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Conserved domains on  [gi|19114874|ref|NP_593962|]
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alpha,alpha-trehalose-phosphate synthase [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
173-652 0e+00

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


:

Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 658.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   173 SRSLSFSMNGTPQRRMtfdAEAWKNVIFKIKPSSFGNASFYNAISAATrskqfdDHLFVGTCGIPTDSLPDslKERISHD 252
Cdd:pfam00982   1 SRLVVVSNRLPVTAVR---DEEDGKWEFSIKMSSGGLVSALNGLSAAT------EGVWVGWPGVPVDESEP--KDKVSQS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   253 YITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNpKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDY 332
Cdd:pfam00982  70 LKEKFNCVPVFLSDELFDSYYNGFSNSILWPLFHYMIPPN-NEDAFDRSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   333 HLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVV 412
Cdd:pfam00982 149 HLMLLPQMLRKRLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGLETRSDGGV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   413 SFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGK-HIILSHDKLDPIRGLRSKLISFERFLQKYPEYREN 491
Cdd:pfam00982 229 EYGGRTVSVKAFPIGIDPGRIESGLASPSVQEKIKELKERFGNKkKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGK 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   492 TILLQVAPESLQDSE----HLPHISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTS 567
Cdd:pfam00982 309 VVLVQIAVPSRGDVEeyqnLRSQIEELVGRINGEFGTLD--YTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVA 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   568 HQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQ 647
Cdd:pfam00982 387 YEYVACQQGRKGVLILSEFAGAAQSLNDGAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFL 466

                  ....*
gi 19114874   648 SLIKE 652
Cdd:pfam00982 467 SDLKR 471
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
684-928 1.83e-75

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


:

Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 246.86  E-value: 1.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   684 LLYFEGTISTWGSQyHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQElEQLFQRVPKLGIVAENGCFVRSPPKGDat 763
Cdd:pfam02358   1 FLDYDGTLSPIVSD-PIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQE-EDLFVGVPNLGLAAEHGAFVRLPGGGD-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   764 mpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDE--AAMWAAKECCESVNNFN 841
Cdd:pfam02358  77 -----------WYNQAEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDFgsFQAKELAEHLESVLQDN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   842 VPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGD---YDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVcVSEH 918
Cdd:pfam02358 146 PPLRVTQGKKVVEVRPVGVSKGKAVEFILEELGSAgslPDFPLCIGDDRTDEDMFSVLRPTKPSGVGIEVFAVSV-GSKP 224
                         250
                  ....*....|
gi 19114874   919 GNSTNADAES 928
Cdd:pfam02358 225 SSASYFLDDP 234
 
Name Accession Description Interval E-value
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
173-652 0e+00

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 658.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   173 SRSLSFSMNGTPQRRMtfdAEAWKNVIFKIKPSSFGNASFYNAISAATrskqfdDHLFVGTCGIPTDSLPDslKERISHD 252
Cdd:pfam00982   1 SRLVVVSNRLPVTAVR---DEEDGKWEFSIKMSSGGLVSALNGLSAAT------EGVWVGWPGVPVDESEP--KDKVSQS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   253 YITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNpKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDY 332
Cdd:pfam00982  70 LKEKFNCVPVFLSDELFDSYYNGFSNSILWPLFHYMIPPN-NEDAFDRSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   333 HLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVV 412
Cdd:pfam00982 149 HLMLLPQMLRKRLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGLETRSDGGV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   413 SFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGK-HIILSHDKLDPIRGLRSKLISFERFLQKYPEYREN 491
Cdd:pfam00982 229 EYGGRTVSVKAFPIGIDPGRIESGLASPSVQEKIKELKERFGNKkKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGK 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   492 TILLQVAPESLQDSE----HLPHISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTS 567
Cdd:pfam00982 309 VVLVQIAVPSRGDVEeyqnLRSQIEELVGRINGEFGTLD--YTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVA 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   568 HQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQ 647
Cdd:pfam00982 387 YEYVACQQGRKGVLILSEFAGAAQSLNDGAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFL 466

                  ....*
gi 19114874   648 SLIKE 652
Cdd:pfam00982 467 SDLKR 471
GT20_TPS cd03788
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ...
186-646 0e+00

trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.


Pssm-ID: 340820 [Multi-domain]  Cd Length: 463  Bit Score: 593.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 186 RRMTFDAEAWKNVIFKIKPSSFGnasFYNAISAATRSKQFddhLFVGTCGIPTDSLPDslKERISHDYITEHSSLVVYPT 265
Cdd:cd03788   7 NRLPVTLERDDDGEVEFRRSAGG---LVTALKGLLKSTGG---LWVGWPGIEADEEES--DQVVSPELLEEYNVVPVFLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 266 DTDFVGHYNHYCKNILWPTFHYQIPDNpkSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERL 345
Cdd:cd03788  79 DEDFEGYYNGFSNSVLWPLFHYLLPLP--DGRFEREWWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRERL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 346 PRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALP 425
Cdd:cd03788 157 PDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSAGGVEYGGRRVRVGAFP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 426 ISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQD- 504
Cdd:cd03788 237 IGIDPDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRTDv 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 505 ---SEHLPHISDIVTRINSAYSNIasRHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPL 581
Cdd:cd03788 317 eeyQELRREVEELVGRINGRFGTL--DWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVL 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114874 582 ILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:cd03788 395 ILSEFAGAASELDG-AILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSF 458
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
229-893 5.94e-144

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 445.14  E-value: 5.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  229 LFVGTCGIPTDSLPDSLKERISHDyITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQipdnPKSKAYEDHSWANYVK 308
Cdd:PRK14501  44 LWVGWPGLDLEEESEEQRARIEPR-LEELGLVPVFLSAEEVDRYYEGFCNSTLWPLFHYF----PEYTEFEDRFWESYER 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  309 VNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIP 388
Cdd:PRK14501 119 VNQRFAEAIAAIARPGDVVWVHDYQLMLLPAMLRERLPDARIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTY 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  389 EFAYHFLQTCSRLVNIDIrKNGVVSFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPI 468
Cdd:PRK14501 199 DYVRHFLSSVLRVLGYET-ELGEIRLGGRIVRVDAFPMGIDYDKFHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYT 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  469 RGLRSKLISFERFLQKYPEYRENTILLQVAPESlqdSEHLPH-------ISDIVTRINSAYSNIASRhvPVILLRQKLGY 541
Cdd:PRK14501 278 KGIPRRLLAFERFLEKNPEWRGKVRLVQVAVPS---RTGVPQyqemkreIDELVGRINGEFGTVDWT--PIHYFYRSLPF 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  542 AQFLALMMISD-ALIdNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSE 620
Cdd:PRK14501 353 EELVALYRAADvALV-TPLRDGMNLVAKEYVASRTDGDGVLILSEMAGAAAELAE-ALLVNPNDIEGIAAAIKRALEMPE 430
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  621 EECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQ--RIPAFTAQLIKEPYQNAQKRLILLYFEGTISTWGSQY 698
Cdd:PRK14501 431 EEQRERMQAMQERLRRYDVHKWASDFLDELREAAEKNKAFAskPITPAAAEEIIARYRAASRRLLLLDYDGTLVPFAPDP 510
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  699 HNVMTSlQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRVPkLGIVAENGCFVRsPPKGDATMPVskkeiaelwknk 778
Cdd:PRK14501 511 ELAVPD-KELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLP-IHLVAEHGAWSR-APGGEWQLLE------------ 575
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  779 vlGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAA------MWAAKECCeSVNNFNVpcsatIQNDM 852
Cdd:PRK14501 576 --PVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEaranelILALSSLL-SNAPLEV-----LRGNK 647
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 19114874  853 VV-CRSNKVSKRLAAEDIYSAngGDYDFIFAASNDPDDDTVF 893
Cdd:PRK14501 648 VVeVRPAGVNKGRAVRRLLEA--GPYDFVLAIGDDTTDEDMF 687
OtsA COG0380
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
265-646 3.60e-119

Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];


Pssm-ID: 440149  Cd Length: 474  Bit Score: 371.76  E-value: 3.60e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 265 TDTDFVGHYNHYCKNILWPTFHYQiPDNPkskAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRER 344
Cdd:COG0380  81 SAEEVDGYYEGFSNETLWPLFHYR-LDLP---EFDREDWEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAMLREL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 345 LPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIAL 424
Cdd:COG0380 157 GPDARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEVDEGGTVRYGGRTVRVGAF 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 425 PISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESlqd 504
Cdd:COG0380 237 PIGIDVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPS--- 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 505 SEHLPH-------ISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKR 577
Cdd:COG0380 314 REDVPAyrelrreIEELVGRINGRFGTLD--WTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDD 391
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114874 578 HRPLILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:COG0380 392 PGVLVLSEFAGAAEELTE-ALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDF 459
trehalose_OtsA TIGR02400
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ...
265-646 8.53e-109

alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274112  Cd Length: 456  Bit Score: 343.87  E-value: 8.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   265 TDTDFVGHYNHYCKNILWPTFHYqIPDNPKskaYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRER 344
Cdd:TIGR02400  73 SEEDVDGYYNGFSNSTLWPLFHY-RPDLIR---YDRKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLREL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   345 LPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFEnRQIDVIAL 424
Cdd:TIGR02400 149 GVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGG-RTVRVGAF 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   425 PISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQD 504
Cdd:TIGR02400 228 PIGIDVDRFAEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGD 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   505 SEHLPHISD----IVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRP 580
Cdd:TIGR02400 308 VPEYQQLRRqveeLVGRINGRFGTLD--WTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGV 385
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114874   581 LILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:TIGR02400 386 LILSEFAGAAQELNG-ALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDF 450
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
684-928 1.83e-75

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 246.86  E-value: 1.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   684 LLYFEGTISTWGSQyHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQElEQLFQRVPKLGIVAENGCFVRSPPKGDat 763
Cdd:pfam02358   1 FLDYDGTLSPIVSD-PIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQE-EDLFVGVPNLGLAAEHGAFVRLPGGGD-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   764 mpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDE--AAMWAAKECCESVNNFN 841
Cdd:pfam02358  77 -----------WYNQAEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDFgsFQAKELAEHLESVLQDN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   842 VPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGD---YDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVcVSEH 918
Cdd:pfam02358 146 PPLRVTQGKKVVEVRPVGVSKGKAVEFILEELGSAgslPDFPLCIGDDRTDEDMFSVLRPTKPSGVGIEVFAVSV-GSKP 224
                         250
                  ....*....|
gi 19114874   919 GNSTNADAES 928
Cdd:pfam02358 225 SSASYFLDDP 234
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
682-917 1.07e-26

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 109.30  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 682 LILLYFEGTISTWGSQYHNVMTSlQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQrVPKLGIVAENGCFVRSPPKGD 761
Cdd:cd01627   1 LLFLDYDGTLAPIVPDPDAAVPS-PELLEALKKLAADPKNAVAIVSGRDLDDLDKWLG-LPGIGLAGEHGAEIRLPGGGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 762 atmpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAamWAAKECCESVNNFN 841
Cdd:cd01627  79 -------------WVTLAPKADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPEGA--RAALELALHLASDL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114874 842 VPCSATIQNDMVV-CRSNKVSKRLAAEDIYSANGGDYDFIFAASNDPDDDTVFSWMknfkqskKEVVPFTFSVCVSE 917
Cdd:cd01627 144 LKALEVVPGKKVVeVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRAL-------NGEGGFSVKVGEGP 213
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
707-826 5.62e-08

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 54.81  E-value: 5.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 707 RTINLLNMLTSDPKNTVYVFSALSCQELEQLFqRVPKLGIVAENGCFVRSPPKGDATMPVSKKEIAelwknkvlgtdltW 786
Cdd:COG1877  29 ELRELLRRLAARPGGAVAIVSGRDLADLDRLL-GPLGLPLAGSHGAERRLPGGEWEVLPLAAEAPE-------------W 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19114874 787 MKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAA 826
Cdd:COG1877  95 LDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAE 134
 
Name Accession Description Interval E-value
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
173-652 0e+00

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 658.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   173 SRSLSFSMNGTPQRRMtfdAEAWKNVIFKIKPSSFGNASFYNAISAATrskqfdDHLFVGTCGIPTDSLPDslKERISHD 252
Cdd:pfam00982   1 SRLVVVSNRLPVTAVR---DEEDGKWEFSIKMSSGGLVSALNGLSAAT------EGVWVGWPGVPVDESEP--KDKVSQS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   253 YITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNpKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDY 332
Cdd:pfam00982  70 LKEKFNCVPVFLSDELFDSYYNGFSNSILWPLFHYMIPPN-NEDAFDRSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   333 HLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVV 412
Cdd:pfam00982 149 HLMLLPQMLRKRLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGLETRSDGGV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   413 SFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGK-HIILSHDKLDPIRGLRSKLISFERFLQKYPEYREN 491
Cdd:pfam00982 229 EYGGRTVSVKAFPIGIDPGRIESGLASPSVQEKIKELKERFGNKkKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGK 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   492 TILLQVAPESLQDSE----HLPHISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTS 567
Cdd:pfam00982 309 VVLVQIAVPSRGDVEeyqnLRSQIEELVGRINGEFGTLD--YTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVA 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   568 HQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQ 647
Cdd:pfam00982 387 YEYVACQQGRKGVLILSEFAGAAQSLNDGAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFL 466

                  ....*
gi 19114874   648 SLIKE 652
Cdd:pfam00982 467 SDLKR 471
GT20_TPS cd03788
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ...
186-646 0e+00

trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.


Pssm-ID: 340820 [Multi-domain]  Cd Length: 463  Bit Score: 593.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 186 RRMTFDAEAWKNVIFKIKPSSFGnasFYNAISAATRSKQFddhLFVGTCGIPTDSLPDslKERISHDYITEHSSLVVYPT 265
Cdd:cd03788   7 NRLPVTLERDDDGEVEFRRSAGG---LVTALKGLLKSTGG---LWVGWPGIEADEEES--DQVVSPELLEEYNVVPVFLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 266 DTDFVGHYNHYCKNILWPTFHYQIPDNpkSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERL 345
Cdd:cd03788  79 DEDFEGYYNGFSNSVLWPLFHYLLPLP--DGRFEREWWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRERL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 346 PRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALP 425
Cdd:cd03788 157 PDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSAGGVEYGGRRVRVGAFP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 426 ISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQD- 504
Cdd:cd03788 237 IGIDPDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRTDv 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 505 ---SEHLPHISDIVTRINSAYSNIasRHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPL 581
Cdd:cd03788 317 eeyQELRREVEELVGRINGRFGTL--DWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVL 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114874 582 ILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:cd03788 395 ILSEFAGAASELDG-AILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSF 458
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
229-893 5.94e-144

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 445.14  E-value: 5.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  229 LFVGTCGIPTDSLPDSLKERISHDyITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQipdnPKSKAYEDHSWANYVK 308
Cdd:PRK14501  44 LWVGWPGLDLEEESEEQRARIEPR-LEELGLVPVFLSAEEVDRYYEGFCNSTLWPLFHYF----PEYTEFEDRFWESYER 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  309 VNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIP 388
Cdd:PRK14501 119 VNQRFAEAIAAIARPGDVVWVHDYQLMLLPAMLRERLPDARIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTY 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  389 EFAYHFLQTCSRLVNIDIrKNGVVSFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPI 468
Cdd:PRK14501 199 DYVRHFLSSVLRVLGYET-ELGEIRLGGRIVRVDAFPMGIDYDKFHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYT 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  469 RGLRSKLISFERFLQKYPEYRENTILLQVAPESlqdSEHLPH-------ISDIVTRINSAYSNIASRhvPVILLRQKLGY 541
Cdd:PRK14501 278 KGIPRRLLAFERFLEKNPEWRGKVRLVQVAVPS---RTGVPQyqemkreIDELVGRINGEFGTVDWT--PIHYFYRSLPF 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  542 AQFLALMMISD-ALIdNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSE 620
Cdd:PRK14501 353 EELVALYRAADvALV-TPLRDGMNLVAKEYVASRTDGDGVLILSEMAGAAAELAE-ALLVNPNDIEGIAAAIKRALEMPE 430
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  621 EECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQ--RIPAFTAQLIKEPYQNAQKRLILLYFEGTISTWGSQY 698
Cdd:PRK14501 431 EEQRERMQAMQERLRRYDVHKWASDFLDELREAAEKNKAFAskPITPAAAEEIIARYRAASRRLLLLDYDGTLVPFAPDP 510
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  699 HNVMTSlQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRVPkLGIVAENGCFVRsPPKGDATMPVskkeiaelwknk 778
Cdd:PRK14501 511 ELAVPD-KELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLP-IHLVAEHGAWSR-APGGEWQLLE------------ 575
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  779 vlGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAA------MWAAKECCeSVNNFNVpcsatIQNDM 852
Cdd:PRK14501 576 --PVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEaranelILALSSLL-SNAPLEV-----LRGNK 647
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 19114874  853 VV-CRSNKVSKRLAAEDIYSAngGDYDFIFAASNDPDDDTVF 893
Cdd:PRK14501 648 VVeVRPAGVNKGRAVRRLLEA--GPYDFVLAIGDDTTDEDMF 687
OtsA COG0380
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
265-646 3.60e-119

Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];


Pssm-ID: 440149  Cd Length: 474  Bit Score: 371.76  E-value: 3.60e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 265 TDTDFVGHYNHYCKNILWPTFHYQiPDNPkskAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRER 344
Cdd:COG0380  81 SAEEVDGYYEGFSNETLWPLFHYR-LDLP---EFDREDWEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAMLREL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 345 LPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIAL 424
Cdd:COG0380 157 GPDARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEVDEGGTVRYGGRTVRVGAF 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 425 PISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESlqd 504
Cdd:COG0380 237 PIGIDVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPS--- 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 505 SEHLPH-------ISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKR 577
Cdd:COG0380 314 REDVPAyrelrreIEELVGRINGRFGTLD--WTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDD 391
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114874 578 HRPLILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:COG0380 392 PGVLVLSEFAGAAEELTE-ALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDF 459
PLN03063 PLN03063
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
272-821 7.00e-111

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215555 [Multi-domain]  Cd Length: 797  Bit Score: 360.34  E-value: 7.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  272 HYNHYCKNILWPTFHY----QIPDNPKSKAYEDHsWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPR 347
Cdd:PLN03063  93 YYNGYCNNILWPIFHYmglpQEDRHDATRTFESQ-YDAYKKANRMFLDVVKENYEEGDVVWCHDYHLMFLPQYLKEYNNK 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  348 AKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVsFENRQIDVIALPIS 427
Cdd:PLN03063 172 MKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSACTRILGVEGTHEGVV-DQGKVTRVAVFPIG 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  428 IDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEH 507
Cdd:PLN03063 251 IDPERFINTCELPEVKQHMKELKRFFAGRKVILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQIAVPTRNDVPE 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  508 LPHISD----IVTRINSAYSNIASrhVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPLIL 583
Cdd:PLN03063 331 YQKLKSqvheLVGRINGRFGSVSS--VPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQKAKKGVLVL 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  584 SEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKE-QIDMQR 662
Cdd:PLN03063 409 SEFAGAGQSLGAGALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDIIVEaELRTRN 488
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  663 IP-AFTAQLIKEPYQNAQKRLILLYFEGTISTwgsqyhnVMTSLQRTINL---------LNMLTSDPKNTVYVFSALSCQ 732
Cdd:PLN03063 489 IPlELPEQDVIQQYSKSNNRLLILGFYGTLTE-------PRNSQIKEMDLglhpelketLKALCSDPKTTVVVLSRSGKD 561
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  733 ELEQLFQRVpKLGIVAENGCFVRsppkgdatmpvskKEIAELWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDAT 812
Cdd:PLN03063 562 ILDKNFGEY-NIWLAAENGMFLR-------------HTSGEWVTTMPEHMNLDWVDGVKNVFKYFTDRTPRSYVEKSETS 627

                 ....*....
gi 19114874  813 VILHLREAE 821
Cdd:PLN03063 628 LVWNYEYAD 636
trehalose_OtsA TIGR02400
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ...
265-646 8.53e-109

alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274112  Cd Length: 456  Bit Score: 343.87  E-value: 8.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   265 TDTDFVGHYNHYCKNILWPTFHYqIPDNPKskaYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRER 344
Cdd:TIGR02400  73 SEEDVDGYYNGFSNSTLWPLFHY-RPDLIR---YDRKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLREL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   345 LPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFEnRQIDVIAL 424
Cdd:TIGR02400 149 GVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGG-RTVRVGAF 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   425 PISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQD 504
Cdd:TIGR02400 228 PIGIDVDRFAEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGD 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   505 SEHLPHISD----IVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRP 580
Cdd:TIGR02400 308 VPEYQQLRRqveeLVGRINGRFGTLD--WTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGV 385
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114874   581 LILSEFVGSASILNDnAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:TIGR02400 386 LILSEFAGAAQELNG-ALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDF 450
PLN03064 PLN03064
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
216-821 4.19e-107

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215556 [Multi-domain]  Cd Length: 934  Bit Score: 353.72  E-value: 4.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  216 ISAATRSKQFDdHLFVGTCGIptdSLPDSLKERISHDYITEHSSLVVYpTDTDFVG-HYNHYCKNILWPTFHYqIPDNPK 294
Cdd:PLN03064 125 VSALLGVKEFE-ARWIGWAGV---NVPDEVGQKALTKALAEKRCIPVF-LDEEIVHqYYNGYCNNILWPLFHY-LGLPQE 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  295 SKAYEDHS----WANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATR 370
Cdd:PLN03064 199 DRLATTRSfqsqFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEYNSNMKVGWFLHTPFPSSEIHRTLPSR 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  371 QEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSfENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQ 450
Cdd:PLN03064 279 SELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVED-QGRLTRVAAFPIGIDSDRFIRALETPQVQQHIKELK 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  451 DRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEHLPHIS----DIVTRINSAYSNIA 526
Cdd:PLN03064 358 ERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENPEWRDKVVLLQIAVPTRTDVPEYQKLTsqvhEIVGRINGRFGTLT 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  527 SrhVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYS 606
Cdd:PLN03064 438 A--VPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQDSKKGVLILSEFAGAAQSLGAGAILVNPWNIT 515
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  607 KTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKE-QIDMQRI-PAFTAQLIKEPYQNAQKRLIL 684
Cdd:PLN03064 516 EVAASIAQALNMPEEEREKRHRHNFMHVTTHTAQEWAETFVSELNDTVVEaQLRTRQVpPQLPPEDAIQRYLQSNNRLLI 595
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  685 LYFEGTIS-------TWGSQYHNVMTSLQRTIN-LLNMLTSDPKNTVYVFSALSCQELEQLFQRVpKLGIVAENGCFVRs 756
Cdd:PLN03064 596 LGFNATLTepvdtpgRRGDQIKEMELRLHPELKePLRALCSDPKTTIVVLSGSDRSVLDENFGEF-DMWLAAENGMFLR- 673
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114874  757 PPKGD--ATMPVSkkeiaelwknkvlgTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAE 821
Cdd:PLN03064 674 HTKGEwmTTMPEH--------------LNMDWVDSVKHVFEYFTERTPRSHFETRETSLVWNYKYAD 726
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
226-893 2.50e-99

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 330.83  E-value: 2.50e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  226 DDHLFVGTCGIPTDSLPDSLKERISHDYITEHSSLVVY-PTDTdFVGHYNHYCKNILWPTFHYQIPDNPKSKAYEDHS-W 303
Cdd:PLN02205 102 DDEIEVIYVGCLKEEIHLNEQEEVSQILLETFKCVPTFlPPDL-FTRYYHGFCKQQLWPLFHYMLPLSPDLGGRFNRSlW 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  304 ANYVKVNKAFADTIVDNYE-QDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANI 382
Cdd:PLN02205 181 QAYVSVNKIFADRIMEVINpEDDFVWIHDYHLMVLPTFLRKRFNRVKLGFFLHSPFPSSEIYKTLPIREELLRALLNSDL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  383 LGFQIPEFAYHFLQTCSRLVNIDIR-KNGVVSFE--NRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRF--RGKH 457
Cdd:PLN02205 261 IGFHTFDYARHFLSCCSRMLGLSYEsKRGYIGLEyyGRTVSIKILPVGIHMGQLQSVLSLPETEAKVKELIKQFcdQDRI 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  458 IILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEHLPHIS----DIVTRINSAYSNIAsrHVPVI 533
Cdd:PLN02205 341 MLLGVDDMDIFKGISLKLLAMEQLLMQHPEWQGKVVLVQIANPARGKGKDVKEVQaethSTVKRINETFGKPG--YDPIV 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  534 LLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHR---------------PLILSEFVGSASILNdNAI 598
Cdd:PLN02205 419 LIDAPLKFYERVAYYVVAECCLVTAVRDGMNLIPYEYIISRQGNEKldkllglepstpkksMLVVSEFIGCSPSLS-GAI 497
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  599 IVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQ----------RI----P 664
Cdd:PLN02205 498 RVNPWNIDAVADAMDSALEMAEPEKQLRHEKHYRYVSTHDVGYWARSFLQDLERTCRDHSRRRcwgigfglsfRVvaldP 577
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  665 AF---TAQLIKEPYQNAQKRLILLYFEGTISTWGSQYHNVMTslqRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRV 741
Cdd:PLN02205 578 NFrklSMEHIVSAYKRTTTRAILLDYDGTLMPQASIDKSPSS---KSIDILNTLCRDKNNMVFIVSARSRKTLADWFSPC 654
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  742 PKLGIVAENGCFVRspPKGDATmpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAE 821
Cdd:PLN02205 655 EKLGIAAEHGYFLR--LKRDVE-----------WETCVPVADCSWKQIAEPVMQLYTETTDGSTIEDKETALVWCYEDAD 721
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114874  822 DDEAAMwAAKECCESVNNF--NVPCSATIQNDMVVCRSNKVSKRLAAEDIYS---ANGGDYDFIFAASNDPDDDTVF 893
Cdd:PLN02205 722 PDFGSC-QAKELLDHLESVlaNEPVTVKSGQNIVEVKPQGVSKGLVAKRLLSimqERGMLPDFVLCIGDDRSDEDMF 797
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
684-928 1.83e-75

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 246.86  E-value: 1.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   684 LLYFEGTISTWGSQyHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQElEQLFQRVPKLGIVAENGCFVRSPPKGDat 763
Cdd:pfam02358   1 FLDYDGTLSPIVSD-PIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQE-EDLFVGVPNLGLAAEHGAFVRLPGGGD-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   764 mpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDE--AAMWAAKECCESVNNFN 841
Cdd:pfam02358  77 -----------WYNQAEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDFgsFQAKELAEHLESVLQDN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874   842 VPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGD---YDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVcVSEH 918
Cdd:pfam02358 146 PPLRVTQGKKVVEVRPVGVSKGKAVEFILEELGSAgslPDFPLCIGDDRTDEDMFSVLRPTKPSGVGIEVFAVSV-GSKP 224
                         250
                  ....*....|
gi 19114874   919 GNSTNADAES 928
Cdd:pfam02358 225 SSASYFLDDP 234
PRK10117 PRK10117
trehalose-6-phosphate synthase; Provisional
268-646 1.23e-50

trehalose-6-phosphate synthase; Provisional


Pssm-ID: 182249  Cd Length: 474  Bit Score: 185.73  E-value: 1.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  268 DFVGHYNHYCKNILWPTFHYQIpdnpKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPR 347
Cdd:PRK10117  72 DYDEYYNQFSNAVLWPAFHYRL----DLVQFQRPAWEGYLRVNALLADKLLPLLKDDDIIWIHDYHLLPFASELRKRGVN 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  348 AKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALPIS 427
Cdd:PRK10117 148 NRIGFFLHIPFPTPEIFNALPPHDELLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVTTRSGKSHTAWGKAFRTEVYPIG 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  428 IDPGFIDRCLASPPVEHWAKVLQDRFRGKHIIlSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPES------ 501
Cdd:PRK10117 228 IEPDEIAKQAAGPLPPKLAQLKAELKNVQNIF-SVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSrgdvqa 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874  502 LQDSEHlpHISDIVTRINSAYSNIAsrHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHrP- 580
Cdd:PRK10117 307 YQDIRH--QLETEAGRINGKYGQLG--WTPLYYLNQHFDRKLLMKIFRYSDVGLVTPLRDGMNLVAKEYVAAQDPAN-Pg 381
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114874  581 -LILSEFVGSASILNdNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTF 646
Cdd:PRK10117 382 vLVLSQFAGAANELT-SALIVNPYDRDEVAAALDRALTMPLAERISRHAEMLDVIVKNDINHWQECF 447
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
682-917 1.07e-26

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 109.30  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 682 LILLYFEGTISTWGSQYHNVMTSlQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQrVPKLGIVAENGCFVRSPPKGD 761
Cdd:cd01627   1 LLFLDYDGTLAPIVPDPDAAVPS-PELLEALKKLAADPKNAVAIVSGRDLDDLDKWLG-LPGIGLAGEHGAEIRLPGGGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 762 atmpvskkeiaelWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAamWAAKECCESVNNFN 841
Cdd:cd01627  79 -------------WVTLAPKADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPEGA--RAALELALHLASDL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114874 842 VPCSATIQNDMVV-CRSNKVSKRLAAEDIYSANGGDYDFIFAASNDPDDDTVFSWMknfkqskKEVVPFTFSVCVSE 917
Cdd:cd01627 144 LKALEVVPGKKVVeVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRAL-------NGEGGFSVKVGEGP 213
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
707-826 5.62e-08

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 54.81  E-value: 5.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114874 707 RTINLLNMLTSDPKNTVYVFSALSCQELEQLFqRVPKLGIVAENGCFVRSPPKGDATMPVSKKEIAelwknkvlgtdltW 786
Cdd:COG1877  29 ELRELLRRLAARPGGAVAIVSGRDLADLDRLL-GPLGLPLAGSHGAERRLPGGEWEVLPLAAEAPE-------------W 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19114874 787 MKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAA 826
Cdd:COG1877  95 LDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAE 134
 
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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