|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 661.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 1 MADKKIKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTV 80
Cdd:PLN02358 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 81 FGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNC 160
Cdd:PLN02358 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVP 240
Cdd:PLN02358 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*...
gi 297828898 321 EWGYSSRVVDLIVHMSKA 338
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSKA 338
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
5-338 |
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: 569.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 5 KIKIGINGFGRIGRLVARVVLQR-DDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIkDEKTLLFGEKPVTVFGI 83
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEV-EGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 84 RNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASCTTNCLA 162
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 297828898 323 GYSSRVVDLIVHMSKA 338
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
7-330 |
1.71e-173 |
|
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: 484.47 E-value: 1.71e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 7 KIGINGFGRIGRLVARVVLQRDD--VELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIkDEKTLLFGEKPVT-VFGI 83
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEG-EVTV-DEDGLVVNGKEVIsVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 84 RNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASCTTNCLA 162
Cdd:TIGR01534 78 RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIA--LSDKFVKLVSWYDN 320
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 297828898 321 EWGYSSRVVD 330
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
156-321 |
7.81e-120 |
|
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: 342.13 E-value: 7.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGM 235
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 236 SFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLV 315
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 297828898 316 SWYDNE 321
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
8-331 |
2.69e-117 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 341.91 E-value: 2.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNelKIKDEKTLLFGEKPVTVFGIRNPE 87
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAE--VTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 88 DIPWAEaGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEHEYKSDLD-IVSNASCTTNCLAPL 164
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHrIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDV 244
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 297828898 325 SSRVVDL 331
Cdd:NF033735 317 ANRMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
161-318 |
5.35e-90 |
|
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: 266.00 E-value: 5.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVP 240
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297828898 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 318
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-156 |
2.16e-73 |
|
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: 223.58 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIKDEkTLLFGEKPVTVFGIRN 85
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPG-TVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASC 156
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 661.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 1 MADKKIKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTV 80
Cdd:PLN02358 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 81 FGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNC 160
Cdd:PLN02358 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVP 240
Cdd:PLN02358 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*...
gi 297828898 321 EWGYSSRVVDLIVHMSKA 338
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSKA 338
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-336 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 623.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 2 ADKKIKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhNELKIKDEKTLLFGEKPVTVF 81
Cdd:PLN02272 82 SSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFK-GTINVVDDSTLEINGKQIKVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 82 GIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCL 161
Cdd:PLN02272 161 SKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 162 APLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPT 241
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 242 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 321
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400
|
330
....*....|....*
gi 297828898 322 WGYSSRVVDLIVHMS 336
Cdd:PLN02272 401 WGYSNRVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
5-338 |
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: 569.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 5 KIKIGINGFGRIGRLVARVVLQR-DDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIkDEKTLLFGEKPVTVFGI 83
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEV-EGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 84 RNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASCTTNCLA 162
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 297828898 323 GYSSRVVDLIVHMSKA 338
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-337 |
2.85e-177 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 494.35 E-value: 2.85e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHnELKIKDEKtLLFGEKPVTVFGIRN 85
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPA-EVSVTDGF-LMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDdTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSM--KDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*
gi 297828898 323 GYSSRVVDLIVHMSK 337
Cdd:PTZ00023 321 GYSNRLLDLAHYITQ 335
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
7-330 |
1.71e-173 |
|
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: 484.47 E-value: 1.71e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 7 KIGINGFGRIGRLVARVVLQRDD--VELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIkDEKTLLFGEKPVT-VFGI 83
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEG-EVTV-DEDGLVVNGKEVIsVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 84 RNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASCTTNCLA 162
Cdd:TIGR01534 78 RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIA--LSDKFVKLVSWYDN 320
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 297828898 321 EWGYSSRVVD 330
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
6-337 |
7.08e-151 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 427.23 E-value: 7.08e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhNELKIKDEKTLLFGEKpVTVFGIRN 85
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFD-GTVEVKDGHLIVNGKK-IRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDlDIVSNASCTTNCLAPL 164
Cdd:PRK15425 80 PANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDV 244
Cdd:PRK15425 159 AKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
Cdd:PRK15425 239 SVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
|
330
....*....|...
gi 297828898 325 SSRVVDLIVHMSK 337
Cdd:PRK15425 319 SNKVLDLIAHISK 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
6-336 |
2.47e-147 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 419.46 E-value: 2.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRD----DVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIK-------DEKTLLFG 74
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKsspsvktDDVLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 75 EKPVTVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAP-SKDAPMFVVGVNEHEYK-SDLDIVS 152
Cdd:PTZ00434 84 HRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 153 NASCTTNCLAPLAKVI-NDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGK 231
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 232 LTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKA----GIAL 307
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnNLPG 323
|
330 340
....*....|....*....|....*....
gi 297828898 308 SDKFVKLVSWYDNEWGYSSRVVDLIVHMS 336
Cdd:PTZ00434 324 ERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
5-337 |
1.19e-129 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 374.07 E-value: 1.19e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 5 KIKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFiTTEYMTYMFKYDSVHGQWKhNELKIKDEKTLLFGEKpVTVFGIR 84
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFD-GTVEAFEDHLLVDGKK-IRLLNNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 85 NPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM-FVVGVNEHEYKSDLD-IVSNASCTTNCLA 162
Cdd:PRK07729 79 DPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTV 242
Cdd:PRK07729 159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
Cdd:PRK07729 238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317
|
330
....*....|....*
gi 297828898 323 GYSSRVVDLIVHMSK 337
Cdd:PRK07729 318 GYSCRVVDLVTLVAD 332
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
156-321 |
7.81e-120 |
|
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: 342.13 E-value: 7.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGM 235
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 236 SFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLV 315
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 297828898 316 SWYDNE 321
Cdd:cd18126 160 AWYDNE 165
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
6-331 |
9.70e-119 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 346.12 E-value: 9.70e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDD--VELVAVNDpfiTTEYMT--YMFKYDSVHGqwKHNELKIKDEKTLLFGEKPVTVF 81
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENsqLELVAIND---TSDPRTnaHLLKYDSMLG--KLNADISADENSITVNGKTIKCV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 82 GIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEHEYKSDL-DIVSNASCTT 158
Cdd:PRK07403 77 SDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKgeDIGTYVVGVNHHEYDHEDhNIISNASCTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 159 NCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFR 238
Cdd:PRK07403 157 NCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 239 VPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 318
Cdd:PRK07403 236 VPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWY 315
|
330
....*....|...
gi 297828898 319 DNEWGYSSRVVDL 331
Cdd:PRK07403 316 DNEWGYSQRVVDL 328
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
8-331 |
2.69e-117 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 341.91 E-value: 2.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNelKIKDEKTLLFGEKPVTVFGIRNPE 87
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAE--VTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 88 DIPWAEaGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEHEYKSDLD-IVSNASCTTNCLAPL 164
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHrIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDV 244
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 297828898 325 SSRVVDL 331
Cdd:NF033735 317 ANRMVDL 323
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
1-331 |
1.47e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 327.27 E-value: 1.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 1 MADKKIKIGINGFGRIGRLVARVVLQRDD--VELVAVNDPFiTTEYMTYMFKYDSVHGQWKhNELKIKDEKTLLFGEKPV 78
Cdd:PLN03096 56 VTEAKIKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTG-GVKQASHLLKYDSTLGTFD-ADVKPVGDDAISVDGKVI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 79 TVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEHEYKSDLDIVSNASCT 157
Cdd:PLN03096 134 KVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKHSDPIISNASCT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 158 TNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSF 237
Cdd:PLN03096 214 TNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 238 RVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSW 317
Cdd:PLN03096 293 RVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAW 372
|
330
....*....|....
gi 297828898 318 YDNEWGYSSRVVDL 331
Cdd:PLN03096 373 YDNEWGYSQRVVDL 386
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
1-331 |
6.49e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 327.24 E-value: 6.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 1 MADKKIKIGINGFGRIGRLVARVVLQRDD--VELVAVNDPFiTTEYMTYMFKYDSVHGQWKhNELKIKDEKTLLFGEKPV 78
Cdd:PLN02237 71 ETVAKLKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSG-GVKNASHLLKYDSMLGTFK-ADVKIVDDETISVDGKPI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 79 TVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEHEYKSDL-DIVSNAS 155
Cdd:PLN02237 149 KVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVaNIVSNAS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGM 235
Cdd:PLN02237 229 CTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 236 SFRVPTVDVSVVDLTVRLEKAA-TYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKL 314
Cdd:PLN02237 308 ALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKV 387
|
330
....*....|....*..
gi 297828898 315 VSWYDNEWGYSSRVVDL 331
Cdd:PLN02237 388 VAWYDNEWGYSQRVVDL 404
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
5-332 |
5.25e-105 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 310.89 E-value: 5.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 5 KIKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNelKIKDEKTLLFGEKPVTVFGIR 84
Cdd:PRK08955 2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHE--VTAEGDAIVINGKRIRTTQNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 85 NPEDIPWAeaGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEHEYKSDLD-IVSNASCTTNCL 161
Cdd:PRK08955 80 AIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHpIVTAASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 162 APLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPT 241
Cdd:PRK08955 158 APVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 242 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 321
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|.
gi 297828898 322 WGYSSRVVDLI 332
Cdd:PRK08955 317 WGYANRTAELA 327
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
6-338 |
9.00e-94 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 282.33 E-value: 9.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQ---RDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHnelKIKDEKTLLF-GEKPVTVF 81
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYEsgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAW---DVRQERDQLFvGDDAIRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 82 GIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEHEYKSDLDIVSNASCTT 158
Cdd:PRK13535 78 HERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 159 NCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFR 238
Cdd:PRK13535 157 NCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 239 VPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 318
Cdd:PRK13535 236 VPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 315
|
330 340
....*....|....*....|
gi 297828898 319 DNEWGYSSRVVDLIVHMSKA 338
Cdd:PRK13535 316 DNEWGFANRMLDTTLAMAAA 335
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
161-318 |
5.35e-90 |
|
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: 266.00 E-value: 5.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVP 240
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297828898 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 318
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
12-338 |
5.03e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 264.48 E-value: 5.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 12 GFGRIGRLVARVVLQR----DDVELVAV-------NDpfitTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTV 80
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggNGLRLRAIvvrkgseGD----LEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 81 FGIRNPEDIPWAEAGAD--YVVESTGVFTDKDKAAAHLKG-GAKKVVISAPSK-DAPMFVVGVNEHEYKSDLDIVSNASC 156
Cdd:PRK08289 210 IYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSDITDEDKIVSAASC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 157 TTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDwRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMS 236
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 237 FRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEES-EGKLKGILGYTED-DVVSTDFVGDNRSSIFDAKAGIAlSDKFVKL 314
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIV-NGNRAVL 447
|
330 340
....*....|....*....|....
gi 297828898 315 VSWYDNEWGYSSRVVDLIVHMSKA 338
Cdd:PRK08289 448 YVWYDNEFGYSCQVVRVMEQMAGV 471
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
6-155 |
2.88e-82 |
|
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467614 [Multi-domain] Cd Length: 164 Bit Score: 246.54 E-value: 2.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITtEYMTYMFKYDSVHGQWKHnELKIKDEKtLLFGEKPVTVFGIRN 85
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDG-EVEVDDDA-LIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDLDIVSNAS 155
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
156-321 |
4.84e-81 |
|
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: 243.68 E-value: 4.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGM 235
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 236 SFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGklKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLV 315
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 297828898 316 SWYDNE 321
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-156 |
2.16e-73 |
|
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: 223.58 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHnELKIKDEkTLLFGEKPVTVFGIRN 85
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPG-TVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLDIVSNASC 156
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-338 |
5.35e-61 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 198.56 E-value: 5.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTVFGIRN 85
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVLNGTQKIRVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 166 KVINDRFGIVEGLMTTVHSITAtQKTVDGPSM--KDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVD 243
Cdd:PTZ00353 163 RALHEVYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 244 VSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRsSIFDAKAGIALSD-KFVKLVSWYDNEW 322
Cdd:PTZ00353 242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSREgEVHKMVLWFDVEC 320
|
330
....*....|....*.
gi 297828898 323 GYSSRVVDLIVHMSKA 338
Cdd:PTZ00353 321 YYAARLLSLVKQLHQI 336
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
156-321 |
9.72e-49 |
|
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: 161.04 E-value: 9.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGM 235
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 236 SFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLV 315
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 297828898 316 SWYDNE 321
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
156-321 |
8.08e-48 |
|
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: 158.84 E-value: 8.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWrgGRAASFNIIPSSTGAAKAVGKVLPALN--GKLT 233
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 234 GMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVK 313
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 297828898 314 LVSWYDNE 321
Cdd:cd18122 159 VFSAVDNE 166
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-109 |
7.02e-44 |
|
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: 146.09 E-value: 7.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHNelKIKDEKTLLFGEKPVTVFGIRN 85
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGE--VEAEEDGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 297828898 86 PEDIPWAEAGADYVVESTGVFTDK 109
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
6-155 |
5.43e-39 |
|
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: 135.86 E-value: 5.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVL---QRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWkHNELKIKDEKTLLFGEKpVTVFG 82
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYesgRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRF-PGEVRVENDQLFVNGDK-IRVLH 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297828898 83 IRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEHEYKSDLDIVSNAS 155
Cdd:cd17892 78 EPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
6-160 |
1.59e-17 |
|
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: 77.01 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAVNDPfitteymtymfkydsvhgqwkhnelkikdektllfgekpvtvfgirn 85
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR----------------------------------------------- 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297828898 86 pedipwaeagADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEHEYKSDLDIVSNASCTTNC 160
Cdd:cd05192 34 ----------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
6-35 |
6.21e-05 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 42.56 E-value: 6.21e-05
10 20 30
....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:cd02270 1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
| DapB_N |
pfam01113 |
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ... |
6-35 |
8.07e-05 |
|
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 41.45 E-value: 8.07e-05
10 20 30
....*....|....*....|....*....|.
gi 297828898 6 IKIGINGF-GRIGRLVARVVLQRDDVELVAV 35
Cdd:pfam01113 1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA 31
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
4-38 |
1.35e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 42.99 E-value: 1.35e-04
10 20 30
....*....|....*....|....*....|....*
gi 297828898 4 KKIKIGINGFGRIGRLVARVVLQRDDVELVAVNDP 38
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
6-37 |
2.64e-04 |
|
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: 40.62 E-value: 2.64e-04
10 20 30
....*....|....*....|....*....|...
gi 297828898 6 IKIGINGF-GRIGRLVARVVLQRDDVELVAVND 37
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVD 33
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
5-35 |
3.19e-04 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 42.12 E-value: 3.19e-04
10 20 30
....*....|....*....|....*....|.
gi 297828898 5 KIKIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:PRK04207 1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGV 31
|
|
| ASADH_C_arch_fung_like |
cd18130 |
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ... |
156-268 |
5.11e-04 |
|
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.
Pssm-ID: 467680 [Multi-domain] Cd Length: 180 Bit Score: 40.30 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSIT-ATQKTVDGPSMKDwrggraasfNIIPSSTGAAKAV----GKVLPALNG 230
Cdd:cd18130 1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISgAGYPGVPSLDILD---------NVIPYIGGEEEKIesetKKILGTLNE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 297828898 231 --------KLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKE 268
Cdd:cd18130 72 dkiepadfKVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALEN 117
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
69-174 |
2.91e-03 |
|
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: 38.86 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297828898 69 KTLLFGEKPVTVfgirnpEDI-PWAEAGADYVVESTGVFTDKD---KAAAHlkgGAkkVVISAPS-----KDAPMFVVGV 139
Cdd:COG0136 41 KTVSFGGKELTV------EDAtDFDFSGVDIALFSAGGSVSKEyapKAAAA---GA--VVIDNSSafrmdPDVPLVVPEV 109
|
90 100 110
....*....|....*....|....*....|....*..
gi 297828898 140 NEHEYKSDLD--IVSNASCTTNCLAPLAKVINDRFGI 174
Cdd:COG0136 110 NPEALADHLPkgIIANPNCSTIQMLVALKPLHDAAGI 146
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
6-35 |
9.87e-03 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, 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). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 36.36 E-value: 9.87e-03
10 20 30
....*....|....*....|....*....|
gi 297828898 6 IKIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:cd24146 1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGA 30
|
|
| |
