NCBI Conserved Domain Search

Conserved domains on [gi|156986379|gb|ABU99281|]

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triosephosphate isomerase/glyceraldehyde-3-phosphate dehydrogenase, partial [Phytophthora inflata]

Protein Classification

bifunctional triose-phosphate isomerase/glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 12850616)

bifunctional triose-phosphate isomerase/glyceraldehyde-3-phosphate dehydrogenase catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate (G3P), and the the NAD-dependent oxidative phosphorylation of G3P to 1,3-bisphosphoglycerate; may be partial

CATH: 3.20.20.70|3.30.360.10|3.40.50.720

EC: 5.3.1.1|1.2.1.12

Gene Ontology: GO:0004807|GO:0005975|GO:0006096|GO:0030554|GO:0004365

PubMed: 23284996|10677844|12206759|11257493|21895736|25286305

SCOP: 4003038|4000077

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

GapA

COG0057

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...

218-522

2.37e-180

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis

Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 509.55 E-value: 2.37e-180

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 218 AVNVAINGFGRIGRLVLRAAATN-PLINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMN 296
Cdd:COG0057    2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASCTTNCLAPL 375
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 376 AKVVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADV 455
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379 456 SVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNL 306

PTZ00333

triosephosphate isomerase; Provisional

1-212

1.22e-108

triosephosphate isomerase; Provisional

Pssm-ID: 240365 Cd Length: 255 Bit Score: 323.79 E-value: 1.22e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:PTZ00333  39 DVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEISAEMLKDLGINWTILGHSERRQYfGETNEIVAQKVKNA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKD--WTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:PTZ00333 119 LENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAE 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPDFLQIINAQNPT 212
Cdd:PTZ00333 199 KVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPDFVDIIKSAEQS 254

Name

Accession

Description

Interval

E-value

GapA

COG0057

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...

218-522

2.37e-180

Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 509.55 E-value: 2.37e-180

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 218 AVNVAINGFGRIGRLVLRAAATN-PLINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMN 296
Cdd:COG0057    2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASCTTNCLAPL 375
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 376 AKVVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADV 455
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379 456 SVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNL 306

PLN02272

glyceraldehyde-3-phosphate dehydrogenase

216-522

1.93e-173

glyceraldehyde-3-phosphate dehydrogenase

Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 495.53 E-value: 1.93e-173

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 216 GGAVNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSH-DEKHIFVNGKPIRVFHE 294
Cdd:PLN02272  83 SGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSK 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 295 MNPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMFVMGVNHELYEKNMHVVSNASCTTNCLAP 374
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 375 LAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASF 390

GAPDH-I

TIGR01534

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...

220-521

6.01e-148

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: 273675 [Multi-domain] Cd Length: 326 Bit Score: 427.08 E-value: 6.01e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  220 NVAINGFGRIGRLVLRAAATNP--LINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKP-IRVFHEMN 296
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASCTTNCLAPL 375
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  376 AKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSkKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADV 455
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379  456 SVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDD 521
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLG 304

PTZ00333

triosephosphate isomerase; Provisional

1-212

1.22e-108

triosephosphate isomerase; Provisional

Pssm-ID: 240365 Cd Length: 255 Bit Score: 323.79 E-value: 1.22e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:PTZ00333  39 DVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEISAEMLKDLGINWTILGHSERRQYfGETNEIVAQKVKNA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKD--WTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:PTZ00333 119 LENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAE 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPDFLQIINAQNPT 212
Cdd:PTZ00333 199 KVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPDFVDIIKSAEQS 254

TIM

cd00311

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...

1-207

4.09e-103

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.

Pssm-ID: 238190 Cd Length: 242 Bit Score: 309.47 E-value: 4.09e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:cd00311   34 EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYfGETDEDVAKKVKAA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKV 158
Cdd:cd00311  114 LEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELY 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 156986379 159 SpEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPD-FLQIIN 207
Cdd:cd00311  194 G-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLDIIK 242

GAPDH_I_C

cd18126

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...

367-522

3.66e-102

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, 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.

Pssm-ID: 467676 Cd Length: 165 Bit Score: 303.99 E-value: 3.66e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 367 CTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKkDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGM 446
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 447 SFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNL 155

TpiA

COG0149

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...

1-208

6.91e-102

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis

Pssm-ID: 439919 [Multi-domain] Cd Length: 249 Bit Score: 306.21 E-value: 6.91e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:COG0149   37 EVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYfGETDELVNKKVKAA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:COG0149  117 LAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAE 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:COG0149  197 LYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAeDFLAIVRA 249

G3PDH_Arsen

NF033735

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;

221-512

2.64e-100

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;

Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 305.32 E-value: 2.64e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 221 VAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPANI 300
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 301 KWGEeQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMF--VMGVNHELYEKNMH-VVSNASCTTNCLAPLAK 377
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHrIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 378 VVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVSV 457
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156986379 458 VDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDA 512
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293

TIM

pfam00121

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...

1-208

2.35e-99

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.

Pssm-ID: 459680 Cd Length: 244 Bit Score: 299.81 E-value: 2.35e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379    1 EVVVAPSQVHAATVKASLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYAL 79
Cdd:pfam00121  34 EVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYfGETDEDVAKKVKAAL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   80 EKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWT-NVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKv 158
Cdd:pfam00121 114 KAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL- 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156986379  159 SPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:pfam00121 193 YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLDIINA 243

Gp_dh_C

pfam02800

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...

372-522

3.40e-77

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: 460700 Cd Length: 158 Bit Score: 239.42 E-value: 3.40e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  372 LAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVP 451
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156986379  452 TADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNF 151

Gp_dh_N

smart00846

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...

219-367

1.10e-72

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 [Multi-domain] Cd Length: 149 Bit Score: 227.43 E-value: 1.10e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   299 NIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASC 367
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149

tim

TIGR00419

triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...

1-201

1.21e-47

triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family. [Energy metabolism, Glycolysis/gluconeogenesis]

Pssm-ID: 129513 [Multi-domain] Cd Length: 205 Bit Score: 164.21 E-value: 1.21e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379    1 EVVVAPSQVHAATVKASLRsdVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREKGETnevVAKKAAYALE 80
Cdd:TIGR00419  34 AVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERRMKLAD---IEKKIARLKE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   81 KGLGVIACIgetkelreanktvEYITEQLDAYAaeikdWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAwlkekvSP 160
Cdd:TIGR00419 109 LGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAVEPPELIGTGIPVSPAQPEVVHGSVRA------VK 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 156986379  161 EAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPD 201
Cdd:TIGR00419 165 EVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205

Name

Accession

Description

Interval

E-value

GapA

COG0057

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...

218-522

2.37e-180

Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 509.55 E-value: 2.37e-180

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 218 AVNVAINGFGRIGRLVLRAAATN-PLINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMN 296
Cdd:COG0057    2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASCTTNCLAPL 375
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 376 AKVVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADV 455
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379 456 SVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNL 306

PLN02272

glyceraldehyde-3-phosphate dehydrogenase

216-522

1.93e-173

glyceraldehyde-3-phosphate dehydrogenase

Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 495.53 E-value: 1.93e-173

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 216 GGAVNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSH-DEKHIFVNGKPIRVFHE 294
Cdd:PLN02272  83 SGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSK 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 295 MNPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMFVMGVNHELYEKNMHVVSNASCTTNCLAP 374
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 375 LAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASF 390

PTZ00023

glyceraldehyde-3-phosphate dehydrogenase; Provisional

218-522

3.32e-150

glyceraldehyde-3-phosphate dehydrogenase; Provisional

Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 433.11 E-value: 3.32e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 218 AVNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNP 297
Cdd:PTZ00023   2 VVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 298 ANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSD-APMFVMGVNHELYEKNMHVVSNASCTTNCLAPLA 376
Cdd:PTZ00023  82 AAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDdTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 377 KVVNDKFGIKEGLMTTVHAVTATQKTVDGPSK--KDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PTZ00023 162 KVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPD 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:PTZ00023 242 VSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTF 309

GAPDH-I

TIGR01534

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...

220-521

6.01e-148

Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 427.08 E-value: 6.01e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  220 NVAINGFGRIGRLVLRAAATNP--LINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKP-IRVFHEMN 296
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASCTTNCLAPL 375
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  376 AKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSkKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADV 455
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379  456 SVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDD 521
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLG 304

PLN02358

glyceraldehyde-3-phosphate dehydrogenase

219-522

1.63e-139

glyceraldehyde-3-phosphate dehydrogenase

Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 406.03 E-value: 1.63e-139

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGS--LSHDEKHIFVNGKPIRVFHEMN 296
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHelKVKDDKTLLFGEKPVTVFGIRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMFVMGVNHELYEKNMHVVSNASCTTNCLAPLA 376
Cdd:PLN02358  86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 377 KVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVS 456
Cdd:PLN02358 166 KVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVS 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 457 VVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:PLN02358 246 VVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKF 311

gapA

PRK15425

glyceraldehyde-3-phosphate dehydrogenase;

219-522

7.97e-127

glyceraldehyde-3-phosphate dehydrogenase;

Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 373.30 E-value: 7.97e-127

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDpFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 299 NIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSD-APMFVMGVNHELYeKNMHVVSNASCTTNCLAPLAK 377
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY-AGQDIVSNASCTTNCLAPLAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 378 VVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVSV 457
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156986379 458 VDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNF 305

PTZ00434

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional

219-514

9.07e-117

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional

Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 348.97 E-value: 9.07e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPL----INIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSHDEKH--------IFVNG 286
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAICDQGLigteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLVVNG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 287 KPIR-VFHEMNPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSD-APMFVMGVNHELYE-KNMHVVS 363
Cdd:PTZ00434  84 HRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGgAKTIVMGVNQHEYSpTEHHVVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 364 NASCTTNCLAPLAKV-VNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGK 442
Cdd:PTZ00434 164 NASCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156986379 443 LTGMSFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASA 514
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKA 315

PTZ00333

triosephosphate isomerase; Provisional

1-212

1.22e-108

triosephosphate isomerase; Provisional

Pssm-ID: 240365 Cd Length: 255 Bit Score: 323.79 E-value: 1.22e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:PTZ00333  39 DVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEISAEMLKDLGINWTILGHSERRQYfGETNEIVAQKVKNA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKD--WTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:PTZ00333 119 LENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAE 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPDFLQIINAQNPT 212
Cdd:PTZ00333 199 KVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPDFVDIIKSAEQS 254

PRK07729

glyceraldehyde-3-phosphate dehydrogenase; Validated

219-511

3.21e-108

glyceraldehyde-3-phosphate dehydrogenase; Validated

Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 326.31 E-value: 3.21e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTyMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:PRK07729   3 TKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSET-LAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 299 NIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPM-FVMGVNHELYE-KNMHVVSNASCTTNCLAPLA 376
Cdd:PRK07729  82 ELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDiEKHTIISNASCTTNCLAPVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 377 KVVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVS 456
Cdd:PRK07729 162 KVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156986379 457 VVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFD 511
Cdd:PRK07729 241 LVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID 295

TIM

cd00311

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...

1-207

4.09e-103

Pssm-ID: 238190 Cd Length: 242 Bit Score: 309.47 E-value: 4.09e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:cd00311   34 EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYfGETDEDVAKKVKAA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKV 158
Cdd:cd00311  114 LEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELY 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 156986379 159 SpEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPD-FLQIIN 207
Cdd:cd00311  194 G-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLDIIK 242

GAPDH_I_C

cd18126

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...

367-522

3.66e-102

Pssm-ID: 467676 Cd Length: 165 Bit Score: 303.99 E-value: 3.66e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 367 CTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKkDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGM 446
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 447 SFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNL 155

TpiA

COG0149

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...

1-208

6.91e-102

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis

Pssm-ID: 439919 [Multi-domain] Cd Length: 249 Bit Score: 306.21 E-value: 6.91e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:COG0149   37 EVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYfGETDELVNKKVKAA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:COG0149  117 LAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAE 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:COG0149  197 LYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAeDFLAIVRA 249

G3PDH_Arsen

NF033735

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;

221-512

2.64e-100

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;

Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 305.32 E-value: 2.64e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 221 VAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPANI 300
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 301 KWGEeQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMF--VMGVNHELYEKNMH-VVSNASCTTNCLAPLAK 377
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHrIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 378 VVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVSV 457
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156986379 458 VDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDA 512
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293

TIM

pfam00121

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...

1-208

2.35e-99

Pssm-ID: 459680 Cd Length: 244 Bit Score: 299.81 E-value: 2.35e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379    1 EVVVAPSQVHAATVKASLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYAL 79
Cdd:pfam00121  34 EVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYfGETDEDVAKKVKAAL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   80 EKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWT-NVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKv 158
Cdd:pfam00121 114 KAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL- 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156986379  159 SPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:pfam00121 193 YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLDIINA 243

PRK07403

type I glyceraldehyde-3-phosphate dehydrogenase;

219-521

4.22e-98

type I glyceraldehyde-3-phosphate dehydrogenase;

Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 299.90 E-value: 4.22e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRA--AATNPLINIVAINDPFISTTyMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMN 296
Cdd:PRK07403   2 IRVAINGFGRIGRNFLRCwlGRENSQLELVAINDTSDPRT-NAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAP--SSDAPMFVMGVNHELYEKNMH-VVSNASCTTNCLA 373
Cdd:PRK07403  81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHnIISNASCTTNCLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 374 PLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGpSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTA 453
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 454 DVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDD 521
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGD 307

tpiA

PRK00042

triosephosphate isomerase; Provisional

1-208

9.82e-96

triosephosphate isomerase; Provisional

Pssm-ID: 234589 Cd Length: 250 Bit Score: 290.48 E-value: 9.82e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:PRK00042  36 EVAVAPPFTALASVKEALKgSNIKLGAQNVHPEDSGAFTGEISAEMLKDLGVKYVIIGHSERRQYfGETDELVNKKVKAA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:PRK00042 116 LKAGLTPILCVGETLEEREAGKTEEVVARQLEAalAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAE 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156986379 157 KVSpEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:PRK00042 196 LYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAeDFLAIVKA 247

PLN02561

triosephosphate isomerase

1-210

4.09e-90

triosephosphate isomerase

Pssm-ID: 178175 Cd Length: 253 Bit Score: 276.32 E-value: 4.09e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYAL 79
Cdd:PLN02561  39 EVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISAEMLVNLGIPWVILGHSERRALlGESNEFVGDKVAYAL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  80 EKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKVS 159
Cdd:PLN02561 119 SQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVS 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156986379 160 PEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPDFLQIINAQN 210
Cdd:PLN02561 199 PEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEFIDIIKSAT 249

PRK08955

glyceraldehyde-3-phosphate dehydrogenase; Validated

218-512

1.03e-87

glyceraldehyde-3-phosphate dehydrogenase; Validated

Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 273.14 E-value: 1.03e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 218 AVNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNP 297
Cdd:PRK08955   2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 298 ANIKWGEEQVqyVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMF--VMGVNHELYEKNMH-VVSNASCTTNCLAP 374
Cdd:PRK08955  82 ADTDWSGCDV--VIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHpIVTAASCTTNCLAP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 375 LAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPsKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PRK08955 160 VVKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLAN 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDA 512
Cdd:PRK08955 239 ASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDA 296

PLN03096

glyceraldehyde-3-phosphate dehydrogenase A; Provisional

219-521

1.06e-84

glyceraldehyde-3-phosphate dehydrogenase A; Provisional

Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 267.57 E-value: 1.06e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRA--AATNPLINIVAINDPFiSTTYMEYMLEYDTVHGKFAGSLS-HDEKHIFVNGKPIRVFHEM 295
Cdd:PLN03096  61 IKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 296 NPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSS-DAPMFVMGVNHELYEKNMHVVSNASCTTNCLAP 374
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 375 LAKVVNDKFGIKEGLMTTVHAVTATQKTVDGpSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDD 521
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDD 365

GAPDH_I_N

cd05214

N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...

219-366

3.48e-82

N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, 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.

Pssm-ID: 467614 [Multi-domain] Cd Length: 164 Bit Score: 252.70 E-value: 3.48e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPFIsTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:cd05214    1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156986379 299 NIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSD-APMFVMGVNHELYEKNMHVVSNAS 366
Cdd:cd05214   80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148

PRK13535

erythrose 4-phosphate dehydrogenase; Provisional

219-513

2.58e-79

erythrose 4-phosphate dehydrogenase; Provisional

Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 251.51 E-value: 2.58e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRA---AATNPLINIVAINDpFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEM 295
Cdd:PRK13535   2 IRVAINGFGRIGRNVLRAlyeSGRRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 296 NPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSS---DAPMfVMGVNHELYEKNMHVVSNASCTTNCL 372
Cdd:PRK13535  81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 373 APLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGpSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPT 452
Cdd:PRK13535 160 IPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156986379 453 ADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDAS 513
Cdd:PRK13535 239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGT 299

Gp_dh_C

pfam02800

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...

372-522

3.40e-77

Pssm-ID: 460700 Cd Length: 158 Bit Score: 239.42 E-value: 3.40e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  372 LAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVP 451
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156986379  452 TADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNF 151

PLN02237

glyceraldehyde-3-phosphate dehydrogenase B

196-521

4.20e-76

glyceraldehyde-3-phosphate dehydrogenase B

Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 246.74 E-value: 4.20e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 196 ASLKPDFLQIINAQNPTDNVGGA---------VNVAINGFGRIGRLVLR---AAATNPLiNIVAINDPFiSTTYMEYMLE 263
Cdd:PLN02237  44 NAREASFFDVVASQLAPKVAGSTpvrgetvakLKVAINGFGRIGRNFLRcwhGRKDSPL-DVVVVNDSG-GVKNASHLLK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 264 YDTVHGKFAGSLS-HDEKHIFVNGKPIRVFHEMNPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPS-- 340
Cdd:PLN02237 122 YDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkg 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 341 SDAPMFVMGVNHELYEKNM-HVVSNASCTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGpSKKDWRGGRGACF 419
Cdd:PLN02237 202 ADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAAL 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 420 NIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTADVSVVDLTARLVNPA-SYDEIKAAI*SASENEMKGILGYTEKAVVS 498
Cdd:PLN02237 281 NIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVS 360

                        330       340
                 ....*....|....*....|...
gi 156986379 499 SDFIGDSHSSIFDASAGIALTDD 521
Cdd:PLN02237 361 VDFRCSDVSSTIDASLTMVMGDD 383

PLN02429

triosephosphate isomerase

1-208

1.56e-75

triosephosphate isomerase

Pssm-ID: 166070 Cd Length: 315 Bit Score: 241.23 E-value: 1.56e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYAL 79
Cdd:PLN02429  98 DVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRHViGEKDEFIGKKAAYAL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  80 EKGLGVIACIGETKELREANKTVEYITEQLDAYAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKEKVS 159
Cdd:PLN02429 178 SEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVS 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 156986379 160 PEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLK-PDFLQIINA 208
Cdd:PLN02429 258 EEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFATIVNS 307

Gp_dh_N

smart00846

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...

219-367

1.10e-72

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 [Multi-domain] Cd Length: 149 Bit Score: 227.43 E-value: 1.10e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPfISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   299 NIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDA-PMFVMGVNHELYEKNMHVVSNASC 367
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149

PRK08289

glyceraldehyde-3-phosphate dehydrogenase; Reviewed

220-517

1.50e-68

glyceraldehyde-3-phosphate dehydrogenase; Reviewed

Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 227.88 E-value: 1.50e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 220 NVAINGFGRIGRLVLR-----AAATNPLiNIVAI-------NDpfisttyME---YMLEYDTVHGKFAGSLSHDEKH--I 282
Cdd:PRK08289 129 DVVLYGFGRIGRLLARlliekTGGGNGL-RLRAIvvrkgseGD-------LEkraSLLRRDSVHGPFNGTITVDEENnaI 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 283 FVNGKPIRVFHEMNPANIKWgeeqVQY------VVESTGAFTTTEKASAHLQ-NGVEKVVISAPSS-DAPMFVMGVNHEL 354
Cdd:PRK08289 201 IANGNYIQVIYANSPEEVDY----TAYginnalVVDNTGKWRDEEGLSQHLKsKGVAKVLLTAPGKgDIKNIVHGVNHSD 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 355 YEKNMHVVSNASCTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDwRGGRGACFNIIPSSTGAAKAVG* 434
Cdd:PRK08289 277 ITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAK 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 435 VIPSLNGKLTGMSFRVPTADVSVVDLTARLVNPASYDEIKAAI*SAS-ENEMKGILGYTE-KAVVSSDFIGDSHSSIFDA 512
Cdd:PRK08289 356 ALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDsTEVVSSDFVGSRHAGVVDS 435


                 ....*
gi 156986379 513 SAGIA 517
Cdd:PRK08289 436 QATIV 440

GAPDH_C

cd18123

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...

367-522

1.04e-67

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, 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.

Pssm-ID: 467673 Cd Length: 164 Bit Score: 215.17 E-value: 1.04e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 367 CTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGM 446
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 447 SFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENemKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNE 154

PRK13962

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional

1-208

1.02e-65

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional

Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 224.61 E-value: 1.02e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLR-SDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYA 78
Cdd:PRK13962 431 EVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTGEISGPMLAEIGVEYVIIGHSERRQYfGETDELVNKKVLAA 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  79 LEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAWLKE 156
Cdd:PRK13962 511 LKAGLTPILCVGETLDERESGITFDVVRLQLKAalNGLSAEQVKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAE 590

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156986379 157 KVSPEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKP-DFLQIINA 208
Cdd:PRK13962 591 LYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAqEFAAIANY 643

PTZ00353

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional

219-520

9.76e-52

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional

Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 179.69 E-value: 9.76e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDPFISTTYMEYMLEYDTVHGKFAG-SLSHDEKHIFVNG-KPIRVFHEMN 296
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAKHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 297 PANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSSDAPMFVMGVNHELYEKNMHVVSNASCTTNCLAPLA 376
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 377 KVVNDKFGIKEGLMTTVHAvTATQKTVDGPSK--KDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGMSFRVPTAD 454
Cdd:PTZ00353 163 RALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 455 VSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDShSSIFDASAGIALTD 520
Cdd:PTZ00353 242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSRE 306

Gp_dh_N

pfam00044

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...

219-319

8.06e-49

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: 459648 [Multi-domain] Cd Length: 101 Bit Score: 163.43 E-value: 8.06e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDpFISTTYMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEMNPA 298
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79

                          90       100
                  ....*....|....*....|.
gi 156986379  299 NIKWGEEQVQYVVESTGAFTT 319
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFTT 100

tim

TIGR00419

triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...

1-201

1.21e-47

Pssm-ID: 129513 [Multi-domain] Cd Length: 205 Bit Score: 164.21 E-value: 1.21e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379    1 EVVVAPSQVHAATVKASLRsdVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREKGETnevVAKKAAYALE 80
Cdd:TIGR00419  34 AVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERRMKLAD---IEKKIARLKE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   81 KGLGVIACIgetkelreanktvEYITEQLDAYAaeikdWTNVVIAYEPIWAIGTGLTASPEQAQEVHASIRAwlkekvSP 160
Cdd:TIGR00419 109 LGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAVEPPELIGTGIPVSPAQPEVVHGSVRA------VK 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 156986379  161 EAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPD 201
Cdd:TIGR00419 165 EVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205

GAPDH_N_E4PDH

cd17892

N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...

219-366

8.82e-43

N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; E4PDH (EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, 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 (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH family of proteins.

Pssm-ID: 467615 [Multi-domain] Cd Length: 169 Bit Score: 150.11 E-value: 8.82e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPL---INIVAINDPFISTTyMEYMLEYDTVHGKFAGSLSHDEKHIFVNGKPIRVFHEM 295
Cdd:cd17892    1 YRVAINGYGRIGRNVLRALYESGRraeFQVVAINELADAET-IAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156986379 296 NPANIKWGEEQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSS---DAPMfVMGVNHELYEKNMHVVSNAS 366
Cdd:cd17892   80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152

GAPDH_C_E4PDH

cd23937

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...

367-513

2.19e-38

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, 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 (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.

Pssm-ID: 467686 Cd Length: 165 Bit Score: 137.93 E-value: 2.19e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 367 CTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGpSKKDWRGGRGACFNIIPSSTGAAKAVG*VIPSLNGKLTGM 446
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379 447 SFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDAS 513
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGT 146

PRK14565

triosephosphate isomerase; Provisional

17-206

7.84e-37

triosephosphate isomerase; Provisional

Pssm-ID: 237758 Cd Length: 237 Bit Score: 136.43 E-value: 7.84e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  17 SLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKKAAYALEKGLGVIACIGETKEL 95
Cdd:PRK14565  52 ECNPNIKLGAQNCFYGSSGGYTGEISAKMLKECGCSYVILGHSERRSTfHETDSDIRLKAESAIESGLIPIICVGETLED 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  96 REANKTVEYITEQLDAYAAEIKDWTnvvIAYEPIWAIGTGLTASPEQAQEVHASIRAWlkekvspeaAEKTRVIYGGSVG 175
Cdd:PRK14565 132 RENGMTKDVLLEQCSNCLPKHGEFI---IAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVN 199

                        170       180       190
                 ....*....|....*....|....*....|..
gi 156986379 176 AKNAPELSQKEDIDGFLVGGASLKPD-FLQII 206
Cdd:PRK14565 200 QENIRDLKSINQLSGVLVGSASLDVDsFCKII 231

GAPDH_like_C

cd18122

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...

367-522

3.52e-36

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.

Pssm-ID: 467672 [Multi-domain] Cd Length: 166 Bit Score: 132.26 E-value: 3.52e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 367 CTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWrgGRGACFNIIPSSTGAAKAVG*VIPSLN--GKLT 444
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156986379 445 GMSFRVPTADVSVVDLTARLVNPASYDEIKAAI*SASENEMKGILGYTEKAVVSSDFIGDSHSSIFDASAGIALTDDF 522
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNK 156

PRK14905

triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...

1-194

8.74e-34

triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional

Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 131.31 E-value: 8.74e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPS------QVHAATVKASlRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERRE-KGETNEVVAK 73
Cdd:PRK14905  41 ELFVIPSyialkdAVEAAASETG-HPKIKIGAQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHvLKETDQEENE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  74 KAAYALEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGT-GLTASPEQAQEVHASI 150
Cdd:PRK14905 120 KVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIglHGVSAEQLPHLFIAYEPVWAIGEgGIPASAEYADEKHAII 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 156986379 151 RAWLKEKVSpEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVG 194
Cdd:PRK14905 200 KQCLFELFA-EESKKIPVLYGGSVNLENANELIMKPHIDGLFIG 242

PRK15492

triosephosphate isomerase; Provisional

1-206

2.29e-32

triosephosphate isomerase; Provisional

Pssm-ID: 185389 Cd Length: 260 Bit Score: 124.72 E-value: 2.29e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPS-----QVHAATVKASLRSDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREK-GETNEVVAKK 74
Cdd:PRK15492  40 ELFVIPSftaiqDAIAATLAIPHDHPIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKfGETDQEENAK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379  75 AAYALEKGLGVIACIGETKELREANKTVEYITEQLDA--YAAEIKDWTNVVIAYEPIWAIGT-GLTASPEQAQEVHASIR 151
Cdd:PRK15492 120 VLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIglHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIK 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156986379 152 AWLKEKVSpEAAEKTRVIYGGSVGAKNAPELSQKEDIDGFLVGGASLKPD-FLQII 206
Cdd:PRK15492 200 QCLIELFG-DAGDDIPVFYGGSVNAENANELFGQPHIDGLFIGRSAWDADkFFAII 254

GAPDH-like_N

cd05192

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...

219-371

9.20e-10

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.

Pssm-ID: 467613 [Multi-domain] Cd Length: 109 Bit Score: 56.21 E-value: 9.20e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379 219 VNVAINGFGRIGRLVLRAAATNPLINIVAINDpfisttymeymleydtvhgkfagslshdekhifvngkpirvfhemnpa 298
Cdd:cd05192    1 IRVAINGFGRIGRIVFRAIADQDDLDVVAIND------------------------------------------------ 32

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156986379 299 nikwgeeQVQYVVESTGAFTTTEKASAHLQNGVEKVVISAPSS-DAPMFVMGVNHELYEKNMHVVSNASCTTNC 371
Cdd:cd05192   33 -------RRDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGATVVSNANETSYS 99

PRK04302

triosephosphate isomerase; Provisional

1-141

2.34e-06

triosephosphate isomerase; Provisional

Pssm-ID: 235274 Cd Length: 223 Bit Score: 48.71 E-value: 2.34e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156986379   1 EVVVAPSQVHAATVKASLrsDVRVSGQDVWKQGNGAFTGETSAEMLKDLGAEYTLVGHSERREKGETNEVVAKKAAyalE 80
Cdd:PRK04302  38 RIAVAPQALDIRRVAEEV--DIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVERAK---K 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156986379  81 KGLGVIAC---IGETKelreanktveyiteqldAYAAEIKDWtnvvIAYEPIWAIGTGL---TASPE 141
Cdd:PRK04302 113 LGLESVVCvnnPETSA-----------------AAAALGPDY----VAVEPPELIGTGIpvsKAKPE 158

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