|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
9-297 |
2.90e-59 |
|
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.
Pssm-ID: 188641 [Multi-domain] Cd Length: 288 Bit Score: 191.37 E-value: 2.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 9 RGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:cd00954 2 KGLIAALLTPF--DENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKG-KVTLIAHVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIvSKSAPNTPLLYYHIPKASMVNIHMGKFLQTVEerI 167
Cdd:cd00954 79 SLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREI-IAAAASLPMIIYHIPALTGVNLTLEQFLELFE--I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 168 PTFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTN 245
Cdd:cd00954 156 PNVIGVKFTATDLYD-LERIRAasPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFN-AGDIDTAREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156551613 246 QEFINKTVKAITHFGTwVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00954 234 QHVINDVITVLIKNGL-YPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAK 283
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
8-305 |
8.79e-53 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 174.96 E-value: 8.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:COG0329 2 FRGVIPALVTPF--DADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAG-RVPVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTsVEDLIEYLSIVSKSAPnTPLLYYHIPKASMVNIHMgkflQTVEE-- 165
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKPT-QEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSP----ETLARla 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMRA-NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLE-FGKGNRDLkiAR 243
Cdd:COG0329 153 EIPNIVGIKEASGDLDRIAELIRAtGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEaALAGDLAE--AR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156551613 244 TNQEFINKTVKAITHFGTWVeTMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNLAEIGL 305
Cdd:COG0329 231 ALQDRLLPLIRALFAEGNPA-PVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
8-256 |
2.44e-31 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 118.62 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFNNDANrsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKeTKQHLMVQIG 87
Cdd:pfam00701 2 FSGIITALVTPFDTDGT--LDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAK-GRIPVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPtSVEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE-- 165
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKP-SQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLT----PETVGRla 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIART 244
Cdd:pfam00701 153 TNPNIVGIKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALK-NGDLATAAL 231
|
250
....*....|..
gi 156551613 245 NQEFINKTVKAI 256
Cdd:pfam00701 232 INHKLLPLIKIL 243
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
8-309 |
8.80e-30 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 114.71 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQI 86
Cdd:PRK04147 4 LKGVYAALLTPFDEDG--QIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKG-KVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 87 GGTSLNDVKELAAHAEKLGVNSLLCLPELYFkPTSVEDLIEYLSIVSKSAPNtPLLYYHIPKASMVNIHMGKFLQTVEer 166
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 167 IPTFSGIKFTSNDLeegFEAMRANKRFA---VFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNrDLKIAR 243
Cdd:PRK04147 157 LPKVIGVKQTAGDL---YQLERIRKAFPdklIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAG-DIQEAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156551613 244 TNQEFINKTVKAITHFGTWVETMKIAMSMTTNlfMGPPRAPLklisRESVEKMKTNLAEIGLKVNQ 309
Cdd:PRK04147 233 ELQHECNDVIDLLIKNGVYPGLKEILHYMGVD--AGLCRKPF----KPVDEKYLPALKALAAKYLK 292
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-302 |
1.37e-19 |
|
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129757 [Multi-domain] Cd Length: 285 Bit Score: 86.61 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 10 GLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVqIGGT 89
Cdd:TIGR00674 1 GVITALITPFKEDG--SVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEF---VVDLVNGRVPV-IAGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 90 SLNDVKE---LAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSKSApNTPLLYYHIPKASMVNIhmgkFLQTVEE- 165
Cdd:TIGR00674 75 GSNATEEaisLTKFAEDVGADGFLVVTPYYNKPTQ-EGLYQHFKAIAEEV-DLPIILYNVPSRTGVSL----YPETVKRl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 -RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgnrdlkiAR 243
Cdd:TIGR00674 149 aEEPNIVAIKEATGNLERISEIKAiAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVN----------NA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156551613 244 TNQEFInktvKAITHFGTWVETMKiAMSMTTN------------LFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:TIGR00674 219 LEGDFA----EAREIHQKLMPLHK-ALFIETNpipvktalallgLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
9-297 |
2.90e-59 |
|
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.
Pssm-ID: 188641 [Multi-domain] Cd Length: 288 Bit Score: 191.37 E-value: 2.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 9 RGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:cd00954 2 KGLIAALLTPF--DENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKG-KVTLIAHVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIvSKSAPNTPLLYYHIPKASMVNIHMGKFLQTVEerI 167
Cdd:cd00954 79 SLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREI-IAAAASLPMIIYHIPALTGVNLTLEQFLELFE--I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 168 PTFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTN 245
Cdd:cd00954 156 PNVIGVKFTATDLYD-LERIRAasPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFN-AGDIDTAREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156551613 246 QEFINKTVKAITHFGTwVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00954 234 QHVINDVITVLIKNGL-YPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAK 283
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
8-305 |
8.79e-53 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 174.96 E-value: 8.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:COG0329 2 FRGVIPALVTPF--DADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAG-RVPVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTsVEDLIEYLSIVSKSAPnTPLLYYHIPKASMVNIHMgkflQTVEE-- 165
Cdd:COG0329 79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKPT-QEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSP----ETLARla 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMRA-NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLE-FGKGNRDLkiAR 243
Cdd:COG0329 153 EIPNIVGIKEASGDLDRIAELIRAtGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEaALAGDLAE--AR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156551613 244 TNQEFINKTVKAITHFGTWVeTMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNLAEIGL 305
Cdd:COG0329 231 ALQDRLLPLIRALFAEGNPA-PVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
11-297 |
4.26e-48 |
|
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.
Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 162.33 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 11 LIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKETKQhLMVQIGGTS 90
Cdd:cd00408 1 VIPALVTPFTADG--EVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVP-VIAGVGANS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 91 LNDVKELAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE--RIP 168
Cdd:cd00408 78 TREAIELARHAEEAGADGVLVVPPYYNKPSQ-EGIVAHFKAVA-DASDLPVILYNIPGRTGVDLS----PETIARlaEHP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 169 TFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTNQ 246
Cdd:cd00408 152 NIVGIKDSSGDLDR-LTRLIAllGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAAR-AGDLEEARALQ 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156551613 247 EFINKTVKAITHFGtWVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00408 230 DRLLPLIEALFKEG-NPAPVKAALAL-LGLDAGPVRLPLVPLSEEERAKLE 278
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-302 |
1.56e-31 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 119.02 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 12 IVPVFSPFNNdaNRsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaaAVKETKQHLMVQIGGTSL 91
Cdd:cd00953 5 ITPVITPFTG--NK-IDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLK----AYSDITDKVIFQVGSLNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 92 NDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIVSKSapnTPLLYYHIPKASMVNIHmGKFLQTVEERIPTFS 171
Cdd:cd00953 78 EESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISSP---YPTFIYNYPKATGYDIN-ARMAKEIKKAGGDII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 172 GIKFTSNDLEEGFEAMRANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgNRDLKIARTNQEFINK 251
Cdd:cd00953 154 GVKDTNEDISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKD----HVAIEDAFKLQFLINE 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156551613 252 TVKAITHFGTW------VETMKiamsmttNLFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:cd00953 230 VLDASRKYGSWsanyslVKIFQ-------GYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
8-256 |
2.44e-31 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 118.62 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFNNDANrsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKeTKQHLMVQIG 87
Cdd:pfam00701 2 FSGIITALVTPFDTDGT--LDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAK-GRIPVIAGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPtSVEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE-- 165
Cdd:pfam00701 79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKP-SQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLT----PETVGRla 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIART 244
Cdd:pfam00701 153 TNPNIVGIKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALK-NGDLATAAL 231
|
250
....*....|..
gi 156551613 245 NQEFINKTVKAI 256
Cdd:pfam00701 232 INHKLLPLIKIL 243
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
8-309 |
8.80e-30 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 114.71 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQI 86
Cdd:PRK04147 4 LKGVYAALLTPFDEDG--QIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKG-KVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 87 GGTSLNDVKELAAHAEKLGVNSLLCLPELYFkPTSVEDLIEYLSIVSKSAPNtPLLYYHIPKASMVNIHMGKFLQTVEer 166
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 167 IPTFSGIKFTSNDLeegFEAMRANKRFA---VFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNrDLKIAR 243
Cdd:PRK04147 157 LPKVIGVKQTAGDL---YQLERIRKAFPdklIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAG-DIQEAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156551613 244 TNQEFINKTVKAITHFGTWVETMKIAMSMTTNlfMGPPRAPLklisRESVEKMKTNLAEIGLKVNQ 309
Cdd:PRK04147 233 ELQHECNDVIDLLIKNGVYPGLKEILHYMGVD--AGLCRKPF----KPVDEKYLPALKALAAKYLK 292
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
8-300 |
1.27e-25 |
|
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.
Pssm-ID: 188637 [Multi-domain] Cd Length: 284 Bit Score: 103.34 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaAAVKETKQHLMVqIG 87
Cdd:cd00950 1 FGGSITALVTPFKDDG--SVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIE---AVVEAVNGRVPV-IA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 88 GTSLND---VKELAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVE 164
Cdd:cd00950 75 GTGSNNtaeAIELTKRAEKAGADAALVVTPYYNKPSQ-EGLYAHFKAIA-EATDLPVILYNVPGRTGVNIE----PETVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 165 E--RIPTFSGIKFTSNDLEEGFE-AMRANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKI 241
Cdd:cd00950 149 RlaEHPNIVGIKEATGDLDRVSElIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAAL-AGDLEK 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156551613 242 ARTNQEFINKTVKAIthFgtwVET----MKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNL 300
Cdd:cd00950 228 ARELHRKLLPLIKAL--F---AEPnpipVKAALAL-LGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
10-302 |
1.37e-19 |
|
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129757 [Multi-domain] Cd Length: 285 Bit Score: 86.61 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 10 GLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVqIGGT 89
Cdd:TIGR00674 1 GVITALITPFKEDG--SVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEF---VVDLVNGRVPV-IAGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 90 SLNDVKE---LAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSKSApNTPLLYYHIPKASMVNIhmgkFLQTVEE- 165
Cdd:TIGR00674 75 GSNATEEaisLTKFAEDVGADGFLVVTPYYNKPTQ-EGLYQHFKAIAEEV-DLPIILYNVPSRTGVSL----YPETVKRl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 -RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgnrdlkiAR 243
Cdd:TIGR00674 149 aEEPNIVAIKEATGNLERISEIKAiAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVN----------NA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156551613 244 TNQEFInktvKAITHFGTWVETMKiAMSMTTN------------LFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:TIGR00674 219 LEGDFA----EAREIHQKLMPLHK-ALFIETNpipvktalallgLIEGELRLPLTELSEEHRNKLRDVLKD 284
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
14-228 |
3.24e-09 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 57.13 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 14 PVfSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVQIG-GTSLN 92
Cdd:PRK03620 15 PV-TPF--DADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRA---AVETTAGRVPVIAGaGGGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 93 DVKELAAHAEKLGVNSLLCLPElYFKPTSVEDLIEYLSIVSKSApNTPLLYYHipKASMVnihmgkF----LQTVEERIP 168
Cdd:PRK03620 89 QAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKST-DLGVIVYN--RDNAV------LtadtLARLAERCP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156551613 169 TFSGIKFTSNDLEEGFEAMRA-NKRFAVFLG---SDVLMAAGSTIGIDSFIMTSLNFIPEPALE 228
Cdd:PRK03620 159 NLVGFKDGVGDIELMQRIVRAlGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALA 222
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
11-298 |
1.27e-08 |
|
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.
Pssm-ID: 188638 Cd Length: 289 Bit Score: 55.02 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 11 LIVPVfSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaAAVKETKQHLMVQIG-GT 89
Cdd:cd00951 5 LSFPV-THFDADG--SFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVR---AAVEETAGRVPVLAGaGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 90 SLNDVKELAAHAEKLGVNSLLCLPElYFKPTSVEDLIEYLSIVSKSAPnTPLLYYHipKASMVniHMGKFLQTVEERIPT 169
Cdd:cd00951 79 GTATAIAYAQAAEKAGADGILLLPP-YLTEAPQEGLYAHVEAVCKSTD-LGVIVYN--RANAV--LTADSLARLAERCPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 170 FSGIKFTSNDLeegfEAMR-----ANKRFAVFLG---SDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNRDLKI 241
Cdd:cd00951 153 LVGFKDGVGDI----ELMRrivakLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATV 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156551613 242 ARTNQEF------INKTVKaithfGTWVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKT 298
Cdd:cd00951 229 KRLLRDFflpyvdIRNRRK-----GYAVSIVKAGARL-VGRDAGPVRPPLTDLTEEELAQLTA 285
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
10-241 |
2.18e-08 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 54.26 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 10 GLIVPVFSPFNNDANRSLnlsiiPEYAKFLASKNING---VLVNGTTGEGTSLSTNERKKVTetwAAAVKETKQHLMVqI 86
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDL-----EAYDSLVNMQIENGaegLIVGGTTGEGQLMSWDEHIMLI---GHTVNCFGGKIKV-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 87 GGTSLNDVKElAAHAEKLGVN-----SLLCLPelYFKPTSVEDLIEYLSIVsksAPNTPLLYYHIPKASMVNIhmgkfLQ 161
Cdd:PLN02417 75 GNTGSNSTRE-AIHATEQGFAvgmhaALHINP--YYGKTSQEGLIKHFETV---LDMGPTIIYNVPGRTGQDI-----PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 162 TVEERI---PTFSGIK-FTSNDLEEGFeamrANKRFAVFLG-----SDVLMAAGStigiDSFIMTSLNFIPEPALELLEF 232
Cdd:PLN02417 144 EVIFKIaqhPNFAGVKeCTGNDRVKQY----TEKGILLWSGnddecHDARWDYGA----DGVISVTSNLVPGLMHKLMFA 215
|
250
....*....|..
gi 156551613 233 GKG---NRDLKI 241
Cdd:PLN02417 216 GKNkelNDKLLP 227
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
44-149 |
2.44e-05 |
|
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188639 Cd Length: 309 Bit Score: 45.13 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 44 INGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVQIGGTSLN--DVKELAAHAEKLGVNSLLCLPELYFKPTs 121
Cdd:cd00952 43 VDGILTMGTFGECATLTWEEKQAFVAT---VVETVAGRVPVFVGATTLNtrDTIARTRALLDLGADGTMLGRPMWLPLD- 118
|
90 100
....*....|....*....|....*...
gi 156551613 122 VEDLIEYLSIVSKSAPNTPLLYYHIPKA 149
Cdd:cd00952 119 VDTAVQFYRDVAEAVPEMAIAIYANPEA 146
|
|
|