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Conserved domains on  [gi|398366083|ref|NP_011708|]
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glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH3 [Saccharomyces cerevisiae S288c]

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List of domain hits

Name Accession Description Interval E-value
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
155-312 7.12e-96

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


:

Pssm-ID: 251539  Cd Length: 158  Bit Score: 283.68  E-value: 7.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  155 LAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVP 234
Cdd:pfam02800   1 LAPLAKVLNDNFGIEKGLMTTVHAYTADQKLVDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLTGMAFRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366083  235 TVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWY 312
Cdd:pfam02800  81 TPNVSVVDLTVELEKPVTVEEVNAALKEAAEGALKGILGYTEEPLVSSDFIGDPHSSIFDAKATIVLNGNFVKVVAWY 158
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
2-150 1.08e-80

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


:

Pssm-ID: 249536  Cd Length: 150  Bit Score: 244.72  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFiTNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:pfam00044   1 IKVGINGFGRIGRLVLRAALAQDDLEVVAINDLT-DPETLAYLLKYDSVHGRFDGEVEVDEDGLIVNGKKIKVFAERDPA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366083   82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS--TAPMFVMGVNEEKYTSDLKIVSNASC 150
Cdd:pfam00044  80 ELPWGELGVDIVVESTGVFTTAEKAEAHLKAGAKKVIISAPAKddADPTFVYGVNHDDYDPEDDIVSNASC 150
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
1-332 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]


:

Pssm-ID: 223135 [Multi-domain]  Cd Length: 335  Bit Score: 530.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRIALSRP-NVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERD 79
Cdd:COG0057    1 MIKVAINGFGRIGRLVARAALERDgDIEVVAINDL-TDPDYLAHLLKYDSVHGRFDGEVEVKDDALVVNGKGIKVLAERD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDA-GAKKVVITAPS-STAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAP 157
Cdd:COG0057   80 PANLPWADLGVDIVVECTGKFTGREKAEKHLKAgGAKKVLISAPGkDDVATVVYGVNHNYYDAGHTIVSNASCTTNCLAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 158 LAKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:COG0057  160 VAKVLNDAFGIEKGLMTTVHAYTNDQKLVDGP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLTGMAIRVPTPN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYG 317
Cdd:COG0057  239 VSVVDLTVELEKEVTVEEINAALKAASEIGLKGILGYTEDPLVSSDFNGDPHSSIFDASATIVLGGNLVKLVAWYDNEWG 318
                        330
                 ....*....|....*
gi 398366083 318 YSTRVVDLVEHVAKA 332
Cdd:COG0057  319 YSNRVVDLLAMVAKA 333
 
Name Accession Description Interval E-value
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
155-312 7.12e-96

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 251539  Cd Length: 158  Bit Score: 283.68  E-value: 7.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  155 LAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVP 234
Cdd:pfam02800   1 LAPLAKVLNDNFGIEKGLMTTVHAYTADQKLVDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLTGMAFRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366083  235 TVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWY 312
Cdd:pfam02800  81 TPNVSVVDLTVELEKPVTVEEVNAALKEAAEGALKGILGYTEEPLVSSDFIGDPHSSIFDAKATIVLNGNFVKVVAWY 158
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
2-150 1.08e-80

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 249536  Cd Length: 150  Bit Score: 244.72  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFiTNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:pfam00044   1 IKVGINGFGRIGRLVLRAALAQDDLEVVAINDLT-DPETLAYLLKYDSVHGRFDGEVEVDEDGLIVNGKKIKVFAERDPA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366083   82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS--TAPMFVMGVNEEKYTSDLKIVSNASC 150
Cdd:pfam00044  80 ELPWGELGVDIVVESTGVFTTAEKAEAHLKAGAKKVIISAPAKddADPTFVYGVNHDDYDPEDDIVSNASC 150
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
2-150 3.44e-77

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851  Cd Length: 149  Bit Score: 235.52  E-value: 3.44e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083     2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA-PMFVMGVNEEKYTSDLKIVSNASC 150
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
3-44 7.16e-04

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 39.47  E-value: 7.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 398366083   3 RVAINGFGRIGRLVMRiaLSRP-NVEVVAlNDPFITNDYAAYM 44
Cdd:cd12167  152 TVGIVGFGRIGRAVVE--LLRPfGLRVLV-YDPYLPAAEAAAL 191
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
1-332 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]


Pssm-ID: 223135 [Multi-domain]  Cd Length: 335  Bit Score: 530.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRIALSRP-NVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERD 79
Cdd:COG0057    1 MIKVAINGFGRIGRLVARAALERDgDIEVVAINDL-TDPDYLAHLLKYDSVHGRFDGEVEVKDDALVVNGKGIKVLAERD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDA-GAKKVVITAPS-STAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAP 157
Cdd:COG0057   80 PANLPWADLGVDIVVECTGKFTGREKAEKHLKAgGAKKVLISAPGkDDVATVVYGVNHNYYDAGHTIVSNASCTTNCLAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 158 LAKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:COG0057  160 VAKVLNDAFGIEKGLMTTVHAYTNDQKLVDGP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLTGMAIRVPTPN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYG 317
Cdd:COG0057  239 VSVVDLTVELEKEVTVEEINAALKAASEIGLKGILGYTEDPLVSSDFNGDPHSSIFDASATIVLGGNLVKLVAWYDNEWG 318
                        330
                 ....*....|....*
gi 398366083 318 YSTRVVDLVEHVAKA 332
Cdd:COG0057  319 YSNRVVDLLAMVAKA 333
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-330 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 540.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSH-DDKHIIVDGKKIATYQERDP 80
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  81 ANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV 240
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 241 VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYST 320
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
                        330
                 ....*....|
gi 398366083 321 RVVDLVEHVA 330
Cdd:PLN02272 406 RVLDLIEHMA 415
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
3-324 2.87e-170

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two PFAM models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model [Energy metabolism, Glycolysis/gluconeogenesis].


Pssm-ID: 233453 [Multi-domain]  Cd Length: 326  Bit Score: 479.46  E-value: 2.87e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    3 RVAINGFGRIGRLVMRIALSRP--NVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATY-QERD 79
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRAILEKPgnDLEVVAINDL-TDLEYLAYLLKYDSVHGRFEGEVTADEDGLVVNGKEVISVfSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPL 158
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEGHLEAGAKKVLISAPSKgDVKTIVYGVNHDEYDPSERIVSNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  159 AKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHSYTNDQNLVDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQ--LSPKFVKLVSWYDNEY 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEAAEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVVAWYDNEW 318

                  ....*...
gi 398366083  317 GYSTRVVD 324
Cdd:TIGR01534 319 GYSNRVVD 326
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
2-331 3.66e-164

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 464.69  E-value: 3.66e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:PTZ00023   3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAK 160
Cdd:PTZ00023  83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKdDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSH--KDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:PTZ00023 163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGY 318
Cdd:PTZ00023 243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGY 322
                        330
                 ....*....|...
gi 398366083 319 STRVVDLVEHVAK 331
Cdd:PTZ00023 323 SNRLLDLAHYITQ 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
2-331 3.24e-151

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 431.46  E-value: 3.24e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDpFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDlKIVSNASCTTNCLAPLAK 160
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKdNTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 241 VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYST 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
                        330
                 ....*....|.
gi 398366083 321 RVVDLVEHVAK 331
Cdd:PRK15425 321 KVLDLIAHISK 331
 
Name Accession Description Interval E-value
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
155-312 7.12e-96

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 251539  Cd Length: 158  Bit Score: 283.68  E-value: 7.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  155 LAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVP 234
Cdd:pfam02800   1 LAPLAKVLNDNFGIEKGLMTTVHAYTADQKLVDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLTGMAFRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366083  235 TVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWY 312
Cdd:pfam02800  81 TPNVSVVDLTVELEKPVTVEEVNAALKEAAEGALKGILGYTEEPLVSSDFIGDPHSSIFDAKATIVLNGNFVKVVAWY 158
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
2-150 1.08e-80

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 249536  Cd Length: 150  Bit Score: 244.72  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFiTNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:pfam00044   1 IKVGINGFGRIGRLVLRAALAQDDLEVVAINDLT-DPETLAYLLKYDSVHGRFDGEVEVDEDGLIVNGKKIKVFAERDPA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366083   82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS--TAPMFVMGVNEEKYTSDLKIVSNASC 150
Cdd:pfam00044  80 ELPWGELGVDIVVESTGVFTTAEKAEAHLKAGAKKVIISAPAKddADPTFVYGVNHDDYDPEDDIVSNASC 150
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
2-150 3.44e-77

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851  Cd Length: 149  Bit Score: 235.52  E-value: 3.44e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083     2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA-PMFVMGVNEEKYTSDLKIVSNASC 150
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
3-44 7.16e-04

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 39.47  E-value: 7.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 398366083   3 RVAINGFGRIGRLVMRiaLSRP-NVEVVAlNDPFITNDYAAYM 44
Cdd:cd12167  152 TVGIVGFGRIGRAVVE--LLRPfGLRVLV-YDPYLPAAEAAAL 191
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
1-332 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]


Pssm-ID: 223135 [Multi-domain]  Cd Length: 335  Bit Score: 530.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRIALSRP-NVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERD 79
Cdd:COG0057    1 MIKVAINGFGRIGRLVARAALERDgDIEVVAINDL-TDPDYLAHLLKYDSVHGRFDGEVEVKDDALVVNGKGIKVLAERD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDA-GAKKVVITAPS-STAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAP 157
Cdd:COG0057   80 PANLPWADLGVDIVVECTGKFTGREKAEKHLKAgGAKKVLISAPGkDDVATVVYGVNHNYYDAGHTIVSNASCTTNCLAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 158 LAKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:COG0057  160 VAKVLNDAFGIEKGLMTTVHAYTNDQKLVDGP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLTGMAIRVPTPN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYG 317
Cdd:COG0057  239 VSVVDLTVELEKEVTVEEINAALKAASEIGLKGILGYTEDPLVSSDFNGDPHSSIFDASATIVLGGNLVKLVAWYDNEWG 318
                        330
                 ....*....|....*
gi 398366083 318 YSTRVVDLVEHVAKA 332
Cdd:COG0057  319 YSNRVVDLLAMVAKA 333
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-330 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 540.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSH-DDKHIIVDGKKIATYQERDP 80
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  81 ANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV 240
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 241 VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYST 320
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
                        330
                 ....*....|
gi 398366083 321 RVVDLVEHVA 330
Cdd:PLN02272 406 RVLDLIEHMA 415
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
3-324 2.87e-170

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two PFAM models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model [Energy metabolism, Glycolysis/gluconeogenesis].


Pssm-ID: 233453 [Multi-domain]  Cd Length: 326  Bit Score: 479.46  E-value: 2.87e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    3 RVAINGFGRIGRLVMRIALSRP--NVEVVALNDPfITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATY-QERD 79
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRAILEKPgnDLEVVAINDL-TDLEYLAYLLKYDSVHGRFEGEVTADEDGLVVNGKEVISVfSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPL 158
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEGHLEAGAKKVLISAPSKgDVKTIVYGVNHDEYDPSERIVSNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  159 AKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHSYTNDQNLVDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQ--LSPKFVKLVSWYDNEY 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEAAEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVVAWYDNEW 318

                  ....*...
gi 398366083  317 GYSTRVVD 324
Cdd:TIGR01534 319 GYSNRVVD 326
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
2-331 3.66e-164

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 464.69  E-value: 3.66e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:PTZ00023   3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAK 160
Cdd:PTZ00023  83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKdDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSH--KDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:PTZ00023 163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGY 318
Cdd:PTZ00023 243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGY 322
                        330
                 ....*....|...
gi 398366083 319 STRVVDLVEHVAK 331
Cdd:PTZ00023 323 SNRLLDLAHYITQ 335
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
2-332 7.50e-162

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 458.80  E-value: 7.50e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYA-GEVS-HDDKHIIVDGKKIATYQERD 79
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKiKDDKTLLFGEKPVTVFGIRN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLA 159
Cdd:PLN02358  86 PEDIPWAEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 160 KVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVS 239
Cdd:PLN02358 166 KVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDVS 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 240 VVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYS 319
Cdd:PLN02358 246 VVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYS 325
                        330
                 ....*....|...
gi 398366083 320 TRVVDLVEHVAKA 332
Cdd:PLN02358 326 SRVVDLIVHMSKA 338
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
2-331 3.24e-151

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 431.46  E-value: 3.24e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDpFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  82 NLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSS-TAPMFVMGVNEEKYTSDlKIVSNASCTTNCLAPLAK 160
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKdNTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 161 VINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 241 VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYST 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
                        330
                 ....*....|.
gi 398366083 321 RVVDLVEHVAK 331
Cdd:PRK15425 321 KVLDLIAHISK 331
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
1-331 3.56e-141

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 406.43  E-value: 3.56e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFiTNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDP 80
Cdd:PRK07729   2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  81 ANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPM-FVMGVNEEKYTSDLK-IVSNASCTTNCLAPL 158
Cdd:PRK07729  81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 159 AKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGY 318
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
                        330
                 ....*....|...
gi 398366083 319 STRVVDLVEHVAK 331
Cdd:PRK07729 320 SCRVVDLVTLVAD 332
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
2-330 3.69e-129

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 376.32  E-value: 3.69e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRI----ALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVS--------HDDKHIIVDG 69
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  70 KKIATYQ-ERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSST-APMFVMGVNEEKYT-SDLKIVS 146
Cdd:PTZ00434  84 HRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGgAKTIVMGVNQHEYSpTEHHVVS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 147 NASCTTNCLAPLAKVI-NDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGK 225
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 226 LTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLS--- 302
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpg 323
                        330       340
                 ....*....|....*....|....*....
gi 398366083 303 -PKFVKLVSWYDNEYGYSTRVVDLVEHVA 330
Cdd:PTZ00434 324 eRRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
PRK07403 PRK07403
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
1-331 4.13e-126

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 367.69  E-value: 4.13e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRIALSRPN--VEVVALNDpfiTND--YAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQ 76
Cdd:PRK07403   1 MIRVAINGFGRIGRNFLRCWLGRENsqLELVAIND---TSDprTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  77 ERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPM--FVMGVNEEKYTSDL-KIVSNASCTTN 153
Cdd:PRK07403  78 DRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgtYVVGVNHHEYDHEDhNIISNASCTTN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 154 CLAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRV 233
Cdd:PRK07403 158 CLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 234 PTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYD 313
Cdd:PRK07403 237 PTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYD 316
                        330
                 ....*....|....*...
gi 398366083 314 NEYGYSTRVVDLVEHVAK 331
Cdd:PRK07403 317 NEWGYSQRVVDLAELVAR 334
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
2-331 1.42e-112

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 335.36  E-value: 1.42e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPN--VEVVALNDPFITNDyAAYMFKYDSTHGRYAGEVS-HDDKHIIVDGKKIATYQER 78
Cdd:PLN03096  61 IKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTGGVKQ-ASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  79 DPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA-PMFVMGVNEEKYTSDLKIVSNASCTTNCLAP 157
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDiPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 158 LAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYG 317
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378
                        330
                 ....*....|....
gi 398366083 318 YSTRVVDLVEHVAK 331
Cdd:PLN03096 379 YSQRVVDLADIVAN 392
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
2-332 5.76e-110

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 326.30  E-value: 5.76e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPA 81
Cdd:PRK08955   3 IKVGINGFGRIGRLALRAAWDWPEVEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  82 NLPWgsSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAP--SSTAPMFVMGVNEEKYTSDL-KIVSNASCTTNCLAPL 158
Cdd:PRK08955  83 DTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 159 AKVINDAFGIEEGLMTTVHSLTATQKTVDGPsHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDV 238
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 239 SVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGY 318
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
                        330
                 ....*....|....
gi 398366083 319 STRVVDLVEHVAKA 332
Cdd:PRK08955 320 ANRTAELARKVGLA 333
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
2-331 9.06e-108

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 324.55  E-value: 9.06e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPN--VEVVALNDPFITNDyAAYMFKYDSTHGRYAGEVS-HDDKHIIVDGKKIATYQER 78
Cdd:PLN02237  76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKN-ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  79 DPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA--PMFVMGVNEEKYTSDL-KIVSNASCTTNCL 155
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGAdiPTYVVGVNEDDYDHEVaNIVSNASCTTNCL 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 156 APLAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPT 235
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 236 VDVSVVDLTVKLNKE-TTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDN 314
Cdd:PLN02237 314 PNVSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
                        330
                 ....*....|....*..
gi 398366083 315 EYGYSTRVVDLVEHVAK 331
Cdd:PLN02237 394 EWGYSQRVVDLAHLVAA 410
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
3-324 6.15e-103

erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine].


Pssm-ID: 130595 [Multi-domain]  Cd Length: 325  Bit Score: 307.98  E-value: 6.15e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083    3 RVAINGFGRIGRLVMRIALSRPN---VEVVALNDpFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERD 79
Cdd:TIGR01532   1 RVAINGFGRIGRNVLRALYESGRraeITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA--PMFVMGVNEEKYTSDLKIVSNASCTTNCLAP 157
Cdd:TIGR01532  80 LQSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDldATIVYGVNQDQLRAEHRIVSNASCTTNCIVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  158 LAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:TIGR01532 160 VIKLLDDAYGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYG 317
Cdd:TIGR01532 239 VTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWG 318

                  ....*..
gi 398366083  318 YSTRVVD 324
Cdd:TIGR01532 319 FANRMLD 325
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
1-332 1.01e-99

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 300.05  E-value: 1.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   1 MVRVAINGFGRIGRLVMRiAL----SRPNVEVVALN---DPfitnDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIA 73
Cdd:PRK13535   1 TIRVAINGFGRIGRNVLR-ALyesgRRAEITVVAINelaDA----EGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  74 TYQERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTA--PMFVMGVNEEKYTSDLKIVSNASCT 151
Cdd:PRK13535  76 LLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDldATVVYGVNHDQLRAEHRIVSNASCT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 152 TNCLAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAF 231
Cdd:PRK13535 156 TNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 232 RVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDAS----AGIQLspkfVK 307
Cdd:PRK13535 235 RVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTqtrvSGAHL----IK 310
                        330       340
                 ....*....|....*....|....*
gi 398366083 308 LVSWYDNEYGYSTRVVDLVEHVAKA 332
Cdd:PRK13535 311 TLVWCDNEWGFANRMLDTTLAMAAA 335
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
4-332 7.65e-85

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 266.40  E-value: 7.65e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   4 VAINGFGRIGRLVMRIALSRPNVE--------VVALNDPfitNDYA--AYMFKYDSTHGRYAG--EVSHDDKHIIVDGKK 71
Cdd:PRK08289 130 VVLYGFGRIGRLLARLLIEKTGGGnglrlraiVVRKGSE---GDLEkrASLLRRDSVHGPFNGtiTVDEENNAIIANGNY 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  72 IATYQERDPANLPWGSSNVD--IAIDSTGVFKELDTAQKHIDA-GAKKVVITAPSSTA-PMFVMGVNEEKYTSDLKIVSN 147
Cdd:PRK08289 207 IQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDiKNIVHGVNHSDITDEDKIVSA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 148 ASCTTNCLAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGpSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLT 227
Cdd:PRK08289 287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLT 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 228 GMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAA-EGKLKGVLGYTEDA-VVSSDFLGDSHSSIFDASAGIqLSPKF 305
Cdd:PRK08289 366 GNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATI-VNGNR 444
                        330       340
                 ....*....|....*....|....*..
gi 398366083 306 VKLVSWYDNEYGYSTRVVDLVEHVAKA 332
Cdd:PRK08289 445 AVLYVWYDNEFGYSCQVVRVMEQMAGV 471
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
2-329 4.09e-49

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 169.29  E-value: 4.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083   2 VRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAG-EVSHDDKHIIVDG-KKIATYQERD 79
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAKHD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  80 PANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLA 159
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 160 KVINDAFGIEEGLMTTVHSlTATQKTVDGPSH--KDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVD 237
Cdd:PTZ00353 163 RALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 238 VSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDShSSIFDASAGIQLSP-KFVKLVSWYDNEY 316
Cdd:PTZ00353 242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREgEVHKMVLWFDVEC 320
                        330
                 ....*....|...
gi 398366083 317 GYSTRVVDLVEHV 329
Cdd:PTZ00353 321 YYAARLLSLVKQL 333
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]
88-267 1.39e-06

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]


Pssm-ID: 223214 [Multi-domain]  Cd Length: 334  Bit Score: 47.99  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  88 SNVDIAIDSTGvfkeLDTAQKHIDAGAK--KVVITAPSS-----TAPMFVMGVNEE---KYTSDLKIVSNASCTTNCLAP 157
Cdd:COG0136   65 SDVDIVFFAAG----GSVSKEVEPKAAEagCVVIDNSSAfrmdpDVPLVVPEVNPEhliDYQKRGFIIANPNCSTIQLVL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083 158 LAKVINDAFGIEE------------GLMTTVHSLTATQKTVDGPSHKDwrGGRTASGNIIP-----SSTGAAKA------ 214
Cdd:COG0136  141 ALKPLHDAFGIKRvvvstyqavsgaGAEGGVELAGQTDALLNGIPILP--IGYPLAFNVIPhidgfLDNGYTKEewkiea 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 398366083 215 -VGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGK 267
Cdd:COG0136  219 eTRKILGDPDIKVSATCVRVPVFYGHSEAVTVEFKKDVDPEEIREELLPSAPGV 272
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
143-261 1.55e-03

aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan [Amino acid biosynthesis, Aspartate family].


Pssm-ID: 233220 [Multi-domain]  Cd Length: 341  Bit Score: 38.59  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366083  143 KIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSLtatqktvdgpSHKDWRGGRTAS--GNIIPSSTGAAKAVGKVLP 220
Cdd:TIGR00978 139 FIVTNPNCTTAGLTLALKPLIDAFGIKKVHVTTMQAV----------SGAGYPGVPSMDilDNIIPHIGGEEEKIERETR 208
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366083  221 ELQGKLTG------------MAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVK 261
Cdd:TIGR00978 209 KILGKLENgkiepapfsvsaTTTRVPVLDGHTESVHVEFDKKFDIEEIREALK 261
DapB COG0289
Dihydrodipicolinate reductase [Amino acid transport and metabolism]
1-30 7.40e-03

Dihydrodipicolinate reductase [Amino acid transport and metabolism]


Pssm-ID: 223366 [Multi-domain]  Cd Length: 266  Bit Score: 36.09  E-value: 7.40e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 398366083   1 MVRVAINGF-GRIGRLVMRIALSRPNVEVVA 30
Cdd:COG0289    2 MIKVAVAGAsGRMGRTLIRAVLEAPDLELVA 32
PRK00048 PRK00048
dihydrodipicolinate reductase; Provisional
1-30 8.54e-03

dihydrodipicolinate reductase; Provisional


Pssm-ID: 234595 [Multi-domain]  Cd Length: 257  Bit Score: 35.89  E-value: 8.54e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 398366083   1 MVRVAINGF-GRIGRLVMRIALSRPNVEVVA 30
Cdd:PRK00048   1 MIKVAVAGAsGRMGRELIEAVEAAEDLELVA 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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