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Conserved domains on  [gi|446534222|ref|WP_000611568|]
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MULTISPECIES: 2,7-anhydro-N-acetylneuraminate hydratase [Enterobacteriaceae]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-249 1.65e-69

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.18  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   1 MINYGVVGVGYFGAELARFMNMHDNAKITCVYD--PENGENIARELQCINMSSLDALVSSKLVDCVIVATPNYLHKEPVI 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADrdPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  79 KAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCHTKRNGWeNKQERL 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHP-RPAGPA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 159 SWKKMKEQSGG--HLYHHIHELDCVQHLLGEIPETVTMIGGNLAHSGPGFgneDDMLFMTLEFPSGKLATLE--WGSAFN 234
Cdd:COG0673  162 DWRFDPELAGGgaLLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEasWVAPGG 238
                        250
                 ....*....|....*
gi 446534222 235 WPEHYVIINGTKGSI 249
Cdd:COG0673  239 ERDERLEVYGTKGTL 253
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-249 1.65e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.18  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   1 MINYGVVGVGYFGAELARFMNMHDNAKITCVYD--PENGENIARELQCINMSSLDALVSSKLVDCVIVATPNYLHKEPVI 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADrdPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  79 KAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCHTKRNGWeNKQERL 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHP-RPAGPA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 159 SWKKMKEQSGG--HLYHHIHELDCVQHLLGEIPETVTMIGGNLAHSGPGFgneDDMLFMTLEFPSGKLATLE--WGSAFN 234
Cdd:COG0673  162 DWRFDPELAGGgaLLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEasWVAPGG 238
                        250
                 ....*....|....*
gi 446534222 235 WPEHYVIINGTKGSI 249
Cdd:COG0673  239 ERDERLEVYGTKGTL 253
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
130-362 2.50e-56

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 183.00  E-value: 2.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  130 RKLIKEGVIGEILSCHT-KRNGWENKQERLSWKKMKEQSGGHLYHH-IHELDCVQHLLGEIPETVTMIGGnlahsgpgfg 207
Cdd:pfam02894   1 KELIENGVLGEVVMVTVhTRDPFRPPQEFKRWRVDPEKSGGALYDLgIHTIDLLIYLFGEPPSVVAVYAS---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  208 neDDMLFMTLEFPSGKLATLEW--GSAFNWPEHYVIINGTKGSIKIDMQEtagslriGGQTKHFLVHETQEEDDDRRkgn 285
Cdd:pfam02894  71 --EDTAFATLEFKNGAVGTLETsgGSIVEANGHRISIHGTKGSIELDGID-------DGLLSVTVVGEPGWATDDPM--- 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446534222  286 mtsemdgaiaYGHPGKKTPLWLASLIRKETLFLHNILCGakPEEDYIDLLNGEAAMSAIATADAATLSRSQDRKVKI 362
Cdd:pfam02894 139 ----------VRKGGDEVPEFLGSFAGGYLLEYDAFLEA--VRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-254 1.05e-27

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 111.16  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222    1 MINYGVVGVGYFG---AE-LARFMnmhDNAKITCVYDP--ENGENIARELQCINM-SSLDALVSSKLVDCVIVATPNYLH 73
Cdd:TIGR04380   1 KLKVGIIGAGRIGkvhAEnLATHV---PGARLKAIVDPfaDAAAELAEKLGIEPVtQDPEAALADPEIDAVLIASPTDTH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   74 KEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCH-TKRNgwe 152
Cdd:TIGR04380  78 ADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRiTSRD--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  153 nkQERLSWKKMKEQSGGHLYHHIHELDCVQHLLGEIPETVTMIGGNLAHsgPGFGNEDDM--LFMTLEFPSGKLATLE-- 228
Cdd:TIGR04380 155 --PAPPPVAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVD--PAIGEAGDVdtAVITLKFENGAIAVIDns 230
                         250       260
                  ....*....|....*....|....*.
gi 446534222  229 WGSAFNWpEHYVIINGTKGSIKIDMQ 254
Cdd:TIGR04380 231 RRAAYGY-DQRVEVFGSKGMLRAEND 255
XylDh_Gfo6_Halo NF041392
D-xylose 1-dehydrogenase Gfo6;
62-145 1.46e-16

D-xylose 1-dehydrogenase Gfo6;


Pssm-ID: 469283 [Multi-domain]  Cd Length: 350  Bit Score: 79.97  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  62 DCVIVATPNYLHKEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEI 141
Cdd:NF041392  84 DAVYVCTPNALHLEYVETAAELGKAVLCEKPMEATVERAERMVEACEDADVPLMVAYRMHTEPAVRRARELIRDGFIGDP 163

                 ....
gi 446534222 142 LSCH 145
Cdd:NF041392 164 VQVH 167
PRK11579 PRK11579
putative oxidoreductase; Provisional
49-255 3.96e-05

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 45.09  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  49 MSSLDALVSSKLVDCVIVATPNYLHKePVIKAAKNK-KHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQ 127
Cdd:PRK11579  53 VSEPQHLFNDPNIDLIVIPTPNDTHF-PLAKAALEAgKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 128 YARKLIKEGVIGEI--LSCHTKRNgweNKQERLSWKKMKEQSGGHLYH-HIHELDCVQHLLGeIPETVTMiggNLAHSGP 204
Cdd:PRK11579 132 TLKALLAEGVLGEVayFESHFDRF---RPQVRQRWREQGGPGSGIWYDlAPHLLDQAIQLFG-LPVSITV---DLAQLRP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446534222 205 GfGNEDDMLFMTLEFPSGK-------LATLEwgSAfnwpeHYvIINGTKGS-IK--IDMQE 255
Cdd:PRK11579 205 G-AQSTDYFHAILSYPQRRvvlhgtmLAAAE--SA-----RY-IVHGSRGSyVKygLDPQE 256
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
6-116 3.62e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.60  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   6 VVGVGYFGAELARFMNMHDNAKITCVYD--PEN-----GENIARELQCINMSS-LDALVSSKLVDCVIVATPNYLHK-EP 76
Cdd:cd24146    5 VWGLGAMGRGIARYLLEKPGLEIVGAVDrdPAKvgkdlGELGGGAPLGVKVTDdLDAVLAATKPDVVVHATTSFLADvAP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446534222  77 VIK-AAKNKKHVF--CEKPI--ALSYEDCVDMV-KACKEAGVTFMA 116
Cdd:cd24146   85 QIErLLEAGLNVIttCEELFypWARDPELAEELdALAKENGVTVLG 130
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-249 1.65e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.18  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   1 MINYGVVGVGYFGAELARFMNMHDNAKITCVYD--PENGENIARELQCINMSSLDALVSSKLVDCVIVATPNYLHKEPVI 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADrdPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  79 KAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCHTKRNGWeNKQERL 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHP-RPAGPA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 159 SWKKMKEQSGG--HLYHHIHELDCVQHLLGEIPETVTMIGGNLAHSGPGFgneDDMLFMTLEFPSGKLATLE--WGSAFN 234
Cdd:COG0673  162 DWRFDPELAGGgaLLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEasWVAPGG 238
                        250
                 ....*....|....*
gi 446534222 235 WPEHYVIINGTKGSI 249
Cdd:COG0673  239 ERDERLEVYGTKGTL 253
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
130-362 2.50e-56

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 183.00  E-value: 2.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  130 RKLIKEGVIGEILSCHT-KRNGWENKQERLSWKKMKEQSGGHLYHH-IHELDCVQHLLGEIPETVTMIGGnlahsgpgfg 207
Cdd:pfam02894   1 KELIENGVLGEVVMVTVhTRDPFRPPQEFKRWRVDPEKSGGALYDLgIHTIDLLIYLFGEPPSVVAVYAS---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  208 neDDMLFMTLEFPSGKLATLEW--GSAFNWPEHYVIINGTKGSIKIDMQEtagslriGGQTKHFLVHETQEEDDDRRkgn 285
Cdd:pfam02894  71 --EDTAFATLEFKNGAVGTLETsgGSIVEANGHRISIHGTKGSIELDGID-------DGLLSVTVVGEPGWATDDPM--- 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446534222  286 mtsemdgaiaYGHPGKKTPLWLASLIRKETLFLHNILCGakPEEDYIDLLNGEAAMSAIATADAATLSRSQDRKVKI 362
Cdd:pfam02894 139 ----------VRKGGDEVPEFLGSFAGGYLLEYDAFLEA--VRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
2-118 8.47e-40

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 137.34  E-value: 8.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222    2 INYGVVGVGYFGAELAR-FMNMHDNAKITCVYDP--ENGENIARELQCINMSSLDALVSSKLVDCVIVATPNYLHKEPVI 78
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARaLNASQPGAELVAILDPnsERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446534222   79 KAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGH 118
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-254 1.05e-27

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 111.16  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222    1 MINYGVVGVGYFG---AE-LARFMnmhDNAKITCVYDP--ENGENIARELQCINM-SSLDALVSSKLVDCVIVATPNYLH 73
Cdd:TIGR04380   1 KLKVGIIGAGRIGkvhAEnLATHV---PGARLKAIVDPfaDAAAELAEKLGIEPVtQDPEAALADPEIDAVLIASPTDTH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   74 KEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCH-TKRNgwe 152
Cdd:TIGR04380  78 ADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRiTSRD--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  153 nkQERLSWKKMKEQSGGHLYHHIHELDCVQHLLGEIPETVTMIGGNLAHsgPGFGNEDDM--LFMTLEFPSGKLATLE-- 228
Cdd:TIGR04380 155 --PAPPPVAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVD--PAIGEAGDVdtAVITLKFENGAIAVIDns 230
                         250       260
                  ....*....|....*....|....*.
gi 446534222  229 WGSAFNWpEHYVIINGTKGSIKIDMQ 254
Cdd:TIGR04380 231 RRAAYGY-DQRVEVFGSKGMLRAEND 255
XylDh_Gfo6_Halo NF041392
D-xylose 1-dehydrogenase Gfo6;
62-145 1.46e-16

D-xylose 1-dehydrogenase Gfo6;


Pssm-ID: 469283 [Multi-domain]  Cd Length: 350  Bit Score: 79.97  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  62 DCVIVATPNYLHKEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEI 141
Cdd:NF041392  84 DAVYVCTPNALHLEYVETAAELGKAVLCEKPMEATVERAERMVEACEDADVPLMVAYRMHTEPAVRRARELIRDGFIGDP 163

                 ....
gi 446534222 142 LSCH 145
Cdd:NF041392 164 VQVH 167
PRK11579 PRK11579
putative oxidoreductase; Provisional
49-255 3.96e-05

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 45.09  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  49 MSSLDALVSSKLVDCVIVATPNYLHKePVIKAAKNK-KHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQ 127
Cdd:PRK11579  53 VSEPQHLFNDPNIDLIVIPTPNDTHF-PLAKAALEAgKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 128 YARKLIKEGVIGEI--LSCHTKRNgweNKQERLSWKKMKEQSGGHLYH-HIHELDCVQHLLGeIPETVTMiggNLAHSGP 204
Cdd:PRK11579 132 TLKALLAEGVLGEVayFESHFDRF---RPQVRQRWREQGGPGSGIWYDlAPHLLDQAIQLFG-LPVSITV---DLAQLRP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446534222 205 GfGNEDDMLFMTLEFPSGK-------LATLEwgSAfnwpeHYvIINGTKGS-IK--IDMQE 255
Cdd:PRK11579 205 G-AQSTDYFHAILSYPQRRvvlhgtmLAAAE--SA-----RY-IVHGSRGSyVKygLDPQE 256
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
6-116 3.62e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.60  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   6 VVGVGYFGAELARFMNMHDNAKITCVYD--PEN-----GENIARELQCINMSS-LDALVSSKLVDCVIVATPNYLHK-EP 76
Cdd:cd24146    5 VWGLGAMGRGIARYLLEKPGLEIVGAVDrdPAKvgkdlGELGGGAPLGVKVTDdLDAVLAATKPDVVVHATTSFLADvAP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446534222  77 VIK-AAKNKKHVF--CEKPI--ALSYEDCVDMV-KACKEAGVTFMA 116
Cdd:cd24146   85 QIErLLEAGLNVIttCEELFypWARDPELAEELdALAKENGVTVLG 130
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
6-115 4.34e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 39.50  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222    6 VVGVGYFGAELARFMNMH-DNAKITCV-YDPENGENIARELQCINM-----------SSLDALVSSklVDCVIVATPNYL 72
Cdd:pfam03435   3 IIGAGSVGQGVAPLLARHfDVDRITVAdRTLEKAQALAAKLGGVRFiavavdadnyeAVLAALLKE--GDLVVNLSPPTL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446534222   73 HkEPVIKAA-KNKKHVFCekpIALSYEDCVDMVKACKEAGVTFM 115
Cdd:pfam03435  81 S-LDVLKACiETGVHYVD---TSYLREAVLALHEKAKDAGVTAV 120
PRK10206 PRK10206
putative oxidoreductase; Provisional
50-263 4.85e-04

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 41.73  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222  50 SSLDALVSSKLVDCVIVATPNYLHKEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYA 129
Cdd:PRK10206  54 SDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222 130 RKLIKEGVIGEILSCHTKRNGWENKQERlswKKMKEQSGGHLYHHIHELDCVQHLLGEiPETVTMIGGNLAHSgpgfGNE 209
Cdd:PRK10206 134 KKAIESGKLGEIVEVESHFDYYRPVAET---KPGLPQDGAFYGLGVHTMDQIISLFGR-PDHVAYDIRSLRNK----ANP 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446534222 210 DDMLFMTLEFPSGKlATLEWGSAFNWPEHYVIINGTKGS-IK--IDMQETagSLRIG 263
Cdd:PRK10206 206 DDTFEAQLFYGDLK-AIVKTSHLVKIDYPKFIVHGKKGSfIKygIDQQET--SLKAN 259
PRK13304 PRK13304
aspartate dehydrogenase;
1-87 1.19e-03

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 40.36  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   1 MINYGVVGVGYFGAELARF-MNMHDNAKITCVYDP--ENGENIARELQCINMSSLDALVssKLVDCVI-VATPNYLhKEP 76
Cdd:PRK13304   1 MLKIGIVGCGAIASLITKAiLSGRINAELYAFYDRnlEKAENLASKTGAKACLSIDELV--EDVDLVVeCASVNAV-EEV 77
                         90
                 ....*....|.
gi 446534222  77 VIKAAKNKKHV 87
Cdd:PRK13304  78 VPKSLENGKDV 88
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
2-88 2.35e-03

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467521 [Multi-domain]  Cd Length: 170  Bit Score: 38.56  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534222   2 INYGVVGV-GYFGAELARFMNMHDNAKITCVY-DPENGENIA------RELQCINMSSLDALVSSKLVDCVIVATPNYLH 73
Cdd:cd17895    1 IKVGIIGAsGYTGAELLRLLLNHPEVEIVALTsRSYAGKPVSevfphlRGLTDLTFEPDDDEEIAEDADVVFLALPHGVS 80
                         90
                 ....*....|....*
gi 446534222  74 KEPVIKAAKNKKHVF 88
Cdd:cd17895   81 MELAPKLLEAGVKVI 95
 
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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