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Conserved domains on  [gi|55725758|emb|CAH89660|]
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hypothetical protein, partial [Pongo abelii]

Protein Classification

dihydrodipicolinate synthase family protein( domain architecture ID 10087124)

dihydrodipicolinate synthase family protein belongs to the pyruvate-dependent class I aldolases

EC:  4.2.1.41|4.1.3.3|4.3.3.7
Gene Ontology:  GO:0009436|GO:0071704

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 10-260 1.09e-84

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: 254.39  E-value: 1.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:cd00408  34 GLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNK--PSQEGI 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00408 112 VAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGP-DFAVLSGDDDLLLPA 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:cd00408 191 LALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLS 270

                       250
                ....*....|.
gi 55725758 250 PAEEEALRMDF 260
Cdd:cd00408 271 EEERAKLEALL 281
 
Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 10-260 1.09e-84

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: 254.39  E-value: 1.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:cd00408  34 GLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNK--PSQEGI 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00408 112 VAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGP-DFAVLSGDDDLLLPA 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:cd00408 191 LALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLS 270

                       250
                ....*....|.
gi 55725758 250 PAEEEALRMDF 260
Cdd:cd00408 271 EEERAKLEALL 281
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 10-257 6.08e-78

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: 237.36  E-value: 6.08e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:COG0329  38 GLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNK--PTQEGL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:COG0329 116 YAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIKEASGDLDRIAELIRATGD-DFAVLSGDDALALPA 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:COG0329 195 LALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLS 274


                ....*...
gi 55725758 250 PAEEEALR 257
Cdd:COG0329 275 EEERAELR 282
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 10-257 3.69e-45

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 153.29  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758    10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRGrmSSAAL 89
Cdd:pfam00701  38 GLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKP--SQEGL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758    90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:pfam00701 116 YQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEASGDLDRMINIKKEAGP-DFVILSGDDETMLPA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQEL 248
Cdd:pfam00701 195 LSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPL 274


                  ....*....
gi 55725758   249 SPAEEEALR 257
Cdd:pfam00701 275 SEEERPELE 283
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 10-257 8.90e-31

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 115.86  E-value: 8.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:PRK04147  41 GLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYP--FSFEEI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGD---VTRIglivhKTRKQDFQVLAGSAGFL 166
Cdd:PRK04147 119 CDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGVKQTAGDlyqLERI-----RKAFPDKLIYNGFDEMF 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  167 MASYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCR 242
Cdd:PRK04147 194 ASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCR 269

                        250
                 ....*....|....*
gi 55725758  243 APLQELSPAEEEALR 257
Cdd:PRK04147 270 KPFKPVDEKYLPALK 284
 
Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 10-260 1.09e-84

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: 254.39  E-value: 1.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:cd00408  34 GLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNK--PSQEGI 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00408 112 VAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSSGDLDRLTRLIALLGP-DFAVLSGDDDLLLPA 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:cd00408 191 LALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLS 270

                       250
                ....*....|.
gi 55725758 250 PAEEEALRMDF 260
Cdd:cd00408 271 EEERAKLEALL 281
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 10-257 6.08e-78

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: 237.36  E-value: 6.08e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:COG0329  38 GLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNK--PTQEGL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:COG0329 116 YAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGIKEASGDLDRIAELIRATGD-DFAVLSGDDALALPA 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELS 249
Cdd:COG0329 195 LALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLS 274


                ....*...
gi 55725758 250 PAEEEALR 257
Cdd:COG0329 275 EEERAELR 282
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 10-257 8.10e-62

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: 196.18  E-value: 8.10e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYyrGRMSSAAL 89
Cdd:cd00950  37 GLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTAEAIELTKRAEKAGADAALVVTPYY--NKPSQEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:cd00950 115 YAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIKEATGDLDRVSELIALCPD-DFAVLSGDDALTLPF 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRL--------IEPNAAvtrrfgipGLKKIMDWFGYYGGPC 241
Cdd:cd00950 194 LALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLlplikalfAEPNPI--------PVKAALALLGLISGEL 265

                       250
                ....*....|....*.
gi 55725758 242 RAPLQELSPAEEEALR 257
Cdd:cd00950 266 RLPLVPLSEELRAKLR 281
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 10-257 3.69e-45

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 153.29  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758    10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRGrmSSAAL 89
Cdd:pfam00701  38 GLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKP--SQEGL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758    90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAGSAGFLMAS 169
Cdd:pfam00701 116 YQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGIKEASGDLDRMINIKKEAGP-DFVILSGDDETMLPA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   170 YALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQEL 248
Cdd:pfam00701 195 LSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPL 274


                  ....*....
gi 55725758   249 SPAEEEALR 257
Cdd:pfam00701 275 SEEERPELE 283
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 10-258 3.50e-44

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: 150.92  E-value: 3.50e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYrgRMSSAAL 89
Cdd:cd00954  38 GLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYY--KFSFEEI 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  90 IHHYTKVADFSP-IPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRkQDFQVLAGSAGFLMA 168
Cdd:cd00954 116 KDYYREIIAAAAsLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGVKFTATDLYDLERIRAASP-EDKLVLNGFDEMLLS 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 169 SYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQEL 248
Cdd:cd00954 195 ALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKV 274

                       250
                ....*....|
gi 55725758 249 SPAEEEALRM 258
Cdd:cd00954 275 TEKALAKAKE 284
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 10-257 8.90e-31

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 115.86  E-value: 8.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRgrMSSAAL 89
Cdd:PRK04147  41 GLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNTAEAQELAKYATELGYDAISAVTPFYYP--FSFEEI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   90 IHHYTKVADFSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGD---VTRIglivhKTRKQDFQVLAGSAGFL 166
Cdd:PRK04147 119 CDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVIGVKQTAGDlyqLERI-----RKAFPDKLIYNGFDEMF 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  167 MASYALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCR 242
Cdd:PRK04147 194 ASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCR 269

                        250
                 ....*....|....*
gi 55725758  243 APLQELSPAEEEALR 257
Cdd:PRK04147 270 KPFKPVDEKYLPALK 284
PLN02417 PLN02417
dihydrodipicolinate synthase
 10-192 1.02e-28

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 110.12  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   10 GFVVQGSNGEFPFLTSSERLEV----VSRVRQAMPknrlLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPcYYrGRMS 85
Cdd:PLN02417  38 GLIVGGTTGEGQLMSWDEHIMLightVNCFGGKIK----VIGNTGSNSTREAIHATEQGFAVGMHAALHINP-YY-GKTS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   86 SAALIHHYTKVADFSPipVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDvTRIGLIVhktrKQDFQVLAGSAG- 164
Cdd:PLN02417 112 QEGLIKHFETVLDMGP--TIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGN-DRVKQYT----EKGILLWSGNDDe 184

                        170       180
                 ....*....|....*....|....*...
gi 55725758  165 FLMASYALGAVGGVCALANVLGAQVCQL 192
Cdd:PLN02417 185 CHDARWDYGADGVISVTSNLVPGLMHKL 212
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 13-257 2.19e-19

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: 85.13  E-value: 2.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  13 VQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAamvvTPCYYRGRMSSAALIHH 92
Cdd:cd00953  39 VAGTTGLGPSLSFQEKLELLKAYSDITDKVIFQVGSLNLEESIELARAAKSFGIYAIAS----LPPYYFPGIPEEWLIKY 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  93 YTKVAdfSPIPVVLYSVPANTGLDLPVDAVVTLSQHP-NIVGMKDSGGDVTRIglIVHKTRKQDFQVLAGSAGFLMASYA 171
Cdd:cd00953 115 FTDIS--SPYPTFIYNYPKATGYDINARMAKEIKKAGgDIIGVKDTNEDISHM--LEYKRLVPDFKVYSGPDSLIFSALR 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 172 LGAVGGVCALANVLGAQVCQLERLCCTgqwEEAQKLQhRLIEPNAAVTRRFG----IPGLKKIMDwfGYYGGPCRAPLQE 247
Cdd:cd00953 191 SGLDGSVAAASNYLPEVFVKIKDHVAI---EDAFKLQ-FLINEVLDASRKYGswsaNYSLVKIFQ--GYDAGEPRPPFYP 264

                       250
                ....*....|
gi 55725758 248 LSPAEEEALR 257
Cdd:cd00953 265 LDEEEEEKLR 274
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 10-244 3.04e-14

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: 70.94  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  10 GFVVQGSNGEFPFLTSSERLEVVSRVRQAMpKNRL-LLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYyrGRMSSAA 88
Cdd:cd00952  45 GILTMGTFGECATLTWEEKQAFVATVVETV-AGRVpVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMW--LPLDVDT 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  89 LIHHYTKVADFSP-IPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSG------GDVT----RIGLIVHktrkqDFQ 157
Cdd:cd00952 122 AVQFYRDVAEAVPeMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKYLGdigallSDLAavkgRMRLLPL-----EDD 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 158 VLAGSAGFLMASYALGAVGGVCALANVLgaqvcQLERLCCTGQWEEAQKLQHRLIEPNAAVTRRFGIP-------GLKKI 230
Cdd:cd00952 197 YYAAARLFPEEVTAFWSSGAACGPAPVT-----ALRDAVATGDWTDARALTDRMRWAAEPLFPRGDFSefskyniALEKA 271

                       250
                ....*....|....*.
gi 55725758 231 -MDWFGYY-GGPCRAP 244
Cdd:cd00952 272 rFDAAGYMrAGPARPP 287
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 15-257 1.41e-09

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: 57.33  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  15 GSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQAtVEMTVSMAQVGADAAMVVTPcyYRGRMSSAALIHHYT 94
Cdd:cd00951  42 GGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGYGTATA-IAYAQAAEKAGADGILLLPP--YLTEAPQEGLYAHVE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  95 KVADFSPIPVVLYSvPANTGLDlpVDAVVTLSQH-PNIVGMKDSGGDVTRIGLIVHKtRKQDFQVLAG--SAGFLMASY- 170
Cdd:cd00951 119 AVCKSTDLGVIVYN-RANAVLT--ADSLARLAERcPNLVGFKDGVGDIELMRRIVAK-LGDRLLYLGGlpTAEVFALAYl 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758 171 ALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRR---FGIPGLKKIMDWFGYYGGPCRAPLQE 247
Cdd:cd00951 195 AMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRLLRDFFLPYVDIRNRrkgYAVSIVKAGARLVGRDAGPVRPPLTD 274

                       250
                ....*....|
gi 55725758 248 LSPAEEEALR 257
Cdd:cd00951 275 LTEEELAQLT 284
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 15-256 4.86e-07

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 49.81  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   15 GSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGcESTQATVEMTVSMAQVGADAAMVVTPcyYRGRMSSAALIHHYT 94
Cdd:PRK03620  49 GGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTAQAIEYAQAAERAGADGILLLPP--YLTEAPQEGLAAHVE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758   95 KVADFSPIPVVLYSvPANTGLDLpvDAVVTLS-QHPNIVGMKDSGGDVTRIGLIVHKTRKqDFQVLAG--SAGFLMASY- 170
Cdd:PRK03620 126 AVCKSTDLGVIVYN-RDNAVLTA--DTLARLAeRCPNLVGFKDGVGDIELMQRIVRALGD-RLLYLGGlpTAEVFAAAYl 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55725758  171 ALGAVGGVCALANVLGAQVCQLERLCCTGQWEEAQKLQHRLIEPNAAVTRR---FGIPGLKKIMDWFGYYGGPCRAPLQE 247
Cdd:PRK03620 202 ALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRLLDDFFLPYVALRNRkkgYAVSIVKAGARLVGLDAGPVRAPLTD 281


                 ....*....
gi 55725758  248 LSPAEEEAL 256
Cdd:PRK03620 282 LTPEELAEL 290
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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