|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-337 |
0e+00 |
|
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: 650.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRY 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLER-GPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDnEKHNIISNASCTTNCL 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTP 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 241 TVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 489518926 321 GYSSRTVDLVKYVAEKL 337
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 551.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAKdEDTLVVNSKEIKILRY 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKE--SAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAF-EDHLLVDGKKIRLLNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHNIISNASCTTNCL 160
Cdd:PRK07729 78 RDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKHTIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTP 240
Cdd:PRK07729 158 APVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 241 TVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEW 320
Cdd:PRK07729 238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317
|
330
....*....|....*...
gi 489518926 321 GYSSRTVDLVKYVAEKLK 338
Cdd:PRK07729 318 GYSCRVVDLVTLVADELA 335
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
0e+00 |
|
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: 506.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 4 KVGMNGFGRIGRAVLRIAQEELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRY-ND 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEVISVFSeRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEkHNIISNASCTTNCLAP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGE-ERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 163 FAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPTV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 243 SLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMV--IEDNMVKVVSWYDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318
|
....*...
gi 489518926 321 GYSSRTVD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-330 |
9.42e-152 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 429.35 E-value: 9.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 5 VGMNGFGRIGRAVLRIAQEelGDNIEIVAINARAT-TESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYNDP 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWG--RPGLEIVHINDLAGdAATLAHLLEFDSVHGRWDAEVTA-EEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 84 EELPWKElGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDI-TIVIGVNEEEYDNEKHNIISNASCTTNCLAP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVlNIVYGVNDHLYDPARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 163 FAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPTV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 243 SLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEWGY 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*...
gi 489518926 323 SSRTVDLV 330
Cdd:NF033735 317 ANRMVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
5.56e-116 |
|
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: 332.50 E-value: 5.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 155 CTTNCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFS 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 235 LRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVS 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 489518926 315 WYDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
3.68e-88 |
|
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: 261.37 E-value: 3.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 160 LAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489518926 239 TPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
2.56e-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 [Multi-domain] Cd Length: 149 Bit Score: 233.60 E-value: 2.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYND 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALER--PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHnIISNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDH-IISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-337 |
0e+00 |
|
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: 650.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRY 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLER-GPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDnEKHNIISNASCTTNCL 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTP 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 241 TVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 489518926 321 GYSSRTVDLVKYVAEKL 337
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 551.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAKdEDTLVVNSKEIKILRY 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKE--SAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAF-EDHLLVDGKKIRLLNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHNIISNASCTTNCL 160
Cdd:PRK07729 78 RDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKHTIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTP 240
Cdd:PRK07729 158 APVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 241 TVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEW 320
Cdd:PRK07729 238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317
|
330
....*....|....*...
gi 489518926 321 GYSSRTVDLVKYVAEKLK 338
Cdd:PRK07729 318 GYSCRVVDLVTLVADELA 335
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
0e+00 |
|
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: 506.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 4 KVGMNGFGRIGRAVLRIAQEELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRY-ND 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEVISVFSeRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEkHNIISNASCTTNCLAP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGE-ERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 163 FAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPTV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 243 SLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMV--IEDNMVKVVSWYDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318
|
....*...
gi 489518926 321 GYSSRTVD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
3-338 |
5.16e-162 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 455.91 E-value: 5.16e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYND 82
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISA-DENSITVNGKTIKCVSDRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDI-TIVIGVNEEEYDNEKHNIISNASCTTNCLA 161
Cdd:PRK07403 81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgTYVVGVNHHEYDHEDHNIISNASCTTNCLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 162 PFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPT 241
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 242 VSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEWG 321
Cdd:PRK07403 241 VSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWG 320
|
330
....*....|....*..
gi 489518926 322 YSSRTVDLVKYVAEKLK 338
Cdd:PRK07403 321 YSQRVVDLAELVARKWK 337
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-337 |
4.69e-160 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 454.74 E-value: 4.69e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 2 KIKVGMNGFGRIGRAVLRIAQEELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAKDEDTLVVNSKEIKILRYN 81
Cdd:PLN02237 75 KLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 82 DPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDI-TIVIGVNEEEYDNEKHNIISNASCTTNCL 160
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIpTYVVGVNEDDYDHEVANIVSNASCTTNCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTP 240
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 241 TVSLVDLVCEL-KENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNE 319
Cdd:PLN02237 315 NVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
|
330
....*....|....*...
gi 489518926 320 WGYSSRTVDLVKYVAEKL 337
Cdd:PLN02237 395 WGYSQRVVDLAHLVAAKW 412
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-338 |
2.26e-156 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 443.60 E-value: 2.26e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 2 KIKVGMNGFGRIGRAVLRIAQEELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAKDEDTLVVNSKEIKILRYN 81
Cdd:PLN03096 60 KIKVAINGFGRIGRNFLRCWHGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDAISVDGKVIKVVSDR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 82 DPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKhNIISNASCTTNCLA 161
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSD-PIISNASCTTNCLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 162 PFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPT 241
Cdd:PLN03096 219 PFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 242 VSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEWG 321
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378
|
330
....*....|....*..
gi 489518926 322 YSSRTVDLVKYVAEKLK 338
Cdd:PLN03096 379 YSQRVVDLADIVANKWK 395
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-330 |
9.42e-152 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 429.35 E-value: 9.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 5 VGMNGFGRIGRAVLRIAQEelGDNIEIVAINARAT-TESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYNDP 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWG--RPGLEIVHINDLAGdAATLAHLLEFDSVHGRWDAEVTA-EEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 84 EELPWKElGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDI-TIVIGVNEEEYDNEKHNIISNASCTTNCLAP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVlNIVYGVNDHLYDPARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 163 FAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPTPTV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 243 SLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNEWGY 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*...
gi 489518926 323 SSRTVDLV 330
Cdd:NF033735 317 ANRMVDLA 324
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-334 |
1.98e-145 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 416.95 E-value: 1.98e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 2 KIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAIN-ARATTESLAHLFTYDSCYGTFRGEVEAKDEDTLVVNSKEIKILRY 80
Cdd:PLN02272 85 KTKIGINGFGRIGRLVLRIATSR--DDIEVVAVNdPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDItIVIGVNEEEYDnEKHNIISNASCTTNCL 160
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPM-FVVGVNEKTYK-PNMNIVSNASCTTNCL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPT 239
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDgPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 240 PTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNE 319
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400
|
330
....*....|....*
gi 489518926 320 WGYSSRTVDLVKYVA 334
Cdd:PLN02272 401 WGYSNRVLDLIEHMA 415
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-333 |
1.04e-141 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 404.11 E-value: 1.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEelGDNIEIVAINARA-TTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILR 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWD--WPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTA-EGDAIVINGKRIRTTQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 80 YNDPEELPWKelGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDI-TIVIGVNEEEYDNEKHNIISNASCTTN 158
Cdd:PRK08955 78 NKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVlNIVMGVNDHLFDPAIHPIVTAASCTTN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 159 CLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVP 238
Cdd:PRK08955 156 CLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 239 TPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDN 318
Cdd:PRK08955 236 LANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDN 315
|
330
....*....|....*
gi 489518926 319 EWGYSSRTVDLVKYV 333
Cdd:PRK08955 316 EWGYANRTAELARKV 330
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-328 |
6.41e-128 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 369.39 E-value: 6.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRiAQEELG--DNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEaKDEDTLVVNSKEIKILRY 80
Cdd:PRK13535 2 IRVAINGFGRIGRNVLR-ALYESGrrAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVR-QERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNE-DITIVIGVNEEEYDNEkHNIISNASCTTNC 159
Cdd:PRK13535 80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDlDATVVYGVNHDQLRAE-HRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 160 LAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPT 239
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 240 PTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNE 319
Cdd:PRK13535 239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318
|
....*....
gi 489518926 320 WGYSSRTVD 328
Cdd:PRK13535 319 WGFANRMLD 327
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-336 |
5.03e-127 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 366.85 E-value: 5.03e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAIN-ARATTESLAHLFTYDSCYGTFRGEVEAKDeDTLVVNSKEIKILR 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALER--EDVEVVAINdPFMTLDYMCYLLKYDSVHGSLPAEVSVTD-GFLMIGSKKVHVFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 80 YNDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDnEKHNIISNASCTTNC 159
Cdd:PTZ00023 78 EKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYD-KSQRIVSNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 160 LAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILD---KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLR 236
Cdd:PTZ00023 157 LAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDgpsKGGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 237 VPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWY 316
Cdd:PTZ00023 237 VPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWY 316
|
330 340
....*....|....*....|
gi 489518926 317 DNEWGYSSRTVDLVKYVAEK 336
Cdd:PTZ00023 317 DNEWGYSNRLLDLAHYITQK 336
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-336 |
5.57e-125 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 362.84 E-value: 5.57e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEE--LGDNIEIVAINARAT-TESLAHLFTYDSCYGTFRGEVEA-------KDEDTLVV 70
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQglIGTEIDVVAVVDMSTnAEYFAYQMKYDTVHGRPKYTVETtksspsvKTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 71 NSKEIKILRYN-DPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHNI 149
Cdd:PTZ00434 82 NGHRIKCVKAQrNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEHHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 150 ISNASCTTNCLAPFAKVL-DEKFGIVKGLMTTVHSYTNDQRILDK-SHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLE 227
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGvSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 228 GKLNGFSLRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVI-- 305
Cdd:PTZ00434 242 GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNnl 321
|
330 340 350
....*....|....*....|....*....|...
gi 489518926 306 --EDNMVKVVSWYDNEWGYSSRTVDLVKYVAEK 336
Cdd:PTZ00434 322 pgERRFFKIVSWYDNEWGYSHRVVDLVRYMAAK 354
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
2-335 |
1.46e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 343.24 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 2 KIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAIN-ARATTESLAHLFTYDSCYGTFR-GEVEAKDEDTLVVNSKEIKILR 79
Cdd:PLN02358 5 KIRIGINGFGRIGRLVARVVLQR--DDVELVAVNdPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKPVTVFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 80 YNDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDItIVIGVNEEEYDNEKhNIISNASCTTNC 159
Cdd:PLN02358 83 IRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM-FVVGVNEHEYKSDL-DIVSNASCTTNC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 160 LAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVP 238
Cdd:PLN02358 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDgPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 239 TPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDN 318
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*..
gi 489518926 319 EWGYSSRTVDLVKYVAE 335
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSK 337
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-335 |
3.21e-116 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 339.40 E-value: 3.21e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAKDeDTLVVNSKEIKILRY 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKR--SDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKD-GHLIVNGKKIRVTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 81 NDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEkhNIISNASCTTNCL 160
Cdd:PRK15425 78 RDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQ--DIVSNASCTTNCL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 161 APFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVPT 239
Cdd:PRK15425 156 APLAKVINDNFGIIEGLMTTVHATTATQKTVDgPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 240 PTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWYDNE 319
Cdd:PRK15425 236 PNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNE 315
|
330
....*....|....*.
gi 489518926 320 WGYSSRTVDLVKYVAE 335
Cdd:PRK15425 316 TGYSNKVLDLIAHISK 331
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
5.56e-116 |
|
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: 332.50 E-value: 5.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 155 CTTNCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFS 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 235 LRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVS 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 489518926 315 WYDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-334 |
7.19e-97 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 294.91 E-value: 7.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 9 GFGRIGRAVLR--IAQEELGDNIEIVAINARATTES----LAHLFTYDSCYGTFRGEVEA-KDEDTLVVNSKEIKILRYN 81
Cdd:PRK08289 134 GFGRIGRLLARllIEKTGGGNGLRLRAIVVRKGSEGdlekRASLLRRDSVHGPFNGTITVdEENNAIIANGNYIQVIYAN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 82 DPEELPWKELGVD--IVIESTGLFTQREKAEKHIKA-GAKKVIITAPGKNEDITIVIGVNEEEYDNEkHNIISNASCTTN 158
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDE-DKIVSAASCTTN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 159 CLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVP 238
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 239 TPTVSLVDLVCELKENVTSEQVNSVLKDAA-EGELKGVLGYCDKP-LVSIDYKGDSRSSIIDALSTMVIEDNMVKVVsWY 316
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAVLYV-WY 451
|
330
....*....|....*...
gi 489518926 317 DNEWGYSSRTVDLVKYVA 334
Cdd:PRK08289 452 DNEFGYSCQVVRVMEQMA 469
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
3.68e-88 |
|
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: 261.37 E-value: 3.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 160 LAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSLRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489518926 239 TPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-154 |
7.09e-84 |
|
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: 250.77 E-value: 7.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYND 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALER--DDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEV-DDDALIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDnEKHNIISNAS 154
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYD-ADDKIISNAS 148
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
2.56e-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 [Multi-domain] Cd Length: 149 Bit Score: 233.60 E-value: 2.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYND 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALER--PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489518926 83 PEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHnIISNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDH-IISNASC 149
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
155-319 |
3.56e-65 |
|
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: 203.03 E-value: 3.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 155 CTTNCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFS 234
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 235 LRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVVS 314
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 489518926 315 WYDNE 319
Cdd:cd23937 161 WCDNE 165
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
155-319 |
2.27e-58 |
|
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: 185.90 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 155 CTTNCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILD-KSHKDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGF 233
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDgPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 234 SLRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGelKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKVV 313
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 489518926 314 SWYDNE 319
Cdd:cd18123 159 QWYDNE 164
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-154 |
4.47e-56 |
|
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: 180.16 E-value: 4.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQE-ELGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYN 81
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRV-ENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489518926 82 DPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNE-DITIVIGVNEEEYDNEkHNIISNAS 154
Cdd:cd17892 80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDvDATIVYGINQDLLRAE-HRIVSNAS 152
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-104 |
2.87e-47 |
|
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: 154.95 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEelGDNIEIVAINARATTESLAHLFTYDSCYGTFRGEVEAkDEDTLVVNSKEIKILRYND 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALE--RPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEA-EEDGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|..
gi 489518926 83 PEELPWKELGVDIVIESTGLFT 104
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFT 99
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-333 |
2.30e-46 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 160.43 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 1 MKIKVGMNGFGRIGRAVLRIAQEElgDNIEIVAIN-ARATTESLAHLFTYDSCYGT-FRGEVEAKDEDTLVVNSKEIKIL 78
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTD--PLVTVVAVNdASVSIAYIAYVLEQESPLSApDGASIRVVGEQIVLNGTQKIRVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 79 RYNDPEELPWKELGVDIVIESTGLFTQREKAEKHIKAGAKKVIITapGKNEDI-TIVIGVNEEEYdNEKHNIISNASCTT 157
Cdd:PTZ00353 79 AKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVA--GQSADApTVMAGSNDERL-SASLPVCCAGAPIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 158 NCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSH--KDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLNGFSL 235
Cdd:PTZ00353 156 VALAPVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 236 RVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSsIIDALSTMVIEDNMV-KVVS 314
Cdd:PTZ00353 236 QVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGKL-CYDATSSSSSREGEVhKMVL 314
|
330
....*....|....*....
gi 489518926 315 WYDNEWGYSSRTVDLVKYV 333
Cdd:PTZ00353 315 WFDVECYYAARLLSLVKQL 333
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
155-319 |
2.20e-32 |
|
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: 118.39 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 155 CTTNCLAPFAKVLDEKFGIVKGLMTTVHSYTNDQRILDKSHkDLRRARAAAESIIPTTTGAAKAVSRVLPQLEGKLN--G 232
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKPIKvdG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 233 FSLRVPTPTVSLVDLVCELKENVTSEQVNSVLKDAAEGELKGVLGYCDKPLVSIDYKGDSRSSIIDALSTMVIEDNMVKV 312
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 489518926 313 VSWYDNE 319
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-159 |
1.69e-16 |
|
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: 74.31 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGFGRIGRAVLRIAQEElgDNIEIVAINARAtteslahlftydscygtfrgeveakdedtlvvnskeikilrynd 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQ--DDLDVVAINDRR-------------------------------------------- 34
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489518926 83 peelpwkelgvDIVIESTGLFTQREKAEKHIKAGAKKVIITAPGKNEDITIVIGVNEEEYDNEKHnIISNASCTTNC 159
Cdd:cd05192 35 -----------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGAT-VVSNANETSYS 99
|
|
| PRK14874 |
PRK14874 |
aspartate-semialdehyde dehydrogenase; Provisional |
76-175 |
1.23e-05 |
|
aspartate-semialdehyde dehydrogenase; Provisional
Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 46.31 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 76 KILRYNDpEELPWKEL------GVDIVIESTGLFTQREKAEKHIKAGAkkVII---TAPGKNEDIT-IVIGVNEEEYDN- 144
Cdd:PRK14874 42 KELSFKG-KELKVEDLttfdfsGVDIALFSAGGSVSKKYAPKAAAAGA--VVIdnsSAFRMDPDVPlVVPEVNPEALAEh 118
|
90 100 110
....*....|....*....|....*....|.
gi 489518926 145 EKHNIISNASCTTNCLAPFAKVLDEKFGIVK 175
Cdd:PRK14874 119 RKKGIIANPNCSTIQMVVALKPLHDAAGIKR 149
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
67-173 |
1.55e-04 |
|
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 43.10 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 67 TLVVNSKEIKILrynDPEELPWKelGVDIVIESTGLFTQREKAEKHIKAGAkkVIITAPG---KNEDITIVI-GVNEEEY 142
Cdd:COG0136 42 TVSFGGKELTVE---DATDFDFS--GVDIALFSAGGSVSKEYAPKAAAAGA--VVIDNSSafrMDPDVPLVVpEVNPEAL 114
|
90 100 110
....*....|....*....|....*....|..
gi 489518926 143 DN-EKHNIISNASCTTNCLAPFAKVLDEKFGI 173
Cdd:COG0136 115 ADhLPKGIIANPNCSTIQMLVALKPLHDAAGI 146
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
3-143 |
8.24e-03 |
|
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.
Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 36.00 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518926 3 IKVGMNGF-GRIGRAVLRIAQEElgDNIEIVAINARATTESLahlftydscyGTFRGEVEAKDEDTLVVNSKEIKIlryn 81
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEA--PDLELVGAVDRPGSGLL----------GGDAGGLAGIGTGVIVSLDLELAA---- 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489518926 82 dpeelpwkeLGVDIVIEstglFTQREKAEKHIKAGAKKviitapGKNeditIVIGV---NEEEYD 143
Cdd:cd02274 65 ---------ADADVVID----FTTPEATLENLEAAAKA------GVP----LVIGTtgfSEEQLA 106
|
|
| |
