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Conserved domains on  [gi|516233030|ref|WP_017636993|]
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MULTISPECIES: mannitol-1-phosphate 5-dehydrogenase [Staphylococcus]

Protein Classification

mannitol-1-phosphate 5-dehydrogenase( domain architecture ID 11479775)

mannitol-1-phosphate 5-dehydrogenase catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway

EC:  1.1.1.17
Gene Ontology:  GO:0008926|GO:0019594
PubMed:  14367396

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-367 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


:

Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 514.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   1 MKAVHFGAGNIGRGFIGYILADNNIKVTFADVNDEIINALQTEHEYDVILADEAKTTTRVNNVDAINSAKPsDELKQAIL 80
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADE-EAVIEAIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  81 EADLITTAVGVNILPIIAKSFAPYLKEK-----ENHVNIVACENAIMATDTLKKAILDIT-----GPLGDNIHFANSAVD 150
Cdd:PRK02318  80 EADLVTTAVGPNILPFIAPLIAKGLKKRkaqgnTKPLNIIACENMIRGTSFLKKHVLKALsedekAWLEEHVGFVDSAVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 151 RIVPLQKNENILDVMVEPFYEWVVEKDAWYGE--ELDHIKYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQ 228
Cdd:PRK02318 160 RIVPAQKNEDPLDVTVEPFSEWIVDKTQFKGAlpKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAIL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 229 DSTIEAGLRRVLAETSDYITREFDFSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIGPKDRIIKPLNYLYEHNLE 308
Cdd:PRK02318 240 DPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGLP 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516233030 309 RDGLVKAAALLLKYDDKADQETVEKNNYIQEHGVKSFLQTYAKVEG--PLAEEIEKEYNEL 367
Cdd:PRK02318 320 HSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDAdsELVEEIVKAYNAL 380
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-367 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 514.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   1 MKAVHFGAGNIGRGFIGYILADNNIKVTFADVNDEIINALQTEHEYDVILADEAKTTTRVNNVDAINSAKPsDELKQAIL 80
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADE-EAVIEAIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  81 EADLITTAVGVNILPIIAKSFAPYLKEK-----ENHVNIVACENAIMATDTLKKAILDIT-----GPLGDNIHFANSAVD 150
Cdd:PRK02318  80 EADLVTTAVGPNILPFIAPLIAKGLKKRkaqgnTKPLNIIACENMIRGTSFLKKHVLKALsedekAWLEEHVGFVDSAVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 151 RIVPLQKNENILDVMVEPFYEWVVEKDAWYGE--ELDHIKYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQ 228
Cdd:PRK02318 160 RIVPAQKNEDPLDVTVEPFSEWIVDKTQFKGAlpKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAIL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 229 DSTIEAGLRRVLAETSDYITREFDFSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIGPKDRIIKPLNYLYEHNLE 308
Cdd:PRK02318 240 DPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGLP 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516233030 309 RDGLVKAAALLLKYDDKADQETVEKNNYIQEHGVKSFLQTYAKVEG--PLAEEIEKEYNEL 367
Cdd:PRK02318 320 HSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDAdsELVEEIVKAYNAL 380
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
140-322 4.19e-36

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 131.73  E-value: 4.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  140 DNIHFANSAVDRIVP------------LQKNENILDVMVEPFYEWVVEKDAWYGE---ELDHIKYVDDLTPYIERKLLTV 204
Cdd:pfam08125   1 DNVGFPNTMVDRIVPattddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGRpllEKVGVEYVEDVDPYEERKLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  205 NTGHAFLAYAGYNDNKATVLDAVQDSTIEAGLRRVLAETSDYITREFDfsKSEQSQYVEKIIERFNNSYLSDEVTRVGRG 284
Cdd:pfam08125  81 NGGHATLAYLGYLAGYQTIHEAMLDPEIRAFVKGVMTEEVAPLLAKVP--GDDLEAYADKIIERFSNPYIKDTVWRVARD 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 516233030  285 TLRKIgPKdRIIKPLNYLYEHNLERDGLVKAAALLLKY 322
Cdd:pfam08125 159 GSQKL-PQ-RKLPSLRRHIRAGPLPELLALGVAGWMRY 194
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
4-320 7.71e-26

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 108.32  E-value: 7.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   4 VHFGAGNIGRGFIGYIL------ADNNIKVTFADV--NDEIINALQtehEYD-----VILADEAKTTTRVnnVDAINSAK 70
Cdd:COG0246   31 VHFGVGNFHRAHQAWYTdrllnaGDFDWGIVGVGLrsGDALRDALA---AQDglytlVERGPDGVEEARV--IGSISEVL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  71 PSDELKQAILE--AD-------LITTAVGVNILP-----------IIA--------KSFAPYL--------KEKENHVNI 114
Cdd:COG0246  106 VAPEDPEAVLAllADpalrivsLTITEKGYCLDPatgeldldhpdIQAdlanpappRSAPGKLtaalyrrrAAGLKPFTV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 115 VACENAIMATDTLKKAILDI---TGP-----LGDNIHFANSAVDRIVP---------LQKNENILD---VMVEPFYEWVV 174
Cdd:COG0246  186 LSCDNLPHNGDVLREAVLAFarlWDPeladwIEENVTFPNTMVDRIVPattdedrarLAAELGYEDaapVVAEPFRQWVI 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 175 EkDAWYGEELD----HIKYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQDSTIEAGLRRVLAE----TSDY 246
Cdd:COG0246  266 E-DDFPAGRPPlekaGVQFVDDVAPYEEMKLRLLNGSHTALAYLGYLAGYETVAEAMADPLLRAFVRRLMLEeiipTLPP 344
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516233030 247 ItrefdfSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIgPKdRIIKPLNylyeHNLERDGLVKAAALLL 320
Cdd:COG0246  345 P------PGVDLEAYADAVLERFANPAIRHTLARIALDGSQKL-PQ-RLLPTLR----DYLAAGRDPKRLALAV 406
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-367 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 514.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   1 MKAVHFGAGNIGRGFIGYILADNNIKVTFADVNDEIINALQTEHEYDVILADEAKTTTRVNNVDAINSAKPsDELKQAIL 80
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADE-EAVIEAIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  81 EADLITTAVGVNILPIIAKSFAPYLKEK-----ENHVNIVACENAIMATDTLKKAILDIT-----GPLGDNIHFANSAVD 150
Cdd:PRK02318  80 EADLVTTAVGPNILPFIAPLIAKGLKKRkaqgnTKPLNIIACENMIRGTSFLKKHVLKALsedekAWLEEHVGFVDSAVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 151 RIVPLQKNENILDVMVEPFYEWVVEKDAWYGE--ELDHIKYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQ 228
Cdd:PRK02318 160 RIVPAQKNEDPLDVTVEPFSEWIVDKTQFKGAlpKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAIL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 229 DSTIEAGLRRVLAETSDYITREFDFSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIGPKDRIIKPLNYLYEHNLE 308
Cdd:PRK02318 240 DPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGLP 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516233030 309 RDGLVKAAALLLKYDDKADQETVEKNNYIQEHGVKSFLQTYAKVEG--PLAEEIEKEYNEL 367
Cdd:PRK02318 320 HSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDAdsELVEEIVKAYNAL 380
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
140-322 4.19e-36

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 131.73  E-value: 4.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  140 DNIHFANSAVDRIVP------------LQKNENILDVMVEPFYEWVVEKDAWYGE---ELDHIKYVDDLTPYIERKLLTV 204
Cdd:pfam08125   1 DNVGFPNTMVDRIVPattddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGRpllEKVGVEYVEDVDPYEERKLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  205 NTGHAFLAYAGYNDNKATVLDAVQDSTIEAGLRRVLAETSDYITREFDfsKSEQSQYVEKIIERFNNSYLSDEVTRVGRG 284
Cdd:pfam08125  81 NGGHATLAYLGYLAGYQTIHEAMLDPEIRAFVKGVMTEEVAPLLAKVP--GDDLEAYADKIIERFSNPYIKDTVWRVARD 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 516233030  285 TLRKIgPKdRIIKPLNYLYEHNLERDGLVKAAALLLKY 322
Cdd:pfam08125 159 GSQKL-PQ-RKLPSLRRHIRAGPLPELLALGVAGWMRY 194
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
4-320 7.71e-26

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 108.32  E-value: 7.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   4 VHFGAGNIGRGFIGYIL------ADNNIKVTFADV--NDEIINALQtehEYD-----VILADEAKTTTRVnnVDAINSAK 70
Cdd:COG0246   31 VHFGVGNFHRAHQAWYTdrllnaGDFDWGIVGVGLrsGDALRDALA---AQDglytlVERGPDGVEEARV--IGSISEVL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  71 PSDELKQAILE--AD-------LITTAVGVNILP-----------IIA--------KSFAPYL--------KEKENHVNI 114
Cdd:COG0246  106 VAPEDPEAVLAllADpalrivsLTITEKGYCLDPatgeldldhpdIQAdlanpappRSAPGKLtaalyrrrAAGLKPFTV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 115 VACENAIMATDTLKKAILDI---TGP-----LGDNIHFANSAVDRIVP---------LQKNENILD---VMVEPFYEWVV 174
Cdd:COG0246  186 LSCDNLPHNGDVLREAVLAFarlWDPeladwIEENVTFPNTMVDRIVPattdedrarLAAELGYEDaapVVAEPFRQWVI 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 175 EkDAWYGEELD----HIKYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQDSTIEAGLRRVLAE----TSDY 246
Cdd:COG0246  266 E-DDFPAGRPPlekaGVQFVDDVAPYEEMKLRLLNGSHTALAYLGYLAGYETVAEAMADPLLRAFVRRLMLEeiipTLPP 344
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516233030 247 ItrefdfSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIgPKdRIIKPLNylyeHNLERDGLVKAAALLL 320
Cdd:COG0246  345 P------PGVDLEAYADAVLERFANPAIRHTLARIALDGSQKL-PQ-RLLPTLR----DYLAAGRDPKRLALAV 406
PRK03643 PRK03643
tagaturonate reductase;
2-274 1.02e-18

tagaturonate reductase;


Pssm-ID: 235147 [Multi-domain]  Cd Length: 471  Bit Score: 87.21  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   2 KAVHFGAGNIGRGFIGYILADNNIKVTF-ADV------NDEIINALQT-EHEYDVILA----DEAKTTTRVNNV--DAIN 67
Cdd:PRK03643  17 KILQFGEGNFLRAFVDWQIDLLNEHTDFnGGVvvvqpiDTGFPPSLNEqDGLYTLIIRglneGEAVSEARLIRSisREIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  68 SAKPSDELKQAILEADL--I---TTAVGV--------NILPiiAKSF----APYLKEKENHVN--------IVACE---- 118
Cdd:PRK03643  97 PYSDWDEFLKLARNPELrfVfsnTTEAGIsyhaedkfDDAP--PVSFpaklTALLYERFKHFNgaadkgliIIPCElidy 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 119 NAimatDTLKKAIL----------DITGPLGDNIHFANSAVDRIVP---------LQKN---ENILDVMVEPFYEWVVEK 176
Cdd:PRK03643 175 NG----EKLKEIVLryaqewnlpeAFIQWLEEANTFCSTLVDRIVTgyprdeaaaLEEElgyEDGLLDTAEPFYLWVIEG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 177 DAWYGEELD------HIKYVDDLTPYIERKLLTVNTGHAFLAYAGY---NDnkaTVLDAVQDSTIEAGLRRVLAETsdyI 247
Cdd:PRK03643 251 PKSLAKELPfdkaglNVLIVDDIKPYRERKVRILNGAHTALVPVAYlagLD---TVGEAMEDAEIGAFVEKAIYEE---I 324
                        330       340
                 ....*....|....*....|....*..
gi 516233030 248 TREFDFSKSEQSQYVEKIIERFNNSYL 274
Cdd:PRK03643 325 IPVLDLPEDELESFAEAVLDRFRNPFI 351
Mannitol_dh pfam01232
Mannitol dehydrogenase Rossmann domain;
1-119 1.30e-17

Mannitol dehydrogenase Rossmann domain;


Pssm-ID: 395986 [Multi-domain]  Cd Length: 151  Bit Score: 78.99  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030    1 MKAVHFGAGNIGRG---FIGYILADNNIKVTFADVNDEIINA---LQTEHEYDVILADEAKTTTR--VNNVDAINSAKPS 72
Cdd:pfam01232   1 MRIVHFGAGNFHRAhqaFIGDLLAENGFDWGIVDVNLRVVDAreaLNAQDGLYTVIEDGEEGRQArlVGSVNAVNSVEED 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   73 -DELKQAILE--ADLITTAVG----------VNILPIIAKSFA--PYLKEKENH--------VNIVACEN 119
Cdd:pfam01232  81 lEALIELMAEpqADIVSTTVTeggidatgqlDNDLPDIAADLAkpEYLVEALKRrraaglkpLTIIACDN 150
PRK15037 PRK15037
D-mannonate oxidoreductase; Provisional
114-329 5.65e-11

D-mannonate oxidoreductase; Provisional


Pssm-ID: 184997 [Multi-domain]  Cd Length: 486  Bit Score: 63.51  E-value: 5.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 114 IVACENAIMATDTLKKAILDITGP--------LGDNIHFANSAVDRIVPLQKNENILDVM------------VEPFYEWV 173
Cdd:PRK15037 182 VMSCDNVRENGHVAKVAVLGLAQArdpqlaawIEENVTFPCTMVDRIVPAATPETLQEIAdqlgvydpcaiaCEPFRQWV 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 174 VEKDAWYGE-ELDHI--KYVDDLTPYIERKLLTVNTGHAFLAYAGYNDNKATVLDAVQDSTI-EAGLRRVLAETSDYITR 249
Cdd:PRK15037 262 IEDNFVNGRpDWDKVgaQFVADVVPFEMMKLRMLNGSHSFLAYLGYLGGYETIADTMTNPAYrKAAFALMMQEQAPTLSM 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030 250 EfdfSKSEQSQYVEKIIERFNNSYLSDEVTRVGRGTLRKIgPKdRIIKPLNYLYEHNLERDGLVKAAALLLKYDDKADQE 329
Cdd:PRK15037 342 P---EGTDLNAYATLLIERFSNPSLRHRTWQIAMDGSQKL-PQ-RLLDPVRLHLQNGGSWRHLALGVAGWMRYTQGVDEQ 416
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
7-175 1.44e-03

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 39.92  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030   7 GAGNIGRGfIGYILADNNIKVTFADVNDEII-------NALQTEHEYDVILADEAKTTtrvnnvDAINSAKPSDELKQAI 79
Cdd:PRK08293  10 GAGVLGSQ-IAFQTAFHGFDVTIYDISDEALekakeriAKLADRYVRDLEATKEAPAE------AALNRITLTTDLAEAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030  80 LEADLITTAVGVNilpiiaksfaPYLKEK-ENHVNIVACENAIMATDT---LKKAILDITG-P---LgdNIHFANsavdr 151
Cdd:PRK08293  83 KDADLVIEAVPED----------PEIKGDfYEELAKVAPEKTIFATNSstlLPSQFAEATGrPekfL--ALHFAN----- 145
                        170       180
                 ....*....|....*....|....*....
gi 516233030 152 ivPLQKNeNILDVMVEP-----FYEWVVE 175
Cdd:PRK08293 146 --EIWKN-NTAEIMGHPgtdpeVFDTVVA 171
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
6-108 4.56e-03

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 37.56  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233030    6 FGAGNIGRGfIGYILADNNIKVTFADVNDEIINALQTEHE---Y--DVILADEAKTTTrvnnvdainsakpsdELKQAIL 80
Cdd:pfam01210   5 LGAGSWGTA-LAKVLADNGHEVRLWGRDEELIEEINTTHEnvrYlpGIKLPENLKATT---------------DLAEALK 68
                          90       100
                  ....*....|....*....|....*...
gi 516233030   81 EADLITTAVGVNILPIIAKSFAPYLKEK 108
Cdd:pfam01210  69 GADIIVIVVPSQALREVLKQLKGLLKPD 96
 
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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