLV 84
Cdd:PRK10565   20 ADDIRRGEREAADALGLTLYELMLRAGE----AAFQVARSAyPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  85 GDYEKLTPDALEETRRLSECGVELErfdpadASQRAWVLGCDVVIDAVFGVGLSRpiAAGSPFAAAVDWMNESRAAVVAA 164
Cdd:PRK10565   96 ESDKPLPEEAALAREAWLNAGGEIH------AADIVWPESVDLIVDALLGTGLRQ--APREPYAALIDQANAHPAPVVAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 165 DIASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEGAVLSGDVEVRDIGipadLVRGLACRAQTVER---DFVRTALP 241
Cdd:PRK10565  168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLG----LDSWLAGQEAPIQRfdaEQLSQWLK 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 242 PRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLV-FLGVPEAIWPVEAAKcvsamPFPLPDKhgkLSPKAKE 320
Cdd:PRK10565  244 PRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLLTAR-----PELMVHE---LTPDSLE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 321 EILKRAagcDAVALGPGLGRGDGVTElVLELLREIRQPVVLDADGINALAGHMDVldaRQDRVtvLTPHDGEFARIGGDL 400
Cdd:PRK10565  316 ESLEWA---DVVVIGPGLGQQEWGKK-ALQKVENFRKPMLWDADALNLLAINPDK---RHNRV--ITPHPGEAARLLGCS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 401 SA---GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGV 477
Cdd:PRK10565  387 VAeieSDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGC 466

                         490       500
                  ....*....|....*....|....*....
gi 1993152036 478 WLHGRAGDLAAERLTAYGMTPEDVVSALP 506
Cdd:PRK10565  467 VAHGAAADVLAARFGTRGMLATDLFSTLQ 495
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 236-509 4.88e-68

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: 219.56  E-value: 4.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 236 VRTALPPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFPLpdkhgKLS 315
Cdd:TIGR00196   8 DLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRL-----MWK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 316 PKAKEEILKRAagcDAVALGPGLGRGDGVTELVLELLrEIRQPVVLDADGINalagHMDVLDARQDRVtVLTPHDGEFAR 395
Cdd:TIGR00196  83 VDEDEELLERY---DVVVIGPGLGQDPSFKKAVEEVL-ELDKPVVLDADALN----LLTYNQKREGEV-ILTPHPGEFKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 396 I-GGDLSAGDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAA 474
Cdd:TIGR00196 154 LlGVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAAC 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993152036 475 GGVWLHGRAGDLAAERLTAYGMTPEDVVSALPAAI 509
Cdd:TIGR00196 234 NAAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVC 268
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 255-506 1.62e-54

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: 183.33  E-value: 1.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 255 VLIVGGAVGYTGAPWLTAAAAARSGCGLV-FLGVPEAIWPVEAAkCVSAMPFPLPDKHGKLspkakeEILKRAagcDAVA 333
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVsVATDSEAIAVLKSP-LPEVMVHPLPETSSIL------EKLSRY---DAVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 334 LGPGLGRGDGVTELVLELLREIRqPVVLDADGINALAGHMDVldARQDRVTVLTPHDGEFARIGGDL--SAGDRLGAARA 411
Cdd:pfam01256  71 IGPGLGRDEKGKAALEEVLAKDC-PLVIDADALNLLAINNEK--PAREGPTVLTPHPGEFERLCGLAgiLGDDRLEAARE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 412 FTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGVWLHGRAGDLAAERl 491
Cdd:pfam01256 148 LAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN- 226

                         250
                  ....*....|....*
gi 1993152036 492 TAYGMTPEDVVSALP 506
Cdd:pfam01256 227 HGVYMLPTLLSKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-196 4.41e-47

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: 161.24  E-value: 4.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  24 SIDLMERAAEGVARAALDLLPqrPGRCRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFLVGDYEKLTPDALEETRRLSE 103
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLS--PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 104 CGVELERFDPaDASQRAWVLGCDVVIDAVFGVGLSRPIAAgsPFAAAVDWMNESRAAVVAADIASGVAADTGDVLGRAVR 183
Cdd:pfam03853  79 LGGKIVTDNP-DEDLEKLLSPVDLIIDALLGTGLSGPLRG--EYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVR 155

                         170
                  ....*....|...
gi 1993152036 184 ADRTVTFTLPKIG 196
Cdd:pfam03853 156 ADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 11-217 2.41e-40

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: 144.48  E-value: 2.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  11 ELDRQAIEERGIPSIDLMERAAEGVARAALDLLPQRPgrcRGAALCGAGNNGGDGIAAARLLflKGLKIRAFLVGDYEKL 90
Cdd:TIGR00197  10 AIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG---HVIIFCGPGNNGGDGFVVARHL--KGFGVEVFLLKKEKRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  91 TPdaLEETRrlsecgVELERFDPADASQRA----WVLGCDVVIDAVFGVGLSRPIAagSPFAAAVDWMNESRAAVVAADI 166
Cdd:TIGR00197  85 EC--TEQAE------VNLKALKVGGISIDEgnlvKPEDCDVIIDAILGTGFKGKLR--EPFKTIVESINELPAPIVSVDI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1993152036 167 ASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEGAVLsGDVEVRDIGIP 217
Cdd:TIGR00197 155 PSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADVT-GELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 6-202 2.87e-21

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 93.02  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   6 ASQMKELDRQAIEERGIPSIDLMERAAEGVARA----ALDLLPQRPGRC--RGAALCGAGNNGGDGIAAARLLFLKGLKI 79
Cdd:PLN03050   11 AQDAAALDEELMSTPGFSLEQLMELAGLSVAEAvyevADGEKASNPPGRhpRVLLVCGPGNNGGDGLVAARHLAHFGYEV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  80 RAFlvgdYEKLTPDALEE--TRRLSECGVELERFDPAD-ASQRAWVLGCDVVIDAVFgvGLSRPIAAGSPFAAAVDWMNE 156
Cdd:PLN03050   91 TVC----YPKQSSKPHYEnlVTQCEDLGIPFVQAIGGTnDSSKPLETTYDVIVDAIF--GFSFHGAPRAPFDTLLAQMVQ 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1993152036 157 SRAA---VVAADIASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEG 202
Cdd:PLN03050  165 QQKSpppIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEG 213
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 227-512 6.65e-104

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: 312.44  E-value: 6.65e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 227 RAQTVERDFVRTALPPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFP 306
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 307 LPDKhgklspkakEEILKRAAGCDAVALGPGLGRGDGVTELVLELLREIRQPVVLDADGINALAGHMDVLDARQDRvTVL 386
Cdd:COG0063    81 LPEE---------DELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAP-TVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 387 TPHDGEFARIGGDLSA---GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLL 463
Cdd:COG0063   151 TPHPGEFARLLGCSVAeiqADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1993152036 464 AQGASPVQAAAGGVWLHGRAGDLAAERLTaYGMTPEDVVSALPAAIGEV 512
Cdd:COG0063   231 AQGLDPFEAAAAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALREL 278
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-509 7.85e-88

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: 278.68  E-value: 7.85e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   1 MKLATASQMKELDRQAIEERGIPSIDLMERAAEGVARAALDLLPQRPGRCrgAALCGAGNNGGDGIAAARLLFLKGLKIR 80
Cdd:COG0062     1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSAARRV--LVLCGPGNNGGDGLVAARLLAEAGYNVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  81 AFLVGDYEKLTPDALEETRRLSECGVELERFDPADAsqraWVLGCDVVIDAVFGVGLSRPIAAgsPFAAAVDWMNESRAA 160
Cdd:COG0062    79 VFLLGDPEKLSGDAAANLERLKAAGIPILELDDELP----ELAEADLIVDALFGTGLSRPLRG--PYAELIEAINASGAP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 161 VVAADIASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEGAVLSGDVEVRDIGIPADLVRgLACRAQTVERDFVRTAL 240
Cdd:COG0062   153 VLAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAA-EAPAALLLLADLLALLL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 241 PPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFPLPDkhgklspKAKE 320
Cdd:COG0062   232 PPRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDD-------DEEL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 321 EILKRAAGCDAVALGPGLGRGDGVTELVLELLREIRQPVVLDADGINALAGHMDVLDARQDRVTVLTPHDGEFARIGGDL 400
Cdd:COG0062   305 LLLLAAAVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELR 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 401 SAGDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGVWLH 480
Cdd:COG0062   385 AAAAALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAA 464

                         490       500
                  ....*....|....*....|....*....
gi 1993152036 481 GRAGDLAAERLTAYGMTPEDVVSALPAAI 509
Cdd:COG0062   465 AAAAAAAAALAAALLAAAAALIALLLAAA 493
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 246-506 7.48e-80

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: 249.84  E-value: 7.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 246 DGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFPLPDKhgklspkAKEEILKR 325
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLET-------DIEELLEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 326 AAGCDAVALGPGLGRGDGVTELVLELLREiRQPVVLDADGINALAGHMDVLDARQDrvTVLTPHDGEFARIGGDL---SA 402
Cdd:cd01171    75 LERADAVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLIKRYGP--VVLTPHPGEFARLLGALveeIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 403 GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGVWLHGR 482
Cdd:cd01171   152 ADRLAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGL 231

                         250       260
                  ....*....|....*....|....
gi 1993152036 483 AGDLAAERLtAYGMTPEDVVSALP 506
Cdd:cd01171   232 AGDLAAKKK-GAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 6-506 1.63e-76

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 249.59  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   6 ASQMKELDRQAIEERGIPSIDLMERAAEgvarAALDLLPQR-PGRCRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFLV 84
Cdd:PRK10565   20 ADDIRRGEREAADALGLTLYELMLRAGE----AAFQVARSAyPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  85 GDYEKLTPDALEETRRLSECGVELErfdpadASQRAWVLGCDVVIDAVFGVGLSRpiAAGSPFAAAVDWMNESRAAVVAA 164
Cdd:PRK10565   96 ESDKPLPEEAALAREAWLNAGGEIH------AADIVWPESVDLIVDALLGTGLRQ--APREPYAALIDQANAHPAPVVAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 165 DIASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEGAVLSGDVEVRDIGipadLVRGLACRAQTVER---DFVRTALP 241
Cdd:PRK10565  168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLG----LDSWLAGQEAPIQRfdaEQLSQWLK 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 242 PRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLV-FLGVPEAIWPVEAAKcvsamPFPLPDKhgkLSPKAKE 320
Cdd:PRK10565  244 PRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVrVLTRSENIAPLLTAR-----PELMVHE---LTPDSLE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 321 EILKRAagcDAVALGPGLGRGDGVTElVLELLREIRQPVVLDADGINALAGHMDVldaRQDRVtvLTPHDGEFARIGGDL 400
Cdd:PRK10565  316 ESLEWA---DVVVIGPGLGQQEWGKK-ALQKVENFRKPMLWDADALNLLAINPDK---RHNRV--ITPHPGEAARLLGCS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 401 SA---GDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGV 477
Cdd:PRK10565  387 VAeieSDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGC 466

                         490       500
                  ....*....|....*....|....*....
gi 1993152036 478 WLHGRAGDLAAERLTAYGMTPEDVVSALP 506
Cdd:PRK10565  467 VAHGAAADVLAARFGTRGMLATDLFSTLQ 495
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 236-509 4.88e-68

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: 219.56  E-value: 4.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 236 VRTALPPRKIDGHKGTFGKVLIVGGAVGYTGAPWLTAAAAARSGCGLVFLGVPEAIWPVEAAKCVSAMPFPLpdkhgKLS 315
Cdd:TIGR00196   8 DLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRL-----MWK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 316 PKAKEEILKRAagcDAVALGPGLGRGDGVTELVLELLrEIRQPVVLDADGINalagHMDVLDARQDRVtVLTPHDGEFAR 395
Cdd:TIGR00196  83 VDEDEELLERY---DVVVIGPGLGQDPSFKKAVEEVL-ELDKPVVLDADALN----LLTYNQKREGEV-ILTPHPGEFKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 396 I-GGDLSAGDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAA 474
Cdd:TIGR00196 154 LlGVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAAC 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993152036 475 GGVWLHGRAGDLAAERLTAYGMTPEDVVSALPAAI 509
Cdd:TIGR00196 234 NAAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVC 268
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 255-506 1.62e-54

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: 183.33  E-value: 1.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 255 VLIVGGAVGYTGAPWLTAAAAARSGCGLV-FLGVPEAIWPVEAAkCVSAMPFPLPDKHGKLspkakeEILKRAagcDAVA 333
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVsVATDSEAIAVLKSP-LPEVMVHPLPETSSIL------EKLSRY---DAVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 334 LGPGLGRGDGVTELVLELLREIRqPVVLDADGINALAGHMDVldARQDRVTVLTPHDGEFARIGGDL--SAGDRLGAARA 411
Cdd:pfam01256  71 IGPGLGRDEKGKAALEEVLAKDC-PLVIDADALNLLAINNEK--PAREGPTVLTPHPGEFERLCGLAgiLGDDRLEAARE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 412 FTEAHGCVLVLKGHRTITAVPSGNALVNTTGNSGLAKGGSGDVLTGVIASLLAQGASPVQAAAGGVWLHGRAGDLAAERl 491
Cdd:pfam01256 148 LAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN- 226

                         250
                  ....*....|....*
gi 1993152036 492 TAYGMTPEDVVSALP 506
Cdd:pfam01256 227 HGVYMLPTLLSKIIP 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 24-196 4.41e-47

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: 161.24  E-value: 4.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  24 SIDLMERAAEGVARAALDLLPqrPGRCRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFLVGDYEKLTPDALEETRRLSE 103
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLS--PAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 104 CGVELERFDPaDASQRAWVLGCDVVIDAVFGVGLSRPIAAgsPFAAAVDWMNESRAAVVAADIASGVAADTGDVLGRAVR 183
Cdd:pfam03853  79 LGGKIVTDNP-DEDLEKLLSPVDLIIDALLGTGLSGPLRG--EYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVR 155

                         170
                  ....*....|...
gi 1993152036 184 ADRTVTFTLPKIG 196
Cdd:pfam03853 156 ADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 11-217 2.41e-40

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: 144.48  E-value: 2.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  11 ELDRQAIEERGIPSIDLMERAAEGVARAALDLLPQRPgrcRGAALCGAGNNGGDGIAAARLLflKGLKIRAFLVGDYEKL 90
Cdd:TIGR00197  10 AIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG---HVIIFCGPGNNGGDGFVVARHL--KGFGVEVFLLKKEKRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  91 TPdaLEETRrlsecgVELERFDPADASQRA----WVLGCDVVIDAVFGVGLSRPIAagSPFAAAVDWMNESRAAVVAADI 166
Cdd:TIGR00197  85 EC--TEQAE------VNLKALKVGGISIDEgnlvKPEDCDVIIDAILGTGFKGKLR--EPFKTIVESINELPAPIVSVDI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1993152036 167 ASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEGAVLsGDVEVRDIGIP 217
Cdd:TIGR00197 155 PSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADVT-GELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 6-202 2.87e-21

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 93.02  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   6 ASQMKELDRQAIEERGIPSIDLMERAAEGVARA----ALDLLPQRPGRC--RGAALCGAGNNGGDGIAAARLLFLKGLKI 79
Cdd:PLN03050   11 AQDAAALDEELMSTPGFSLEQLMELAGLSVAEAvyevADGEKASNPPGRhpRVLLVCGPGNNGGDGLVAARHLAHFGYEV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  80 RAFlvgdYEKLTPDALEE--TRRLSECGVELERFDPAD-ASQRAWVLGCDVVIDAVFgvGLSRPIAAGSPFAAAVDWMNE 156
Cdd:PLN03050   91 TVC----YPKQSSKPHYEnlVTQCEDLGIPFVQAIGGTnDSSKPLETTYDVIVDAIF--GFSFHGAPRAPFDTLLAQMVQ 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1993152036 157 SRAA---VVAADIASGVAADTGDVLGRAVRADRTVTFTLPKIGQAVGEG 202
Cdd:PLN03050  165 QQKSpppIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEG 213
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 24-203 4.43e-15

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 77.58  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  24 SID-LMERAAEGVARAALDLLPQRPGRcRGAALCGAGNNGGDGIAAARLLFLKGLKIRAFlvgdYEKLTPDALEE--TRR 100
Cdd:PLN03049   34 SVDqLMELAGLSVASAIAEVYSPSEYR-RVLALCGPGNNGGDGLVAARHLHHFGYKPSIC----YPKRTDKPLYNglVTQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 101 LSECGVELERFD--PADASQRAwvlgcDVVIDAVFGV---GLSRPiaagsPFAAAVDWMNESRAA--VVAADIASGVAAD 173
Cdd:PLN03049  109 LESLSVPFLSVEdlPSDLSSQF-----DIVVDAMFGFsfhGAPRP-----PFDDLIQKLVRAAGPppIVSVDIPSGWHVE 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 1993152036 174 TGDVLGRAVRADRTVTFTLPKIGQAVGEGA 203
Cdd:PLN03049  179 EGDVNGEGLKPDMLVSLTAPKLCAKMFKGP 208
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 5-195 1.56e-13

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 73.05  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036   5 TASQMKELDRQAIEERGIPSIDLMERAAEGVARAALDLLpqRPGR-CRGAALCGAGNNGGDGIAAARLLFLKGLKirAFL 83
Cdd:PLN02918   92 TQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVY--KPGEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036  84 VgdYEKLTPDAL-----EETRRLSECGVELERFdPADASQRAwvlgcDVVIDAVFGV---GLSRPiaagsPFAAAVDWM- 154
Cdd:PLN02918  168 C--YPKRTAKPLytglvTQLESLSVPFVSVEDL-PADLSKDF-----DIIVDAMFGFsfhGAPRP-----PFDDLIRRLv 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1993152036 155 -------NESRAAVVAADIASGVAADTGDVLGRAVRADRTVTFTLPKI 195
Cdd:PLN02918  235 slqnyeqTLKHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKL 282
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 356-495 5.31e-08

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: 53.70  E-value: 5.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 356 RQPVVLDADGINALAGHMDVLDA--RQDRVTVLTPHDGEFARIGG-----------DLSAGDRLGAARAFTEAHGCV--- 419
Cdd:cd01170    79 GKPVVLDPVGVGATSFRTEVAKEllAEGQPTVIRGNASEIAALAGltglgkgvdssSSDEEDALELAKALARKYGAVvvv 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 420 -----LVLKGHRTITaVPSGNALvnttgnsgLAK-GGSGDVLTGVIASLLAQGASPVQAAAGGVWLHGRAGDLAAERLTA 493
Cdd:cd01170   159 tgevdYITDGERVVV-VKNGHPL--------LTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGELAAERAKG 229


                  ..
gi 1993152036 494 YG 495
Cdd:cd01170   230 PG 231
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 401-501 4.30e-05

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 45.18  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 401 SAGDRLGAARAFTEAHGCVLVLKGHRTITAVPSGNALVNTtGNSGLAK-GGSGDVLTGVIASLLAQGASPVQAAAGGVWL 479
Cdd:PRK09355  141 GSADAVEIAKAAAKKYGTVVVVTGEVDYITDGERVVSVHN-GHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAV 219

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1993152036 480 HGRAGDLAAERLTA-------------YGMTPEDV 501
Cdd:PRK09355  220 YGIAGELAAERSEKgpgsfqpafldalYQLTEEDI 254
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 327-499 6.27e-03

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 38.71  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 327 AGCDAVALGPGLGRGDGVTELVLELLREIRQ---PVVLD-ADGINALAGHMDVLDARQDRVTVLTPHDGEFARIGGDLSA 402
Cdd:COG0524   126 AGADILHLGGITLASEPPREALLAALEAARAagvPVSLDpNYRPALWEPARELLRELLALVDILFPNEEEAELLTGETDP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152036 403 GDrlgAARAFTE-----------AHGCVLVLKGHRTITAVPSGNAlVNTTGnsglakggSGDVLTGVIASLLAQGASPVQ 471
Cdd:COG0524   206 EE---AAAALLArgvklvvvtlgAEGALLYTGGEVVHVPAFPVEV-VDTTG--------AGDAFAAGFLAGLLEGLDLEE 273

                         170       180
                  ....*....|....*....|....*...
gi 1993152036 472 AAAGGVwlhgRAGDLAAERLTAYGMTPE 499
Cdd:COG0524   274 ALRFAN----AAAALVVTRPGAQPALPT 297
 
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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