|
Name |
Accession |
Description |
Interval |
E-value |
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
5-281 |
4.53e-83 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 251.19 E-value: 4.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAV-QADIIFSCLPTSTEVENLIAQVQ---- 79
Cdd:COG2084 4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAaAADVVITMLPDDAAVEEVLLGEDglla 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 80 -LKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHVGE 158
Cdd:COG2084 84 aLRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 159 PGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPqRVLNRAFPNTFALPLLAKDTG 238
Cdd:COG2084 164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-RMLAGDFDPGFALDLMLKDLG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1253006089 239 IALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMY 281
Cdd:COG2084 243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-157 |
3.24e-50 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 163.02 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 4 SVAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAVQ-ADIIFSCLPTSTEVENLIAQVQ--- 79
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAgLDVVITMVPAGAAVDAVIFGEGllp 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006089 80 -LKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHVG 157
Cdd:pfam03446 81 gLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-282 |
1.22e-45 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 155.59 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 1 MIQSVAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAE---QHAAEYGTQAVELAQavQADIIFSCLPTSTEV------ 71
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAeviAAGAETASTAKAVAE--QCDVIITMLPNSPHVkevalg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 72 ENLIAQvQLKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGK 151
Cdd:PRK11559 79 ENGIIE-GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 152 VIQHVGEPGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPqRVLNRAFPNTFALP 231
Cdd:PRK11559 158 SVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRID 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1253006089 232 LLAKDTGIALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMYE 282
Cdd:PRK11559 237 LHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYE 287
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
5-88 |
2.16e-06 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 48.03 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHL-PKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAV----QADIIFSCLPTST---EVENLIA 76
Cdd:cd05213 181 VLVIGAGEMGELAAKHLaAKGVAEITIANRTYERAEELAKELGGNAVPLDELLellnEADVVISATGAPHyakIVERAMK 260
|
90
....*....|..
gi 1253006089 77 QVQLKAgSVWVD 88
Cdd:cd05213 261 KRSGKP-RLIVD 271
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
5-281 |
4.53e-83 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 251.19 E-value: 4.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAV-QADIIFSCLPTSTEVENLIAQVQ---- 79
Cdd:COG2084 4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAaAADVVITMLPDDAAVEEVLLGEDglla 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 80 -LKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHVGE 158
Cdd:COG2084 84 aLRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 159 PGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPqRVLNRAFPNTFALPLLAKDTG 238
Cdd:COG2084 164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-RMLAGDFDPGFALDLMLKDLG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1253006089 239 IALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMY 281
Cdd:COG2084 243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-157 |
3.24e-50 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 163.02 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 4 SVAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAVQ-ADIIFSCLPTSTEVENLIAQVQ--- 79
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAgLDVVITMVPAGAAVDAVIFGEGllp 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006089 80 -LKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHVG 157
Cdd:pfam03446 81 gLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-282 |
1.22e-45 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 155.59 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 1 MIQSVAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAE---QHAAEYGTQAVELAQavQADIIFSCLPTSTEV------ 71
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAeviAAGAETASTAKAVAE--QCDVIITMLPNSPHVkevalg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 72 ENLIAQvQLKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGK 151
Cdd:PRK11559 79 ENGIIE-GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 152 VIQHVGEPGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPqRVLNRAFPNTFALP 231
Cdd:PRK11559 158 SVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRID 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1253006089 232 LLAKDTGIALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMYE 282
Cdd:PRK11559 237 LHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYE 287
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
160-281 |
4.87e-36 |
|
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.
Pssm-ID: 434252 [Multi-domain] Cd Length: 122 Bit Score: 125.33 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 160 GAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPQRVLNRAFPNTFALPLLAKDTGI 239
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQRVLSRDFDPGFALDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1253006089 240 ALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMY 281
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
5-286 |
1.76e-33 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 123.98 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVwnRNFAKAEQHAAEYGTQAVELAQAV--QADIIFSCLPTSTEVENLI------A 76
Cdd:PRK15059 3 LGFIGLGIMGTPMAINLARAGHQLHV--TTIGPVADELLSLGAVSVETARQVteASDIIFIMVPDTPQVEEVLfgengcT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 77 QVQLKaGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHV 156
Cdd:PRK15059 81 KASLK-GKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 157 GEPGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEmILPQRVLNRAFPNTFALPLLAKD 236
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILE-VHGERMIKRTFNPGFKIALHQKD 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1253006089 237 TGIALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMYELWSN 286
Cdd:PRK15059 239 LNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMAN 288
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
5-275 |
6.86e-30 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 114.57 E-value: 6.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNRNfAKAEQHAAEYGTQAVELAQ--AVQADIIFSCLPTSTEVENLIAQVQ--- 79
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVN-PQAVDALVDKGATPAASPAqaAAGAEFVITMLPNGDLVRSVLFGENgvc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 80 --LKAGSVWVDCTSGVPESAKKLVQQLEAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVIQHVG 157
Cdd:PRK15461 83 egLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 158 EPGAGFAVKAVNNmLMAVSLCA-AAEGFTTLKAHGVNLNQALQCINAS-SGKSAVTeMILPQRVLNRAFPNTFALPLLAK 235
Cdd:PRK15461 163 GPGMGIRVKLINN-YMSIALNAlSAEAAVLCEALGLSFDVALKVMSGTaAGKGHFT-TTWPNKVLKGDLSPAFMIDLAHK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1253006089 236 DTGIALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFS 275
Cdd:PRK15461 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWS 280
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
2-290 |
1.81e-26 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 109.17 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 2 IQSVAFIGLGAMGYRMAAHLPKH------FDtvyVWNRNFAKAEQHAAEYGTQAVELAQAVqaDIIFSCLPTSTEVENLI 75
Cdd:PLN02858 324 VKRIGFIGLGAMGFGMASHLLKSnfsvcgYD---VYKPTLVRFENAGGLAGNSPAEVAKDV--DVLVIMVANEVQAENVL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 76 -----AQVQLKAGSVWVDCTSGVPESAKKLVQQLEAQ--QIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQA 148
Cdd:PLN02858 399 fgdlgAVSALPAGASIVLSSTVSPGFVIQLERRLENEgrDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 149 FGKVIQHV-GEPGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPqRVLNRAFPNT 227
Cdd:PLN02858 479 LSEKLYVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVP-HMLDNDYTPY 557
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253006089 228 FALPLLAKDTGIALDLVHEAALPAPVLALTQSLIQAANLTAEKDSDFSTAVKMYELWSNITLE 290
Cdd:PLN02858 558 SALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVE 620
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
5-195 |
4.89e-22 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 93.23 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNRNfAKAEQHAAEYGTQAV----ELAQAVQA-DIIFSCLPTSTEVENLIAQVQ 79
Cdd:COG1023 3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRN-PEAVAALAAEGATGAdsleELVAKLPApRVVWLMVPAGEITDQVIEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 80 --LKAGSVWVDctsG--------VPESAkklvqQLEAQQIDFLDAPVSGQTIGAEN-ATLtvMIGGKAAAFEKALPAIQA 148
Cdd:COG1023 82 plLEPGDIVID---GgnsnykddIRRAE-----ELAEKGIHFVDVGTSGGVWGLENgYCL--MIGGDKEAVERLEPIFKA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006089 149 ------FGKViqHVGEPGAGFAVKAVNN----MLMAvslcAAAEGFTTLKAHGVNLN 195
Cdd:COG1023 152 lapgaeNGYL--HCGPVGAGHFVKMVHNgieyGMMQ----AYAEGFELLEASEFDLD 202
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
5-282 |
3.48e-21 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 93.38 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNrNFAKAEQHAAEYG----TQAVELAQAVQADIIFscLPTSTEVENLIAQVQ- 79
Cdd:PLN02858 7 VGFVGLDSLSFELASSLLRSGFKVQAFE-ISTPLMEKFCELGghrcDSPAEAAKDAAALVVV--LSHPDQVDDVFFGDEg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 80 ----LKAGSVWVDCTSGVPESAKKLVQQL--EAQQIDFLDAPVSGQTIGAENATLTVMIGGKAAAFEKALPAIQAFGKVI 153
Cdd:PLN02858 84 aakgLQKGAVILIRSTILPLQLQKLEKKLteRKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 154 QHV-GEPGAGFAVKAVNNMLMAVSLCAAAEGFTTLKAHGVNLNQALQCINASSGKSAVTEMILPQRVLNRAFPNTFaLPL 232
Cdd:PLN02858 164 YTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRF-LNV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1253006089 233 LAKDTGIALDLVHEAALPAPVLALT-QSLIQAANlTAEKDSDFSTAVKMYE 282
Cdd:PLN02858 243 LVQNLGIVLDMAKSLPFPLPLLAVAhQQLISGSS-SMQGDDTATSLAKVWE 292
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
5-195 |
1.93e-20 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 88.65 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQhAAEYGTQAV----ELAQAVQAD-IIFSCLPTSTEVENLIAQV- 78
Cdd:PRK09599 3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEA-LAEEGATGAdsleELVAKLPAPrVVWLMVPAGEITDATIDELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 79 -QLKAGSVWVD-CTSGVPESAKKlVQQLEAQQIDFLDAPVSGQTIGAEN-ATLtvMIGGKAAAFEKALPAIQA------F 149
Cdd:PRK09599 82 pLLSPGDIVIDgGNSYYKDDIRR-AELLAEKGIHFVDVGTSGGVWGLERgYCL--MIGGDKEAVERLEPIFKAlapraeD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1253006089 150 GKViqHVGEPGAGFAVKAVNN----MLMAvslcAAAEGFTTLKAHGVNLN 195
Cdd:PRK09599 159 GYL--HAGPVGAGHFVKMVHNgieyGMMQ----AYAEGFELLEASRFDLD 202
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
3-64 |
6.41e-09 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 56.35 E-value: 6.41e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006089 3 QSVAFIGLGAMGYRMAAHLP-KHFDTVYVWNRNFAKAEQHAAEYGTQAV---ELAQAV-QADIIFSC 64
Cdd:PRK00045 183 KKVLVIGAGEMGELVAKHLAeKGVRKITVANRTLERAEELAEEFGGEAIpldELPEALaEADIVISS 249
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
3-64 |
1.82e-08 |
|
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 54.73 E-value: 1.82e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006089 3 QSVAFIGLGAMGYRMAAHLPKH-FDTVYVWNRNFAKAEQHAAEYGTQAVELAQ----AVQADIIFSC 64
Cdd:COG0373 183 KTVLVIGAGEMGELAARHLAAKgVKRITVANRTLERAEELAEEFGGEAVPLEElpeaLAEADIVISS 249
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
5-88 |
2.16e-06 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 48.03 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 5 VAFIGLGAMGYRMAAHL-PKHFDTVYVWNRNFAKAEQHAAEYGTQAVELAQAV----QADIIFSCLPTST---EVENLIA 76
Cdd:cd05213 181 VLVIGAGEMGELAAKHLaAKGVAEITIANRTYERAEELAKELGGNAVPLDELLellnEADVVISATGAPHyakIVERAMK 260
|
90
....*....|..
gi 1253006089 77 QVQLKAgSVWVD 88
Cdd:cd05213 261 KRSGKP-RLIVD 271
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
3-75 |
2.44e-05 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 44.02 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1253006089 3 QSVAFIGLGAMGYRMAAHLpKHFD-TVYVWNRnFAKAEQHAAEYGTQAVELAQAV-QADIIFSCLPTSTEVENLI 75
Cdd:pfam02826 37 KTVGIIGLGRIGRAVAKRL-KAFGmKVIAYDR-YPKPEEEEEELGARYVSLDELLaESDVVSLHLPLTPETRHLI 109
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-64 |
5.25e-05 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 43.90 E-value: 5.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006089 1 MIQSVAFIGLGAMGYRMAAHLPKHF---DTVYVWNRNFAKAEQHAAEYGTQAVELAQAV--QADIIFSC 64
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERYGVRVTTDNAEAaaQADVVVLA 69
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
5-69 |
1.17e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 42.99 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1253006089 5 VAFIGLGAMGYRMAAHLPKH--FDTVYVWNRNFAKAEQHAAEYGTQAV----ELAQAVQADIIFSCLPTST 69
Cdd:COG0673 6 VGIIGAGGIGRAHAPALAALpgVELVAVADRDPERAEAFAEEYGVRVYtdyeELLADPDIDAVVIATPNHL 76
|
|
| PRK06141 |
PRK06141 |
ornithine cyclodeaminase family protein; |
16-106 |
1.88e-04 |
|
ornithine cyclodeaminase family protein;
Pssm-ID: 180421 Cd Length: 314 Bit Score: 42.20 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 16 RMAAHLPK-H-----FDTVYVWNRNFAKAEQHAAEYGTQ------AVELAQAV-QADIIfSCLPTSTevENLIAQVQLKA 82
Cdd:PRK06141 135 RLASLLALaHasvrpIKQVRVWGRDPAKAEALAAELRAQgfdaevVTDLEAAVrQADII-SCATLST--EPLVRGEWLKP 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1253006089 83 G------------------------SVWVDCTSGVPESAKKLVQQLEA 106
Cdd:PRK06141 212 GthldlvgnftpdmrecddeairraSVYVDTRAGALAEAGDLLIPIAE 259
|
|
| OCDMu |
COG2423 |
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ... |
3-70 |
8.09e-04 |
|
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 441972 [Multi-domain] Cd Length: 322 Bit Score: 40.51 E-value: 8.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006089 3 QSVAFIGLGAMGYRMAAHLPKHFD--TVYVWNRNFAKAEQHAAEYGTQAVE------LAQAV-QADIIfSCLPTSTE 70
Cdd:COG2423 128 RTLGIIGAGVQARTQLRALAAVRPieRVRVWGRDPEKAEAFAARLAAEGLPveaaddLEEAVaDADII-VTATPSRE 203
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-92 |
1.95e-03 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 39.20 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 1 MIQSVAFIGLGAMGYRMAAHLPKHFDTVYVWNRNfakaeqhaaeygtQAVELAQAVQ-ADIIFSCLPTS--TEVENLIAQ 77
Cdd:PRK14619 3 QPKTIAILGAGAWGSTLAGLASANGHRVRVWSRR-------------SGLSLAAVLAdADVIVSAVSMKgvRPVAEQVQA 69
|
90
....*....|....*
gi 1253006089 78 VQLKAGSVWVDCTSG 92
Cdd:PRK14619 70 LNLPPETIIVTATKG 84
|
|
| PGDH_1 |
cd12155 |
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ... |
3-113 |
3.29e-03 |
|
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240632 [Multi-domain] Cd Length: 314 Bit Score: 38.33 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 3 QSVAFIGLGAMGYRMAAHLpKHFDtVYVW--NRNfakaeQHAAEYGTQAVELAQ----AVQADIIFSCLPTSTEVENLIA 76
Cdd:cd12155 136 KTILFLGTGSIGQEIAKRL-KAFG-MKVIgvNTS-----GRDVEYFDKCYPLEEldevLKEADIVVNVLPLTEETHHLFD 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1253006089 77 QV---QLKAGSVWVDCTSG--VPESAkkLVQQLEAQQIDF--LD 113
Cdd:cd12155 209 EAffeQMKKGALFINVGRGpsVDEDA--LIEALKNKQIRGaaLD 250
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
9-91 |
5.98e-03 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 38.04 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006089 9 GLGAMGYRMAAHLPKHFDTVYVWNRNFAKAEQHAAEYGTQAVE--LAQAVQADIIFSCLPTSTeVENLIAQV--QLKAGS 84
Cdd:PRK08655 8 GTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANdnIDAAKDADIVIISVPINV-TEDVIKEVapHVKEGS 86
|
....*..
gi 1253006089 85 VWVDCTS 91
Cdd:PRK08655 87 LLMDVTS 93
|
|
| formate_dh_like |
cd05198 |
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
3-75 |
9.10e-03 |
|
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 37.22 E-value: 9.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1253006089 3 QSVAFIGLGAMGyRMAAHLPKHFD-TVYVWNRnFAKAEQHAAEyGTQAVELAQAV-QADIIFSCLPTSTEVENLI 75
Cdd:cd05198 141 KTVGIVGLGRIG-QRVAKRLQAFGmKVLYYDR-TRKPEPEEDL-GFRVVSLDELLaQSDVVVLHLPLTPETRHLI 212
|
|
| |
