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Conserved domains on  [gi|194375125|dbj|BAG62675|]
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unnamed protein product [Homo sapiens]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 40-193 1.27e-45

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd00954:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 288  Bit Score: 152.46  E-value: 1.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  40 AERLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKTT 119
Cdd:cd00954   67 AKGKVTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLT 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125 120 VE----------------CSGD-------------------------------------GSNWS--------------SG 132
Cdd:cd00954  146 LEqflelfeipnvigvkfTATDlydleriraaspedklvlngfdemllsalalgadgaiGSTYNvngkryrkifeafnAG 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194375125 133 --------QFCIQRFINFVVKLGFgVSQTKAIMTLVsGIPMGPPRLPLqkasREFTDSAEAKLKSLDFL 193
Cdd:cd00954  226 didtarelQHVINDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPL----RKVTEKALAKAKELAAK 288
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 40-193 1.27e-45

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: 152.46  E-value: 1.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  40 AERLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKTT 119
Cdd:cd00954   67 AKGKVTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLT 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125 120 VE----------------CSGD-------------------------------------GSNWS--------------SG 132
Cdd:cd00954  146 LEqflelfeipnvigvkfTATDlydleriraaspedklvlngfdemllsalalgadgaiGSTYNvngkryrkifeafnAG 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194375125 133 --------QFCIQRFINFVVKLGFgVSQTKAIMTLVsGIPMGPPRLPLqkasREFTDSAEAKLKSLDFL 193
Cdd:cd00954  226 didtarelQHVINDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPL----RKVTEKALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 33-121 3.77e-21

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: 88.29  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  33 LTVTRLWAERLD---QVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYH 109
Cdd:COG0329   57 KRVLEAVVEAAAgrvPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYN 134

                         90
                 ....*....|..
gi 194375125 110 IPALTGVKTTVE 121
Cdd:COG0329  135 IPGRTGVDLSPE 146
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 46-121 1.41e-14

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 70.47  E-value: 1.41e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194375125   46 VIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKTTVE 121
Cdd:pfam00701  73 VIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPE 146
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 47-121 9.85e-14

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 68.10  E-value: 9.85e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194375125  47 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKTTVE 121
Cdd:PRK04147  77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLD 149
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 40-193 1.27e-45

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: 152.46  E-value: 1.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  40 AERLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKTT 119
Cdd:cd00954   67 AKGKVTLIAHVGSLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLT 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125 120 VE----------------CSGD-------------------------------------GSNWS--------------SG 132
Cdd:cd00954  146 LEqflelfeipnvigvkfTATDlydleriraaspedklvlngfdemllsalalgadgaiGSTYNvngkryrkifeafnAG 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194375125 133 --------QFCIQRFINFVVKLGFgVSQTKAIMTLVsGIPMGPPRLPLqkasREFTDSAEAKLKSLDFL 193
Cdd:cd00954  226 didtarelQHVINDVITVLIKNGL-YPTLKAILRLM-GLDAGPCRLPL----RKVTEKALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 33-121 3.77e-21

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: 88.29  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  33 LTVTRLWAERLD---QVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYH 109
Cdd:COG0329   57 KRVLEAVVEAAAgrvPVIAGVGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYN 134

                         90
                 ....*....|..
gi 194375125 110 IPALTGVKTTVE 121
Cdd:COG0329  135 IPGRTGVDLSPE 146
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 33-121 7.22e-20

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: 84.91  E-value: 7.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  33 LTVTRLWAERLD---QVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVaAAAPALPFYYYH 109
Cdd:cd00408   53 KEVIEAVVEAVAgrvPVIAGVGANSTREAIELARHAEEAGADGVLVVPPYYNKP-SQEGIVAHFKAV-ADASDLPVILYN 130

                         90
                 ....*....|..
gi 194375125 110 IPALTGVKTTVE 121
Cdd:cd00408  131 IPGRTGVDLSPE 142
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 46-121 1.41e-14

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 70.47  E-value: 1.41e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194375125   46 VIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKTTVE 121
Cdd:pfam00701  73 VIAGVGSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPE 146
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 47-121 9.85e-14

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 68.10  E-value: 9.85e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194375125  47 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKTTVE 121
Cdd:PRK04147  77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLD 149
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 46-121 6.05e-09

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: 54.42  E-value: 6.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194375125  46 VIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKTTVE 121
Cdd:cd00950   72 VIAGTGSNNTAEAIELTKRAEKAGADAALVVTPYYNKP-SQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPE 145
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 44-115 2.13e-06

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: 46.99  E-value: 2.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194375125  44 DQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKEVAAaapALPFYYYHIPALTG 115
Cdd:cd00953   66 DKVIFQVGSLNLEESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISS---PYPTFIYNYPKATG 134
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 34-111 4.86e-03

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: 37.04  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375125  34 TVTRLWAERldqVIIHVGALSL--KESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPALPFYYYHIP 111
Cdd:cd00952   69 TVVETVAGR---VPVFVGATTLntRDTIARTRALLDLGADGTMLGRPMWLPL-DVDTAVQFYRDVAEAVPEMAIAIYANP 144
 
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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