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Conserved domains on  [gi|2452224051|gb|WEF34490|]
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NAD(P)H-hydrate dehydratase [Pseudoduganella chitinolytica]

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 ...
 217-493 7.24e-92

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: 281.24  E-value: 7.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 217 TIHLNDTAGFAHAAVARPQNSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQ-CDAGQPELMCRT 295
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPaVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 296 AHGVDFATG------VTVAGPGLGGSDEAAHLLEQAI-ASPQPLVVDADGLNLVAARSGLaarLRSRKAATILTPHPLEA 368
Cdd:COG0063    81 LPEEDELLElleradAVVIGPGLGRDEETRELLRALLeAADKPLVLDADALNLLAEDPEL---LAALPAPTVLTPHPGEF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 369 ARLLATSIGAIQRDRLDSARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGW 448
Cdd:COG0063   158 ARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2452224051 449 EAALGAVWLHGMAADVLVTEgtGPVGLTAGELIPAIRTALNRLVA 493
Cdd:COG0063   238 EAAAAGVYLHGLAGDLAAEE--RGRGLLASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-188 4.24e-25

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: 101.53  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  44 FATSRARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGG--------TAPERVRALeRARASPARFMAEDGIGAGE 115
Cdd:pfam03853  20 LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEeklsedarRQLDLFKKL-GGKIVTDNPDEDLEKLLSP 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452224051 116 WHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVPSGLDADTGCVvgpDGCAVHATHTLTFIGDKPG 188
Cdd:pfam03853  99 VDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAV---LGTAVRADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 217-493 7.24e-92

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: 281.24  E-value: 7.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 217 TIHLNDTAGFAHAAVARPQNSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQ-CDAGQPELMCRT 295
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPaVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 296 AHGVDFATG------VTVAGPGLGGSDEAAHLLEQAI-ASPQPLVVDADGLNLVAARSGLaarLRSRKAATILTPHPLEA 368
Cdd:COG0063    81 LPEEDELLElleradAVVIGPGLGRDEETRELLRALLeAADKPLVLDADALNLLAEDPEL---LAALPAPTVLTPHPGEF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 369 ARLLATSIGAIQRDRLDSARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGW 448
Cdd:COG0063   158 ARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2452224051 449 EAALGAVWLHGMAADVLVTEgtGPVGLTAGELIPAIRTALNRLVA 493
Cdd:COG0063   238 EAAAAGVYLHGLAGDLAAEE--RGRGLLASDLIEALPAALRELLE 280
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 10-489 2.40e-76

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 248.44  E-value: 2.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  10 IRQIETESARRLPAG--ALMQRAGQAAANAALDLLPFAtsrARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGGT 87
Cdd:PRK10565   23 IRRGEREAADALGLTlyELMLRAGEAAFQVARSAYPDA---RHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  88 A--PERVRALERARASPARFMAEDGIGAGEWHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVPSGLDADTGC 165
Cdd:PRK10565  100 PlpEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 166 VVGpdgCAVHATHTLTFIGDKPGLHTCDGRDHAGAVTVAHLDIDA--AHYPAATIHLnDTAGFAHAAVARPQNSHKGSYG 243
Cdd:PRK10565  180 TPG---AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSwlAGQEAPIQRF-DAEQLSQWLKPRRPTSHKGDHG 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 244 NVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLC----FAGPALqcdAGQPELMCR--TAHGVDFA---TGVTVAGPGLGG 314
Cdd:PRK10565  256 RLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLtrseNIAPLL---TARPELMVHelTPDSLEESlewADVVVIGPGLGQ 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 315 SDEAAHLLEQAIASPQPLVVDADGLNLVAarsgLAARLRSRKaatILTPHPLEAARLLATSIGAIQRDRLDSARRLATAL 394
Cdd:PRK10565  333 QEWGKKALQKVENFRKPMLWDADALNLLA----INPDKRHNR---VITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 395 HAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVLVTEgTGPVG 474
Cdd:PRK10565  406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAAR-FGTRG 484

                         490
                  ....*....|....*
gi 2452224051 475 LTAGELIPAIRTALN 489
Cdd:PRK10565  485 MLATDLFSTLQRIVN 499
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-485 6.63e-74

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: 234.04  E-value: 6.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 236 NSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQCDAGQ-PELMCRTAHG--------VDFATGVT 306
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYsPELMVHPLLEtdieelleLLERADAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 307 VAGPGLGGSDEAAHLLEQAIASPQPLVVDADGLNLVAARSGLaarlRSRKAATILTPHPLEAARLLATSIGAIQRDRLDS 386
Cdd:cd01171    82 VIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSL----IKRYGPVVLTPHPGEFARLLGALVEEIQADRLAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 387 ARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVLV 466
Cdd:cd01171   158 AREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAA 237

                         250
                  ....*....|....*....
gi 2452224051 467 TEGTGpvGLTAGELIPAIR 485
Cdd:cd01171   238 KKKGA--GLTAADLVAEIP 254
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 233-490 5.60e-51

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: 174.88  E-value: 5.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 233 RPQNSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRV-FLCFAGPALQCDAGQPELMCR-----TAHGVDFAT--G 304
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVtVAAPENVITLINSVSPELIVHrlmwkVDEDEELLEryD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 305 VTVAGPGLGGSDEAAHLLEQAIASPQPLVVDADGLNLVAarsglaaRLRSRKAATILTPHPLEAARLLATSIgaIQRDRL 384
Cdd:TIGR00196  95 VVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLT-------YNQKREGEVILTPHPGEFKRLLGVNE--IQGDRL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 385 DSARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADV 464
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDL 245

                         250       260
                  ....*....|....*....|....*.
gi 2452224051 465 LvTEGTGPVGLTAGELIPAIRTALNR 490
Cdd:TIGR00196 246 A-LKNHGAYGLTALDLIEKIPRVCKR 270
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 245-465 3.15e-45

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: 158.68  E-value: 3.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 245 VAVLGGAPGMTGAPVLAGRAALHAGAGRV-FLCFAGPALQCDAGQPELMC---RTAHGVDFATG---VTVAGPGLGGSDE 317
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVsVATDSEAIAVLKSPLPEVMVhplPETSSILEKLSrydAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 318 AAHLLEQAIASPQPLVVDADGLNLVAARSGLAARlrsrKAATILTPHPLEAARLLAtSIGAIQRDRLDSARRLATALHAI 397
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPAR----EGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNGT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2452224051 398 VILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVL 465
Cdd:pfam01256 156 ILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLA 223
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-188 4.24e-25

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: 101.53  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  44 FATSRARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGG--------TAPERVRALeRARASPARFMAEDGIGAGE 115
Cdd:pfam03853  20 LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEeklsedarRQLDLFKKL-GGKIVTDNPDEDLEKLLSP 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452224051 116 WHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVPSGLDADTGCVvgpDGCAVHATHTLTFIGDKPG 188
Cdd:pfam03853  99 VDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAV---LGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 8-209 1.35e-18

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: 84.00  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051   8 AQIRQIETESARRL--PAGALMQRAGQAAANAALDLLPFAtsrARVLVLAGPGNNGGDALEAAAHLAHAGAhvaLVHFEG 85
Cdd:TIGR00197   6 PKDMAIDKENAEYLglTLDLLMENAGKAVAQAVLQAYPLA---GHVIIFCGPGNNGGDGFVVARHLKGFGV---EVFLLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  86 gtAPERVRALERARASPARFmaedGIGAGEWH-----------LVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALD 154
Cdd:TIGR00197  80 --KEKRIECTEQAEVNLKAL----KVGGISIDegnlvkpedcdVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2452224051 155 VPSGLDADTGCVVGPdgcAVHATHTLTFIGDKPGLHTCDGrDHAGAVTVAHLDID 209
Cdd:TIGR00197 154 IPSGLDVDTGAIEGP---AVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 47-168 8.16e-08

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 53.34  E-value: 8.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  47 SRARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGGTAPERVRALERARASPARFMAEDGIGAGEWHL-------V 119
Cdd:PLN03050   59 RHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAIGGTNDSSKPlettydvI 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2452224051 120 IDGLFGIGL-GRPVAgTFAALVAAINAL---PCPVLALDVPSGLDADTGCVVG 168
Cdd:PLN03050  139 VDAIFGFSFhGAPRA-PFDTLLAQMVQQqksPPPIVSVDVPSGWDVDEGDVSG 190
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 217-493 7.24e-92

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: 281.24  E-value: 7.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 217 TIHLNDTAGFAHAAVARPQNSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQ-CDAGQPELMCRT 295
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPaVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 296 AHGVDFATG------VTVAGPGLGGSDEAAHLLEQAI-ASPQPLVVDADGLNLVAARSGLaarLRSRKAATILTPHPLEA 368
Cdd:COG0063    81 LPEEDELLElleradAVVIGPGLGRDEETRELLRALLeAADKPLVLDADALNLLAEDPEL---LAALPAPTVLTPHPGEF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 369 ARLLATSIGAIQRDRLDSARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGW 448
Cdd:COG0063   158 ARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2452224051 449 EAALGAVWLHGMAADVLVTEgtGPVGLTAGELIPAIRTALNRLVA 493
Cdd:COG0063   238 EAAAAGVYLHGLAGDLAAEE--RGRGLLASDLIEALPAALRELLE 280
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 10-489 2.40e-76

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 248.44  E-value: 2.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  10 IRQIETESARRLPAG--ALMQRAGQAAANAALDLLPFAtsrARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGGT 87
Cdd:PRK10565   23 IRRGEREAADALGLTlyELMLRAGEAAFQVARSAYPDA---RHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  88 A--PERVRALERARASPARFMAEDGIGAGEWHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVPSGLDADTGC 165
Cdd:PRK10565  100 PlpEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 166 VVGpdgCAVHATHTLTFIGDKPGLHTCDGRDHAGAVTVAHLDIDA--AHYPAATIHLnDTAGFAHAAVARPQNSHKGSYG 243
Cdd:PRK10565  180 TPG---AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSwlAGQEAPIQRF-DAEQLSQWLKPRRPTSHKGDHG 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 244 NVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLC----FAGPALqcdAGQPELMCR--TAHGVDFA---TGVTVAGPGLGG 314
Cdd:PRK10565  256 RLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLtrseNIAPLL---TARPELMVHelTPDSLEESlewADVVVIGPGLGQ 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 315 SDEAAHLLEQAIASPQPLVVDADGLNLVAarsgLAARLRSRKaatILTPHPLEAARLLATSIGAIQRDRLDSARRLATAL 394
Cdd:PRK10565  333 QEWGKKALQKVENFRKPMLWDADALNLLA----INPDKRHNR---VITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 395 HAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVLVTEgTGPVG 474
Cdd:PRK10565  406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAAR-FGTRG 484

                         490
                  ....*....|....*
gi 2452224051 475 LTAGELIPAIRTALN 489
Cdd:PRK10565  485 MLATDLFSTLQRIVN 499
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-485 6.63e-74

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: 234.04  E-value: 6.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 236 NSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQCDAGQ-PELMCRTAHG--------VDFATGVT 306
Cdd:cd01171     2 DSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYsPELMVHPLLEtdieelleLLERADAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 307 VAGPGLGGSDEAAHLLEQAIASPQPLVVDADGLNLVAARSGLaarlRSRKAATILTPHPLEAARLLATSIGAIQRDRLDS 386
Cdd:cd01171    82 VIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSL----IKRYGPVVLTPHPGEFARLLGALVEEIQADRLAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 387 ARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVLV 466
Cdd:cd01171   158 AREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAA 237

                         250
                  ....*....|....*....
gi 2452224051 467 TEGTGpvGLTAGELIPAIR 485
Cdd:cd01171   238 KKKGA--GLTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 3-494 7.24e-52

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: 183.53  E-value: 7.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051   3 PLYTVAQIRQIETESARRL--PAGALMQRAGQAAANAALDLLPFAtsRARVLVLAGPGNNGGDALEAAAHLAHAGAHVAL 80
Cdd:COG0062     2 KLLTAAQMRALDRAAIEALgiPGLVLMERAGRAVARAIRRRFPSA--ARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  81 VHFEGGTA--PERVRALERARAS--PARFMAEDGIGAGEWHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVP 156
Cdd:COG0062    80 FLLGDPEKlsGDAAANLERLKAAgiPILELDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 157 SGLDADTGCVvgpDGCAVHATHTLTFIGDKPGLHTCDGRDHAGAVTVAHLDID-AAHYPAATIHLNDTAGFAHAAVARPQ 235
Cdd:COG0062   160 SGLDADTGEV---LGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGiPAAAEAPAALLLLADLLALLLPPRRR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 236 NSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRVFLCFAGPALQCDAGQPELMCRTAH-------GVDFATGVTVA 308
Cdd:COG0062   237 SHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALdddeellLLLAAAVVVAG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 309 GPGLGGSDEAAHLLEQAIASPQPLVVDADGLNLVAArsgLAARLRSRKAATILTPHPLEAARLLATSIGAIQRDRLDSAR 388
Cdd:COG0062   317 GGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLA---LAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAA 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 389 RLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVLVTE 468
Cdd:COG0062   394 AAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAA 473

                         490       500
                  ....*....|....*....|....*.
gi 2452224051 469 GTGPVGLTAGELIPAIRTALNRLVAR 494
Cdd:COG0062   474 LAAALLAAAAALIALLLAAALLLLLA 499
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 233-490 5.60e-51

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: 174.88  E-value: 5.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 233 RPQNSHKGSYGNVAVLGGAPGMTGAPVLAGRAALHAGAGRV-FLCFAGPALQCDAGQPELMCR-----TAHGVDFAT--G 304
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVtVAAPENVITLINSVSPELIVHrlmwkVDEDEELLEryD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 305 VTVAGPGLGGSDEAAHLLEQAIASPQPLVVDADGLNLVAarsglaaRLRSRKAATILTPHPLEAARLLATSIgaIQRDRL 384
Cdd:TIGR00196  95 VVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLT-------YNQKREGEVILTPHPGEFKRLLGVNE--IQGDRL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 385 DSARRLATALHAIVILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADV 464
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDL 245

                         250       260
                  ....*....|....*....|....*.
gi 2452224051 465 LvTEGTGPVGLTAGELIPAIRTALNR 490
Cdd:TIGR00196 246 A-LKNHGAYGLTALDLIEKIPRVCKR 270
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 245-465 3.15e-45

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: 158.68  E-value: 3.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 245 VAVLGGAPGMTGAPVLAGRAALHAGAGRV-FLCFAGPALQCDAGQPELMC---RTAHGVDFATG---VTVAGPGLGGSDE 317
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVsVATDSEAIAVLKSPLPEVMVhplPETSSILEKLSrydAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 318 AAHLLEQAIASPQPLVVDADGLNLVAARSGLAARlrsrKAATILTPHPLEAARLLAtSIGAIQRDRLDSARRLATALHAI 397
Cdd:pfam01256  81 GKAALEEVLAKDCPLVIDADALNLLAINNEKPAR----EGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNGT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2452224051 398 VILKGSGTVIGAPGGAIVINPTGNPALATAGTGDVLAGLCGALLAQGWPGWEAALGAVWLHGMAADVL 465
Cdd:pfam01256 156 ILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLA 223
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-188 4.24e-25

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: 101.53  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  44 FATSRARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGG--------TAPERVRALeRARASPARFMAEDGIGAGE 115
Cdd:pfam03853  20 LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEeklsedarRQLDLFKKL-GGKIVTDNPDEDLEKLLSP 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452224051 116 WHLVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALDVPSGLDADTGCVvgpDGCAVHATHTLTFIGDKPG 188
Cdd:pfam03853  99 VDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAV---LGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 8-209 1.35e-18

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: 84.00  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051   8 AQIRQIETESARRL--PAGALMQRAGQAAANAALDLLPFAtsrARVLVLAGPGNNGGDALEAAAHLAHAGAhvaLVHFEG 85
Cdd:TIGR00197   6 PKDMAIDKENAEYLglTLDLLMENAGKAVAQAVLQAYPLA---GHVIIFCGPGNNGGDGFVVARHLKGFGV---EVFLLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  86 gtAPERVRALERARASPARFmaedGIGAGEWH-----------LVIDGLFGIGLGRPVAGTFAALVAAINALPCPVLALD 154
Cdd:TIGR00197  80 --KEKRIECTEQAEVNLKAL----KVGGISIDegnlvkpedcdVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2452224051 155 VPSGLDADTGCVVGPdgcAVHATHTLTFIGDKPGLHTCDGrDHAGAVTVAHLDID 209
Cdd:TIGR00197 154 IPSGLDVDTGAIEGP---AVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 47-168 8.16e-08

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 53.34  E-value: 8.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  47 SRARVLVLAGPGNNGGDALEAAAHLAHAGAHVALVHFEGGTAPERVRALERARASPARFMAEDGIGAGEWHL-------V 119
Cdd:PLN03050   59 RHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAIGGTNDSSKPlettydvI 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2452224051 120 IDGLFGIGL-GRPVAgTFAALVAAINAL---PCPVLALDVPSGLDADTGCVVG 168
Cdd:PLN03050  139 VDAIFGFSFhGAPRA-PFDTLLAQMVQQqksPPPIVSVDVPSGWDVDEGDVSG 190
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 49-168 2.70e-04

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 43.30  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051  49 ARVLVLAGPGNNGGDaleaaahlaHAGAHVALVHFegGTAP-----------------ERVRALERARASPARFMAEDgi 111
Cdd:PLN03049   60 RRVLALCGPGNNGGD---------GLVAARHLHHF--GYKPsicypkrtdkplynglvTQLESLSVPFLSVEDLPSDL-- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452224051 112 gAGEWHLVIDGLFGI---GLGRPvagTFAALVAAINAL--PCPVLALDVPSGLDADTGCVVG 168
Cdd:PLN03049  127 -SSQFDIVVDAMFGFsfhGAPRP---PFDDLIQKLVRAagPPPIVSVDIPSGWHVEEGDVNG 184
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
358-473 7.40e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 42.08  E-value: 7.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 358 ATILTPHPLEAARLLATSIGAIQRDRLDSARRLATALHAIVILKGsGTVIGAPGGAIVINPTGNPALA---------TAG 428
Cdd:PRK14713  158 ADLITPNLPELAVLLGEPPATTWEEALAQARRLAAETGTTVLVKG-GHLDGQRAPDALVGPDGAVTEVpgprvdtrnTHG 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2452224051 429 TGDVLAGLCGALLAQGwPGWEAALGAV--WLHGM--AADVL-VTEGTGPV 473
Cdd:PRK14713  237 TGCSLSSALATRLGRG-GDWAAALRWAtaWLHGAiaAGAALqVGTGNGPV 285
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 375-472 2.08e-03

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: 39.83  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 375 SIGAIQRDRLDSARRLATALHAIVILKGSGTVIgAPGGAIVINPTGNPALAT-AGTGDVLAGLCGALLAQGWPGWEAALG 453
Cdd:cd01170   133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYI-TDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVS 211

                          90
                  ....*....|....*....
gi 2452224051 454 AVWLHGMAADVLVTEGTGP 472
Cdd:cd01170   212 AVLVYGIAGELAAERAKGP 230
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 314-451 7.62e-03

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 38.10  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 314 GSDEAAHLLEQAIA--SPQPLVVD----ADGLNLVAARSGLAArLRSR--KAATILTPHPLEAARLLATSIgaiqrDRLD 385
Cdd:COG0351    76 GSAEIIEAVAEILAdyPLVPVVLDpvmvAKSGDRLLDEDAVEA-LRELllPLATVVTPNLPEAEALLGIEI-----TTLD 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452224051 386 SARRLATALHAI----VILKGsgtviGAPGGAIVIN----------------PTGNpalaTAGTGDVLAGLCGALLAQGW 445
Cdd:COG0351   150 DMREAAKALLELgakaVLVKG-----GHLPGDEAVDvlydgdgvrefsapriDTGN----THGTGCTLSSAIAALLAKGL 220


                  ....*.
gi 2452224051 446 PGWEAA 451
Cdd:COG0351   221 DLEEAV 226
 
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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