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Conserved domains on  [gi|1338983386|gb|AUY39047|]
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bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Leclercia sp. LSNIH3]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 11484799)

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

CATH:  3.40.1190.20|3.40.50.10260
EC:  5.1.99.6|4.2.1.136
Gene Ontology:  GO:0005524|GO:0052855|GO:0052856|GO:0052857|GO:0046496
PubMed:  21994945

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


:

Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 989.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386   1 MTDHTVKKNPASIPHSVWPAEALRRVEQEAADSIGMTLYELMQRAGEAAFAVARRAYPQARHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  81 RLALAAGITVTLLAQESDKPLPEEAAKARETWLEAAGVIHAADTAWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 161 PASIVALDVPSGLNAQTGTTPGDVIHANHTVTFVALKPGLLTGKARDVVGELHHNALGLEGWLAGQETPISRFDASQLAQ 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 241 WLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALDDSLQW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 321 ADVVVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 401 LVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQY 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1338983386 481 GTRGMLATDLFDTLRRVVNPEIIDVEND 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 989.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386   1 MTDHTVKKNPASIPHSVWPAEALRRVEQEAADSIGMTLYELMQRAGEAAFAVARRAYPQARHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  81 RLALAAGITVTLLAQESDKPLPEEAAKARETWLEAAGVIHAADTAWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 161 PASIVALDVPSGLNAQTGTTPGDVIHANHTVTFVALKPGLLTGKARDVVGELHHNALGLEGWLAGQETPISRFDASQLAQ 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 241 WLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALDDSLQW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 321 ADVVVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 401 LVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQY 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1338983386 481 GTRGMLATDLFDTLRRVVNPEIIDVEND 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 232-500 1.62e-115

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: 342.10  E-value: 1.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 232 RFDASQLAQWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHEL-T 310
Cdd:COG0063     4 LLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLpE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 311 AEALDDSLQWADVVVIGPGLGQASWGKEALRKV-ENFRHAMLWDADALNLLAINPD----KRHNRILTPHPGEAARLLNC 385
Cdd:COG0063    84 EDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARLLGC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 386 SVAEIESDRLHSAQRLVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAG 465
Cdd:COG0063   164 SVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAG 243

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1338983386 466 CVVHGAAADRLADQYGtRGMLATDLFDTLRRVVNP 500
Cdd:COG0063   244 VYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 232-500 1.10e-107

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: 321.64  E-value: 1.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 232 RFDASQLAQWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHEL-- 309
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 310 TAEALDDSLQWADVVVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNcsVAE 389
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VNE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 390 IESDRLHSAQRLVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVH 469
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1338983386 470 GAAADRLADQYGTRGMLATDLFDTLRRVVNP 500
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 247-490 3.27e-93

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: 284.12  E-value: 3.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 247 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELT---AEALDDSLQWADV 323
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLetdIEELLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 324 VVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRH---NRILTPHPGEAARLLNCSVAEIESDRLHSAQR 400
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 401 LVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQY 480
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1338983386 481 GTRGMLATDL 490
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 257-496 5.63e-86

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: 265.00  E-value: 5.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 257 LVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALD-DSLQWADVVVIGPGLGQASW 335
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 336 GKEALRKVENFRHAMLWDADALNLLAIN---PDKRHNRILTPHPGEAARLLNCSVAeIESDRLHSAQRLVKRYGGVVVLK 412
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 413 GAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQYGtRGMLATDLFD 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1338983386 493 TLRR 496
Cdd:pfam01256 239 IIPR 242
 
Name Accession Description Interval E-value
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 1-508 0e+00

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 989.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386   1 MTDHTVKKNPASIPHSVWPAEALRRVEQEAADSIGMTLYELMQRAGEAAFAVARRAYPQARHWLILCGHGNNGGDGYVVA 80
Cdd:PRK10565    1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  81 RLALAAGITVTLLAQESDKPLPEEAAKARETWLEAAGVIHAADTAWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHH 160
Cdd:PRK10565   81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 161 PASIVALDVPSGLNAQTGTTPGDVIHANHTVTFVALKPGLLTGKARDVVGELHHNALGLEGWLAGQETPISRFDASQLAQ 240
Cdd:PRK10565  161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 241 WLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALDDSLQW 320
Cdd:PRK10565  241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 321 ADVVVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLHSAQR 400
Cdd:PRK10565  321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 401 LVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQY 480
Cdd:PRK10565  401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480

                         490       500
                  ....*....|....*....|....*...
gi 1338983386 481 GTRGMLATDLFDTLRRVVNPEIIDVEND 508
Cdd:PRK10565  481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 232-500 1.62e-115

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: 342.10  E-value: 1.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 232 RFDASQLAQWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHEL-T 310
Cdd:COG0063     4 LLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLpE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 311 AEALDDSLQWADVVVIGPGLGQASWGKEALRKV-ENFRHAMLWDADALNLLAINPD----KRHNRILTPHPGEAARLLNC 385
Cdd:COG0063    84 EDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARLLGC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 386 SVAEIESDRLHSAQRLVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAG 465
Cdd:COG0063   164 SVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAG 243

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1338983386 466 CVVHGAAADRLADQYGtRGMLATDLFDTLRRVVNP 500
Cdd:COG0063   244 VYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 232-500 1.10e-107

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: 321.64  E-value: 1.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 232 RFDASQLAQWLPPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHEL-- 309
Cdd:TIGR00196   2 TFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 310 TAEALDDSLQWADVVVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNcsVAE 389
Cdd:TIGR00196  82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VNE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 390 IESDRLHSAQRLVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVH 469
Cdd:TIGR00196 160 IQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAH 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1338983386 470 GAAADRLADQYGTRGMLATDLFDTLRRVVNP 500
Cdd:TIGR00196 240 GLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 17-508 1.94e-106

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: 326.83  E-value: 1.94e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  17 VWPAEALRRVEQEAADSIGMTLYELMQRAGEAAFAVARRAYP-QARHWLILCGHGNNGGDGYVVARLALAAGITVTLLAQ 95
Cdd:COG0062     3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  96 ESDKPLPEEAAKARETWLEAAGVIHAADT--AWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHHPASIVALDVPSGL 173
Cdd:COG0062    83 GDPEKLSGDAAANLERLKAAGIPILELDDelPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 174 NAQTGTTPGDVIHANHTVTFVALKPGLLTGKARDVVGELHHNALGLEGWLAGQETPISRFDASQLAQWLPPRRPTSHKGD 253
Cdd:COG0062   163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 254 HGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALDDSLqWADVVVIGPGLGQA 333
Cdd:COG0062   243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLL-LAAAVVVAGGGGGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 334 SWGKEALRKVENFRHAMLWDADALNLLAINPDKRHNRILTPHPGEAARLLNCSVAEIESDRLHSAQRLVKRYGGVVVLKG 413
Cdd:COG0062   322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVA 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 414 AGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQYGTRGMLATDLFDT 493
Cdd:COG0062   402 AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAA 481

                         490
                  ....*....|....*
gi 1338983386 494 LRRVVNPEIIDVEND 508
Cdd:COG0062   482 AAALIALLLAAALLL 496
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 247-490 3.27e-93

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: 284.12  E-value: 3.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 247 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELT---AEALDDSLQWADV 323
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLetdIEELLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 324 VVIGPGLGQASWGKEALRKVENFRHAMLWDADALNLLAINPDKRH---NRILTPHPGEAARLLNCSVAEIESDRLHSAQR 400
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 401 LVKRYGGVVVLKGAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQY 480
Cdd:cd01171   161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240

                         250
                  ....*....|
gi 1338983386 481 GTRGMLATDL 490
Cdd:cd01171   241 GAGLTAADLV 250
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 257-496 5.63e-86

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: 265.00  E-value: 5.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 257 LVIIGGDHGTAGAIRMTGEAALRTGAGLVRVLTRRENIAPIVTARPELMVHELTAEALD-DSLQWADVVVIGPGLGQASW 335
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 336 GKEALRKVENFRHAMLWDADALNLLAIN---PDKRHNRILTPHPGEAARLLNCSVAeIESDRLHSAQRLVKRYGGVVVLK 412
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 413 GAGTVVASESGMSGIIDAGNAGMASGGMGDVLSGIIGALLGQKLALYDAACAGCVVHGAAADRLADQYGtRGMLATDLFD 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238


                  ....
gi 1338983386 493 TLRR 496
Cdd:pfam01256 239 IIPR 242
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 17-219 1.35e-67

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: 216.12  E-value: 1.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  17 VWPAEALRRVEQEAADSIGMTLYELMQRAGEAAFAVARRAYPQARHWLILCGHGNNGGDGYVVARLALAAGITVTLLAQE 96
Cdd:TIGR00197   2 VVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  97 SDKPLPEEAAKARETWLEAAGVIHAADTAWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHHPASIVALDVPSGLNAQ 176
Cdd:TIGR00197  82 KRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1338983386 177 TGTTPGDVIHANHTVTFVALKPGLLTGKArDVVGELHHNALGL 219
Cdd:TIGR00197 162 TGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGI 203
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 39-199 7.10e-46

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: 157.77  E-value: 7.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  39 YELMQRAGEAAFAVARRAY-PQARHWLILCGHGNNGGDGYVVARLALAAGITVTLLAQESDKPLPEEAAKARETWLEAAG 117
Cdd:pfam03853   2 AVLMENAGRAAARVLKALLsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 118 VIH-----AADTAWPEEVDLIVDGLLGTGLRSAPRNEIARLIAHANHHPASIVALDVPSGLNAQTGTTPGDVIHANHTVT 192
Cdd:pfam03853  82 KIVtdnpdEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161


                  ....*..
gi 1338983386 193 FVALKPG 199
Cdd:pfam03853 162 FGAPKPG 168
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 20-210 7.85e-18

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 83.00  E-value: 7.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  20 AEALRRVEQEAADSIGMTLYELMQRAG----EAAFAVARRAYPQA-----RHWLILCGHGNNGGDGYVVARLALAAGITV 90
Cdd:PLN03050   11 AQDAAALDEELMSTPGFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHFGYEV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  91 TLL-AQESDKPLPEEAAKARETwLEAAGVIHAADTAWPEEV-----DLIVDGLLGTGLRSAPRNEIARLIAHANH---HP 161
Cdd:PLN03050   91 TVCyPKQSSKPHYENLVTQCED-LGIPFVQAIGGTNDSSKPlettyDVIVDAIFGFSFHGAPRAPFDTLLAQMVQqqkSP 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1338983386 162 ASIVALDVPSGLNAQTGTTPGDVIHANHTVTFVALKPGLLTGKARDVVG 210
Cdd:PLN03050  170 PPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 34-197 9.32e-15

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 76.43  E-value: 9.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  34 IGMTLYELMQRAGEAAFAVARRAYPQARHW--LILCGHGNNGGDGYVVARLALAAGITVTLL-AQESDKPLPEEAAKARE 110
Cdd:PLN03049   31 LGFSVDQLMELAGLSVASAIAEVYSPSEYRrvLALCGPGNNGGDGLVAARHLHHFGYKPSICyPKRTDKPLYNGLVTQLE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 111 TwLEAAGVIHAA-DTAWPEEVDLIVDGLLGTGLRSAPR----NEIARLIAHANhhPASIVALDVPSGLNAQTGTTPGDVI 185
Cdd:PLN03049  111 S-LSVPFLSVEDlPSDLSSQFDIVVDAMFGFSFHGAPRppfdDLIQKLVRAAG--PPPIVSVDIPSGWHVEEGDVNGEGL 187

                         170
                  ....*....|..
gi 1338983386 186 HANHTVTFVALK 197
Cdd:PLN03049  188 KPDMLVSLTAPK 199
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 34-249 6.12e-10

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 61.49  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386  34 IGMTLYELMQRAGEAAFAVARRAYPQARH--WLILCGHGNNGGDGYVVARLALAAGItvtllaqesdKPL---PEEAAKA 108
Cdd:PLN02918  107 LGFSVDQLMELAGLSVAASIAEVYKPGEYsrVLAICGPGNNGGDGLVAARHLHHFGY----------KPFvcyPKRTAKP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 109 RE----TWLEAAGVIHAADTAWP----EEVDLIVDGLLGTGLRSAPR----NEIARLIAHANH-----HPAsIVALDVPS 171
Cdd:PLN02918  177 LYtglvTQLESLSVPFVSVEDLPadlsKDFDIIVDAMFGFSFHGAPRppfdDLIRRLVSLQNYeqtlkHPV-IVSVDIPS 255

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1338983386 172 GLNAQTGTTPGDVIHANHTVTFVAlkPGLLTGKARDVvgelHHnalglegWLAGQETPISRFDASQLAqwLPPRRPTS 249
Cdd:PLN02918  256 GWHVEEGDHEGGGIKPDMLVSLTA--PKLCAKKFRGP----HH-------FLGGRFVPPSIVEKYKLH--LPPYPGTS 318
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 386-494 1.18e-07

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: 52.93  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 386 SVAEIESDRLHSAQRLVKRYGGVVVLKGAGTVVASESgMSGIIDAGNAGMAS-GGMGDVLSGIIGALLGQKLALYDAACA 464
Cdd:cd01170   133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYITDGE-RVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVS 211

                          90       100       110
                  ....*....|....*....|....*....|
gi 1338983386 465 GCVVHGAAADRLADQYGTRGMLATDLFDTL 494
Cdd:cd01170   212 AVLVYGIAGELAAERAKGPGSFRVALLDEL 241
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 388-503 7.69e-05

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 44.41  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338983386 388 AEIESDRLHSAQRLVKRYGGVVVLKGAGTVVASESGMSgIIDAGNAGMAS-GGMGDVLSGIIGALLGQKLALYDAACAGC 466
Cdd:PRK09355  139 TDGSADAVEIAKAAAKKYGTVVVVTGEVDYITDGERVV-SVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAAC 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1338983386 467 VVHGAAADRLADQYGTR-GMLATDLFDTLRRvVNPEII 503
Cdd:PRK09355  218 AVYGIAGELAAERSEKGpGSFQPAFLDALYQ-LTEEDI 254
 
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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