|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
3-482 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 804.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 3 FNKVYEKELSFQADRRKATVEFINIVSDLWYDKSIELVLFRNQMINRNVSDILDLHEYAGEFVGKPISIFDSVEIAKAIQ 82
Cdd:PRK08289 1 MTMSPEKHLQDWQEREELAEAMIPLIGKLYRNKNVVVSLYGRSLINRSVIDILKAHRFARRIVGKELSVRETFPILEALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 83 DLNLPPAKLDIGKLTYEYHLDGQpHSNAMAFVSNKLSDAKETEA-VTPKDVILYGFGRIGRLVARELMTRTGKGNQLRLR 161
Cdd:PRK08289 81 KLDLGPARVDIGKLAVKYKAEGD-GSDVEAFVAEELADAVGGADdIEPRDVVLYGFGRIGRLLARLLIEKTGGGNGLRLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 162 AVVTRGKVDQSvLEKRASLLKSDSVHGPFSGTVTIDEKNSALIINGTTVHMISANQPEDIDYTKYGINNALVIDNTGAFR 241
Cdd:PRK08289 160 AIVVRKGSEGD-LEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQVIYANSPEEVDYTAYGINNALVVDNTGKWR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 242 DKEALSRHLSSKGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFSAASCTTNAITPVLKAVQDSLGVVHGHLETIHA 320
Cdd:PRK08289 239 DEEGLSQHLKSKGVAKVLLTAPGKGdIKNIVHGVNHSDITDED-KIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 321 YTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIRVPVPNGSLAILNLEVEKETSLEDVNTL 400
Cdd:PRK08289 318 YTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 401 LKKYALEGELVEQIQYSIDNELVSSDIIGSSAPAIYDSNATIVsaDGKNVILYIWYDNEYGYSHQVIRLAKYIAKVRRYT 480
Cdd:PRK08289 398 LRQMSLHSPLQNQIDYTDSTEVVSSDFVGSRHAGVVDSQATIV--NGNRAVLYVWYDNEFGYSCQVVRVMEQMAGVRYPT 475
|
..
gi 500027819 481 YY 482
Cdd:PRK08289 476 YP 477
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
130-476 |
3.27e-167 |
|
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: 474.50 E-value: 3.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 130 KDVILYGFGRIGRLVARELMTRtgkGNQLRLRAVVTRGKvdqsvLEKRASLLKSDSVHGPFSGTVTIDEknSALIINGTT 209
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLER---GPDIEVVAINDLGD-----AETLAHLLKYDSVHGRFPGEVEVEG--DSLIVNGKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 210 VHMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFS 288
Cdd:COG0057 73 IKVLAERDPAELPWGELGVD--VVIECTGKFTDREKASAHLKA-GAKKVLISAPAKGdDPTIVYGVNHDDYDADH-RIIS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 289 AASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLT 368
Cdd:COG0057 149 NASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 369 SNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGK 448
Cdd:COG0057 229 GMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGYT-EEPLVSSDFNGDPHSSIFDALQTIVI-GGN 305
|
330 340
....*....|....*....|....*...
gi 500027819 449 NVILYIWYDNEYGYSHQVIRLAKYIAKV 476
Cdd:COG0057 306 LVKVLAWYDNEWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
131-468 |
6.76e-139 |
|
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: 402.43 E-value: 6.76e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 131 DVILYGFGRIGRLVARELMTRtgkgNQLRLRAVVTRGKVDqsvLEKRASLLKSDSVHGPFSGTVTIDEKnsALIINGT-T 209
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK----PGNDLEVVAINDLTD---LEKLAYLLKYDSVHGRFEGEVTVDED--GLVVNGKeV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 210 VHMISANQPEDIDYTKYGInnALVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFS 288
Cdd:TIGR01534 72 ISVFSERDPSDLPWKALGV--DIVIECTGKFRDKEKLEKHLEA-GAKKVLISAPSKGdVKTIVYGVNHDEYDGEE-RIIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 289 AASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLT 368
Cdd:TIGR01534 148 NASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 369 SNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADG- 447
Cdd:TIGR01534 228 GMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEAS-EGELKGVLGYT-EDELVSSDFIGSPYSSIVDATATKVTGLGd 305
|
330 340
....*....|....*....|.
gi 500027819 448 KNVILYIWYDNEYGYSHQVIR 468
Cdd:TIGR01534 306 SLVKVYAWYDNEWGYSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
136-470 |
2.01e-80 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 252.55 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRTGkgnqlrLRAV-VTRGKVDQSVLekrASLLKSDSVHGPFSGTVTIDEknSALIINGTTVHMIS 214
Cdd:NF033735 5 GFGRIGRLALRALWGRPG------LEIVhINDLAGDAATL---AHLLEFDSVHGRWDAEVTAEE--DSIVIDGKRISFSS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 215 ANQPEDIDYtkyGINNALVIDNTGAFRDKEALSRHLSsKGAAKVLLTAPGK--GVPNIVHGVNQKEHNPDEIDIFSAASC 292
Cdd:NF033735 74 NKDIEDTPW---GDGVDVVIECTGKFKTPEKLQPYFD-QGVKKVVVSAPVKeeGVLNIVYGVNDHLYDPARHRIVTAASC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 293 TTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAI 372
Cdd:NF033735 150 TTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 373 RVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVsADGKNVIL 452
Cdd:NF033735 230 RVPLLNASLTDCVFEVERPTTVEEVNALFKA-AAEGPLKGILGYE-ERPLVSVDYVNDPRSSIIDALSTMV-VNGTQVKI 306
|
330
....*....|....*...
gi 500027819 453 YIWYDNEYGYSHQVIRLA 470
Cdd:NF033735 307 YAWYDNEWGYANRMVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
292-459 |
8.98e-75 |
|
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: 232.35 E-value: 8.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 292 CTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNA 371
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 372 IRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSIDnELVSSDIIGSSAPAIYDSNATIVsADGKNVI 451
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAA-EGPLKGILGYTED-PLVSSDFVGDPHSSIFDATATIV-LGGNLVK 157
|
....*...
gi 500027819 452 LYIWYDNE 459
Cdd:cd18126 158 VVAWYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
297-456 |
1.16e-48 |
|
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: 164.30 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 297 ITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIRVP 375
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKdLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 376 VPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGKNVILYIW 455
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAA-EGALKGILSYT-EDPLVSSDFIGDPHSSIFDAKETIVV-NGNFVKVVAW 157
|
.
gi 500027819 456 Y 456
Cdd:pfam02800 158 Y 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
131-292 |
1.53e-42 |
|
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: 147.70 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 131 DVILYGFGRIGRLVARELMTRtgkgNQLRLRAVvtrgkVDQSVLEKRASLLKSDSVHGPFSGTVTIDEKNsaLIINGTTV 210
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALER----PDVEVVAI-----NDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDG--LVVNGKAI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 211 HMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGV-PNIVHGVNQKEHNPDEiDIFSA 289
Cdd:smart00846 71 KVFAERDPANLPWGELGVD--IVVECTGGFTTREKASAHLKA-GAKKVIISAPSKDAdPTFVYGVNHDEYDGED-HIISN 146
|
...
gi 500027819 290 ASC 292
Cdd:smart00846 147 ASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
3-482 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 804.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 3 FNKVYEKELSFQADRRKATVEFINIVSDLWYDKSIELVLFRNQMINRNVSDILDLHEYAGEFVGKPISIFDSVEIAKAIQ 82
Cdd:PRK08289 1 MTMSPEKHLQDWQEREELAEAMIPLIGKLYRNKNVVVSLYGRSLINRSVIDILKAHRFARRIVGKELSVRETFPILEALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 83 DLNLPPAKLDIGKLTYEYHLDGQpHSNAMAFVSNKLSDAKETEA-VTPKDVILYGFGRIGRLVARELMTRTGKGNQLRLR 161
Cdd:PRK08289 81 KLDLGPARVDIGKLAVKYKAEGD-GSDVEAFVAEELADAVGGADdIEPRDVVLYGFGRIGRLLARLLIEKTGGGNGLRLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 162 AVVTRGKVDQSvLEKRASLLKSDSVHGPFSGTVTIDEKNSALIINGTTVHMISANQPEDIDYTKYGINNALVIDNTGAFR 241
Cdd:PRK08289 160 AIVVRKGSEGD-LEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQVIYANSPEEVDYTAYGINNALVVDNTGKWR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 242 DKEALSRHLSSKGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFSAASCTTNAITPVLKAVQDSLGVVHGHLETIHA 320
Cdd:PRK08289 239 DEEGLSQHLKSKGVAKVLLTAPGKGdIKNIVHGVNHSDITDED-KIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 321 YTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIRVPVPNGSLAILNLEVEKETSLEDVNTL 400
Cdd:PRK08289 318 YTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 401 LKKYALEGELVEQIQYSIDNELVSSDIIGSSAPAIYDSNATIVsaDGKNVILYIWYDNEYGYSHQVIRLAKYIAKVRRYT 480
Cdd:PRK08289 398 LRQMSLHSPLQNQIDYTDSTEVVSSDFVGSRHAGVVDSQATIV--NGNRAVLYVWYDNEFGYSCQVVRVMEQMAGVRYPT 475
|
..
gi 500027819 481 YY 482
Cdd:PRK08289 476 YP 477
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
130-476 |
3.27e-167 |
|
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: 474.50 E-value: 3.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 130 KDVILYGFGRIGRLVARELMTRtgkGNQLRLRAVVTRGKvdqsvLEKRASLLKSDSVHGPFSGTVTIDEknSALIINGTT 209
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLER---GPDIEVVAINDLGD-----AETLAHLLKYDSVHGRFPGEVEVEG--DSLIVNGKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 210 VHMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFS 288
Cdd:COG0057 73 IKVLAERDPAELPWGELGVD--VVIECTGKFTDREKASAHLKA-GAKKVLISAPAKGdDPTIVYGVNHDDYDADH-RIIS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 289 AASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLT 368
Cdd:COG0057 149 NASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 369 SNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGK 448
Cdd:COG0057 229 GMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGYT-EEPLVSSDFNGDPHSSIFDALQTIVI-GGN 305
|
330 340
....*....|....*....|....*...
gi 500027819 449 NVILYIWYDNEYGYSHQVIRLAKYIAKV 476
Cdd:COG0057 306 LVKVLAWYDNEWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
131-468 |
6.76e-139 |
|
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: 402.43 E-value: 6.76e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 131 DVILYGFGRIGRLVARELMTRtgkgNQLRLRAVVTRGKVDqsvLEKRASLLKSDSVHGPFSGTVTIDEKnsALIINGT-T 209
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK----PGNDLEVVAINDLTD---LEKLAYLLKYDSVHGRFEGEVTVDED--GLVVNGKeV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 210 VHMISANQPEDIDYTKYGInnALVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFS 288
Cdd:TIGR01534 72 ISVFSERDPSDLPWKALGV--DIVIECTGKFRDKEKLEKHLEA-GAKKVLISAPSKGdVKTIVYGVNHDEYDGEE-RIIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 289 AASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLT 368
Cdd:TIGR01534 148 NASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 369 SNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADG- 447
Cdd:TIGR01534 228 GMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEAS-EGELKGVLGYT-EDELVSSDFIGSPYSSIVDATATKVTGLGd 305
|
330 340
....*....|....*....|.
gi 500027819 448 KNVILYIWYDNEYGYSHQVIR 468
Cdd:TIGR01534 306 SLVKVYAWYDNEWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
132-475 |
2.47e-88 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 273.92 E-value: 2.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 132 VILYGFGRIGRLVARELMtrtgKGNQLRLRAVVTRGKVdqsvlEKRASLLKSDSVHGPFSGTVTIdeKNSALIINGTTVH 211
Cdd:PRK07729 5 VAINGFGRIGRMVFRKAI----KESAFEIVAINASYPS-----ETLAHLIKYDTVHGKFDGTVEA--FEDHLLVDGKKIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 212 MISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGVP-NIVHGVNQKEHNPDEIDIFSAA 290
Cdd:PRK07729 74 LLNNRDPKELPWTDLGID--IVIEATGKFNSKEKAILHVEA-GAKKVILTAPGKNEDvTIVVGVNEDQLDIEKHTIISNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 291 SCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSN 370
Cdd:PRK07729 151 SCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 371 AIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADGKNV 450
Cdd:PRK07729 231 ALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKT-AANGALKGILEFS-EEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVK 308
|
330 340
....*....|....*....|....*
gi 500027819 451 ILyIWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PRK07729 309 VL-AWYDNEWGYSCRVVDLVTLVAD 332
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
132-475 |
5.77e-84 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 262.54 E-value: 5.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 132 VILYGFGRIGRLVARELMTRTGkgNQLRLRAVVtrgkvDQSVLEKRASLLKSDSVHGPFSGTVTIDEknSALIINGTTVH 211
Cdd:PRK07403 4 VAINGFGRIGRNFLRCWLGREN--SQLELVAIN-----DTSDPRTNAHLLKYDSMLGKLNADISADE--NSITVNGKTIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 212 MISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG--VPNIVHGVNQKEHNPDEIDIFSA 289
Cdd:PRK07403 75 CVSDRNPLNLPWKEWGID--LIIESTGVFVTKEGASKHIQA-GAKKVLITAPGKGedIGTYVVGVNHHEYDHEDHNIISN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 290 ASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTS 369
Cdd:PRK07403 152 ASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 370 NAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVsADGKN 449
Cdd:PRK07403 232 IALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKD-ASEGPLKGILEYS-DLPLVSSDYRGTDASSIVDASLTMV-MGGDM 308
|
330 340
....*....|....*....|....*.
gi 500027819 450 VILYIWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PRK07403 309 VKVIAWYDNEWGYSQRVVDLAELVAR 334
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
136-470 |
2.01e-80 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 252.55 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRTGkgnqlrLRAV-VTRGKVDQSVLekrASLLKSDSVHGPFSGTVTIDEknSALIINGTTVHMIS 214
Cdd:NF033735 5 GFGRIGRLALRALWGRPG------LEIVhINDLAGDAATL---AHLLEFDSVHGRWDAEVTAEE--DSIVIDGKRISFSS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 215 ANQPEDIDYtkyGINNALVIDNTGAFRDKEALSRHLSsKGAAKVLLTAPGK--GVPNIVHGVNQKEHNPDEIDIFSAASC 292
Cdd:NF033735 74 NKDIEDTPW---GDGVDVVIECTGKFKTPEKLQPYFD-QGVKKVVVSAPVKeeGVLNIVYGVNDHLYDPARHRIVTAASC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 293 TTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAI 372
Cdd:NF033735 150 TTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 373 RVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVsADGKNVIL 452
Cdd:NF033735 230 RVPLLNASLTDCVFEVERPTTVEEVNALFKA-AAEGPLKGILGYE-ERPLVSVDYVNDPRSSIIDALSTMV-VNGTQVKI 306
|
330
....*....|....*...
gi 500027819 453 YIWYDNEYGYSHQVIRLA 470
Cdd:NF033735 307 YAWYDNEWGYANRMVDLA 324
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
136-476 |
2.56e-75 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 242.84 E-value: 2.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRtgkgNQLRLRAVvTRGKVDQSVLekrASLLKSDSVHGPFSGTV-TIDEknSALIINGTTVHMIS 214
Cdd:PLN02272 92 GFGRIGRLVLRIATSR----DDIEVVAV-NDPFIDAKYM---AYMFKYDSTHGNFKGTInVVDD--STLEINGKQIKVTS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 215 ANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGVPNIVHGVNQKEHNPDeIDIFSAASCTT 294
Cdd:PLN02272 162 KRDPAEIPWGDFGAE--YVVESSGVFTTVEKASAHLKG-GAKKVVISAPSADAPMFVVGVNEKTYKPN-MNIVSNASCTT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 295 NAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIR 373
Cdd:PLN02272 238 NCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKdWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 374 VPVPNGSLAILNLEVEKETSLEDVNTLLKkYALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADgKNVILY 453
Cdd:PLN02272 318 VPTPNVSVVDLTCRLEKSASYEDVKAAIK-YASEGPLKGILGYT-DEDVVSNDFVGDSRSSIFDAKAGIGLSA-SFMKLV 394
|
330 340
....*....|....*....|...
gi 500027819 454 IWYDNEYGYSHQVIRLAKYIAKV 476
Cdd:PLN02272 395 SWYDNEWGYSNRVLDLIEHMALV 417
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
292-459 |
8.98e-75 |
|
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: 232.35 E-value: 8.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 292 CTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNA 371
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 372 IRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSIDnELVSSDIIGSSAPAIYDSNATIVsADGKNVI 451
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAA-EGPLKGILGYTED-PLVSSDFVGDPHSSIFDATATIV-LGGNLVK 157
|
....*...
gi 500027819 452 LYIWYDNE 459
Cdd:cd18126 158 VVAWYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
121-475 |
1.97e-72 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 234.44 E-value: 1.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 121 AKETEAVTPKDVILYGFGRIGRLVARELMTRtgKGNQLRLRAVVTRGKVDQSvlekrASLLKSDSVHGPFSGTVTIdEKN 200
Cdd:PLN03096 52 ARRAVTEAKIKVAINGFGRIGRNFLRCWHGR--KDSPLDVVAINDTGGVKQA-----SHLLKYDSTLGTFDADVKP-VGD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 201 SALIINGTTVHMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEH 279
Cdd:PLN03096 124 DAISVDGKVIKVVSDRNPLNLPWGELGID--LVIEGTGVFVDREGAGKHIQA-GAKKVLITAPGKGdIPTYVVGVNADDY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 280 NPDEiDIFSAASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKA 359
Cdd:PLN03096 201 KHSD-PIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 360 LPVFEGKLTSNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELvEQIQYSIDNELVSSDIIGSSAPAIYDSN 439
Cdd:PLN03096 280 LPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAA-EKEL-KGILAVCDEPLVSVDFRCSDVSSTIDSS 357
|
330 340 350
....*....|....*....|....*....|....*.
gi 500027819 440 ATIVSADGKnVILYIWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PLN03096 358 LTMVMGDDM-VKVVAWYDNEWGYSQRVVDLADIVAN 392
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
129-474 |
1.58e-71 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 231.10 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 129 PKDVILYGFGRIGRLVARELMTRTGKGNQLRLRAVVtrgkvDQSV-LEKRASLLKSDSVHGPFSGTVTIDE------KNS 201
Cdd:PTZ00434 3 PIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVV-----DMSTnAEYFAYQMKYDTVHGRPKYTVETTKsspsvkTDD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 202 ALIINGTTVHMISANQ-PEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEH 279
Cdd:PTZ00434 78 VLVVNGHRIKCVKAQRnPADLPWGKLGVD--YVIESTGLFTDKLAAEGHLKG-GAKKVVISAPASGgAKTIVMGVNQHEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 280 NPDEIDIFSAASCTTNAITPVLKA-VQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVS 357
Cdd:PTZ00434 155 SPTEHHVVSNASCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKdWRGGRAAAVNIIPSTTGAAKAVG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 358 KALPVFEGKLTSNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYD 437
Cdd:PTZ00434 235 MVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKR-ASQTYMKGILGFT-DDELVSADFINDNRSSIYD 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 500027819 438 SNATI---VSADGKNVILYIWYDNEYGYSHQVIRLAKYIA 474
Cdd:PTZ00434 313 SKATLqnnLPGERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
119-475 |
9.47e-68 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 223.62 E-value: 9.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 119 SDAKETEAVTPKDVILYGFGRIGRLVARELMTRtgKGNQLRLRAVVTRGKVDQSvlekrASLLKSDSVHGPFSGTVTIDE 198
Cdd:PLN02237 65 STPVRGETVAKLKVAINGFGRIGRNFLRCWHGR--KDSPLDVVVVNDSGGVKNA-----SHLLKYDSMLGTFKADVKIVD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 199 kNSALIINGTTVHMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG--VPNIVHGVNQ 276
Cdd:PLN02237 138 -DETISVDGKPIKVVSNRDPLKLPWAELGID--IVIEGTGVFVDGPGAGKHIQA-GAKKVIITAPAKGadIPTYVVGVNE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 277 KEHNPDEIDIFSAASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAV 356
Cdd:PLN02237 214 DDYDHEVANIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 357 SKALPVFEGKLTSNAIRVPVPNGSLAILNLEVEKE-TSLEDVNTLLKKyALEGELvEQIQYSIDNELVSSDIIGSSAPAI 435
Cdd:PLN02237 294 SLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKgITAEDVNAAFRK-AADGPL-KGILAVCDVPLVSVDFRCSDVSST 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 500027819 436 YDSNATIVSADGKnVILYIWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PLN02237 372 IDASLTMVMGDDM-VKVVAWYDNEWGYSQRVVDLAHLVAA 410
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
136-471 |
2.13e-66 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 216.91 E-value: 2.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVarelmtrtgkgnqlrLRAVVTRGKV----------DQSVLekrASLLKSDSVHGPFSGTVTIDekNSALII 205
Cdd:PRK08955 9 GFGRIGRLA---------------LRAAWDWPELefvqindpagDAATL---AHLLEFDSVHGRWHHEVTAE--GDAIVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 206 NGttvHMISANQPEDIDYTKYGiNNALVIDNTGAFRDKEALSRHLSsKGAAKVLLTAPGK--GVPNIVHGVNQKEHNPDE 283
Cdd:PRK08955 69 NG---KRIRTTQNKAIADTDWS-GCDVVIEASGVMKTKALLQAYLD-QGVKRVVVTAPVKeeGVLNIVMGVNDHLFDPAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 284 IDIFSAASCTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVF 363
Cdd:PRK08955 144 HPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 364 EGKLTSNAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIV 443
Cdd:PRK08955 224 KGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKE-AAEGELKGILGYE-ERPLVSIDYKTDPRSSIVDALSTMV 301
|
330 340
....*....|....*....|....*...
gi 500027819 444 sADGKNVILYIWYDNEYGYSHQVIRLAK 471
Cdd:PRK08955 302 -VNGTQVKLYAWYDNEWGYANRTAELAR 328
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
136-475 |
2.36e-60 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 201.22 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRtgkgNQLRLRAVvtrgKVDQSVLEKRASLLKSDSVHGPFSGTVTIdeKNSALIINGTTVHMISA 215
Cdd:PTZ00023 9 GFGRIGRLVFRAALER----EDVEVVAI----NDPFMTLDYMCYLLKYDSVHGSLPAEVSV--TDGFLMIGSKKVHVFFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 216 NQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGK-GVPNIVHGVNQKEHNPDEIdIFSAASCTT 294
Cdd:PTZ00023 79 KDPAAIPWGKNGVD--VVCESTGVFLTKEKAQAHLKG-GAKKVIMSAPPKdDTPIYVMGVNHTQYDKSQR-IVSNASCTT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 295 NAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMH---NKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNA 371
Cdd:PTZ00023 155 NCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 372 IRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADgKNVI 451
Cdd:PTZ00023 235 FRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKK-AAEGPLKGILGYT-DDEVVSSDFVHDKRSSIFDVKAGIALND-TFVK 311
|
330 340
....*....|....*....|....
gi 500027819 452 LYIWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PTZ00023 312 LVSWYDNEWGYSNRLLDLAHYITQ 335
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
136-475 |
5.91e-60 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 200.33 E-value: 5.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRtgkgNQLRLRAVvtrgKVDQSVLEKRASLLKSDSVHGPFSGTVTIDEKNSALIINGTTVHMISA 215
Cdd:PLN02358 12 GFGRIGRLVARVVLQR----DDVELVAV----NDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTVFGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 216 NQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGVPNIVHGVNQKEHNPDeIDIFSAASCTTN 295
Cdd:PLN02358 84 RNPEDIPWGEAGAD--FVVESTGVFTDKDKAAAHLKG-GAKKVVISAPSKDAPMFVVGVNEHEYKSD-LDIVSNASCTTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 296 AITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIRV 374
Cdd:PLN02358 160 CLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKdWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 375 PVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADgKNVILYI 454
Cdd:PLN02358 240 PTVDVSVVDLTVRLEKAATYDEIKKAIKEES-EGKLKGILGYT-EDDVVSTDFVGDNRSSIFDAKAGIALSD-KFVKLVS 316
|
330 340
....*....|....*....|.
gi 500027819 455 WYDNEYGYSHQVIRLAKYIAK 475
Cdd:PLN02358 317 WYDNEWGYSSRVVDLIVHMSK 337
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
136-475 |
1.58e-59 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 198.80 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRTGkgnqlrLRAVVTRGKVDQsvlEKRASLLKSDSVHGPFSGTVTIdeKNSALIINGTTVHMISA 215
Cdd:PRK15425 9 GFGRIGRIVFRAAQKRSD------IEIVAINDLLDA---DYMAYMLKYDSTHGRFDGTVEV--KDGHLIVNGKKIRVTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 216 NQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGK-GVPNIVHGVNQKEHNPDeiDIFSAASCTT 294
Cdd:PRK15425 78 RDPANLKWDEVGVD--VVAEATGLFLTDETARKHITA-GAKKVVMTGPSKdNTPMFVKGANFDKYAGQ--DIVSNASCTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 295 NAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDN-MHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIR 373
Cdd:PRK15425 153 NCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 374 VPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSADgKNVILY 453
Cdd:PRK15425 233 VPTPNVSVVDLTVRLEKAATYEQIKAAVKA-AAEGEMKGVLGYT-EDDVVSTDFNGEVCTSVFDAKAGIALND-NFVKLV 309
|
330 340
....*....|....*....|..
gi 500027819 454 IWYDNEYGYSHQVIRLAKYIAK 475
Cdd:PRK15425 310 SWYDNETGYSNKVLDLIAHISK 331
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
131-291 |
8.79e-52 |
|
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: 172.58 E-value: 8.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 131 DVILYGFGRIGRLVARELMTRtgkgNQLRLRAVVTRGKVdqsvlEKRASLLKSDSVHGPFSGTVTIDEknSALIINGTTV 210
Cdd:cd05214 2 KVGINGFGRIGRLVFRAALER----DDIEVVAINDLTDD-----ETLAYLLKYDSVHGRFDGEVEVDD--DALIVNGKKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 211 HMISANQPEDIDYTKYGInnALVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPNIVHGVNQKEHNPDEiDIFSA 289
Cdd:cd05214 71 KVFAERDPAELPWGELGV--DIVIESTGVFTTKEKASAHLKA-GAKKVIISAPAKDdDPTIVMGVNHDKYDADD-KIISN 146
|
..
gi 500027819 290 AS 291
Cdd:cd05214 147 AS 148
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
297-456 |
1.16e-48 |
|
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: 164.30 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 297 ITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIRVP 375
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKdLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 376 VPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGKNVILYIW 455
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAA-EGALKGILSYT-EDPLVSSDFIGDPHSSIFDAKETIVV-NGNFVKVVAW 157
|
.
gi 500027819 456 Y 456
Cdd:pfam02800 158 Y 158
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
136-467 |
1.36e-46 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 164.84 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMtRTGKGNQLRLRAVVTRGKVdqsvlEKRASLLKSDSVHGPFSGTVTIDekNSALIINGTTVHMISA 215
Cdd:PRK13535 8 GFGRIGRNVLRALY-ESGRRAEITVVAINELADA-----EGMAHLLKYDTSHGRFAWDVRQE--RDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 216 NQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPN-IVHGVNQKEHNPDEiDIFSAASCT 293
Cdd:PRK13535 80 RDIASLPWRELGVD--VVLDCTGVYGSREDGEAHIAA-GAKKVLFSHPGSNdLDAtVVYGVNHDQLRAEH-RIVSNASCT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 294 TNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNAIR 373
Cdd:PRK13535 156 TNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 374 VPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGKNVILY 453
Cdd:PRK13535 236 VPTINVTAIDLSVTVKKPVKVNEVNQLLQK-AAQGAFHGIVDYT-ELPLVSIDFNHDPHSAIVDGTQTRVS-GAHLIKTL 312
|
330
....*....|....
gi 500027819 454 IWYDNEYGYSHQVI 467
Cdd:PRK13535 313 VWCDNEWGFANRML 326
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
131-292 |
1.53e-42 |
|
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: 147.70 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 131 DVILYGFGRIGRLVARELMTRtgkgNQLRLRAVvtrgkVDQSVLEKRASLLKSDSVHGPFSGTVTIDEKNsaLIINGTTV 210
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALER----PDVEVVAI-----NDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDG--LVVNGKAI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 211 HMISANQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGV-PNIVHGVNQKEHNPDEiDIFSA 289
Cdd:smart00846 71 KVFAERDPANLPWGELGVD--IVVECTGGFTTREKASAHLKA-GAKKVIISAPSKDAdPTFVYGVNHDEYDGED-HIISN 146
|
...
gi 500027819 290 ASC 292
Cdd:smart00846 147 ASC 149
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
292-459 |
2.04e-33 |
|
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: 123.88 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 292 CTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNK-YRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSN 370
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKdWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 371 AIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlegELVEQIQYsIDNELVSSDIIGSSAPAIYDSNATIVSADgkNV 450
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAP---EGKGRLGY-TEAEDVSSDFRGDIFESVFDAESIIAVND--NE 154
|
170
....*....|
gi 500027819 451 ILYI-WYDNE 459
Cdd:cd18123 155 VKLMqWYDNE 164
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
292-459 |
1.04e-28 |
|
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: 111.35 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 292 CTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTSNA 371
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 372 IRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSAPAIYDSNATIVSaDGKNVI 451
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQ-ASQGRLKGILGYT-EEPLVSVDFNHDPHSCIVDGTQTRVS-GKRLVK 157
|
....*...
gi 500027819 452 LYIWYDNE 459
Cdd:cd23937 158 LLVWCDNE 165
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
132-243 |
4.00e-26 |
|
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: 101.79 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 132 VILYGFGRIGRLVARELMTRtgkgNQLRLRAVVTRGKvdqsvLEKRASLLKSDSVHGPFSGTVTIDEKnsALIINGTTVH 211
Cdd:pfam00044 3 VGINGFGRIGRLVLRAALER----PDIEVVAINDLTD-----PETLAYLLKYDSVHGRFPGEVEAEED--GLVVNGKKIK 71
|
90 100 110
....*....|....*....|....*....|..
gi 500027819 212 MISANQPEDIDYTKYGINnaLVIDNTGAFRDK 243
Cdd:pfam00044 72 VFAERDPAELPWGDLGVD--VVIESTGVFTTK 101
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
136-291 |
5.26e-22 |
|
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: 92.72 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRtGKGNQLRLRAVVtrgkvDQSVLEKRASLLKSDSVHGPFSGTVTIDekNSALIINGTTVHMISA 215
Cdd:cd17892 7 GYGRIGRNVLRALYES-GRRAEFQVVAIN-----ELADAETIAHLTKYDTTHGRFPGEVRVE--NDQLFVNGDKIRVLHE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500027819 216 NQPEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKG-VPN-IVHGVNQKEHNPDEiDIFSAAS 291
Cdd:cd17892 79 PDPENLPWRELGID--LVLECTGVFGSREDAERHLAA-GAKKVLFSHPASNdVDAtIVYGINQDLLRAEH-RIVSNAS 152
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
136-471 |
2.11e-17 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 83.39 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 136 GFGRIGRLVARELMTRTgkgnQLRLRAVVtrgkvDQSV-LEKRASLLKSDSVHGPFSGTvTIDEKNSALIINGTTVHMIS 214
Cdd:PTZ00353 9 GFGPVGKAVLFASLTDP----LVTVVAVN-----DASVsIAYIAYVLEQESPLSAPDGA-SIRVVGEQIVLNGTQKIRVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 215 ANQ-PEDIDYTKYGINnaLVIDNTGAFRDKEALSRHLSSkGAAKVLLTAPGKGVPNIVHGVNQKEHNPdEIDIFSAASCT 293
Cdd:PTZ00353 79 AKHdLVEIAWRDYGVQ--YVVECTGLYSTRSRCWGHVTG-GAKGVFVAGQSADAPTVMAGSNDERLSA-SLPVCCAGAPI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 294 TNAITPVLKAVQDSLGVVHGHLETIHAyTNDQNLV----DNMHNkYRRGRAAALNMVITETGAGKAVSKALPVFEGKLTS 369
Cdd:PTZ00353 155 AVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIaarsKNSQD-WRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 370 NAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKyALEGELVEQIQYSiDNELVSSDIIGSSApAIYDSNATIVSADGKN 449
Cdd:PTZ00353 233 SAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAE-AASDRLNGVLCIS-KRDMISVDCIPNGK-LCYDATSSSSSREGEV 309
|
330 340
....*....|....*....|..
gi 500027819 450 VILYIWYDNEYGYSHQVIRLAK 471
Cdd:PTZ00353 310 HKMVLWFDVECYYAARLLSLVK 331
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
292-459 |
2.82e-17 |
|
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: 79.10 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 292 CTTNAITPVLKAVQDSLGVVHGHLETIHAYTNDQNLVDNMHNKYrRGRAAALNMVITETGAGKAVSKALPVFE--GKLTS 369
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKS-EVRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500027819 370 NAIRVPVPNGSLAILNLEVEKETSLEDVNTLLKKYAlEGELVEQIQYSIDNElVSSDIIGSSAPAIYDSNATIVSaDGKN 449
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAV-EEVQISAEDGLTYAK-VSTRSVGGVYGVPVGRQREFAF-DDNK 156
|
170
....*....|
gi 500027819 450 VILYIWYDNE 459
Cdd:cd18122 157 LKVFSAVDNE 166
|
|
| Glyco_32 |
smart00640 |
Glycosyl hydrolases family 32; |
187-242 |
6.08e-03 |
|
Glycosyl hydrolases family 32;
Pssm-ID: 214757 [Multi-domain] Cd Length: 437 Bit Score: 38.84 E-value: 6.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500027819 187 HGPFSGTVTIDEKNSALIINGTTV-----------HMISANQPEDIDYTKYGINnaLVID-----NTGAFRD 242
Cdd:smart00640 67 NGVFSGSAVIDPGNLSLLYTGNVAidtnvqvqrqaYQCAASDDLGGTWTKYDGN--PVLTpppggGTEHFRD 136
|
|
| |
