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Conserved domains on  [gi|695721597]
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Chain A, Transketolase

Protein Classification

transketolase family protein( domain architecture ID 11414320)

transketolase family protein such as transketolase, which catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate

EC:  2.2.1.-
Gene Ontology:  GO:0016744
PubMed:  9924800

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
21-680 0e+00

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


:

Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 1203.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:COG0021    1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPA-NPKWPNRDRFVLSAGHGSMLLYSLLHLTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:COG0021   80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPT 260
Cdd:COG0021  160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 261 IIEIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLqDKGVKAENKWNEMFEAYKKE 339
Cdd:COG0021  240 LIICKTIIGYGSPNkQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAG-ERGAAAEAEWNERFAAYAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 340 YSDLAQKFSDGFSNKVPNTLGDILPQYGEDD-SIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESY 418
Cdd:COG0021  319 YPELAAELERRLAGELPEDWDAALPAFEADAkGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 419 EGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLA 498
Cdd:COG0021  399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 499 SLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVfDGVEKGGYVVQGAENEADGILIATGS 578
Cdd:COG0021  479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLADAEGTPDVILIATGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 579 EVGLALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSA 658
Cdd:COG0021  558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
                        650       660
                 ....*....|....*....|..
gi 695721597 659 PSDIVLRELGMSVENIVDKYLE 680
Cdd:COG0021  638 PAKVLFEEFGFTVENVVAAAKE 659
 
Name Accession Description Interval E-value
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
21-680 0e+00

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 1203.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:COG0021    1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPA-NPKWPNRDRFVLSAGHGSMLLYSLLHLTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:COG0021   80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPT 260
Cdd:COG0021  160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 261 IIEIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLqDKGVKAENKWNEMFEAYKKE 339
Cdd:COG0021  240 LIICKTIIGYGSPNkQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAG-ERGAAAEAEWNERFAAYAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 340 YSDLAQKFSDGFSNKVPNTLGDILPQYGEDD-SIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESY 418
Cdd:COG0021  319 YPELAAELERRLAGELPEDWDAALPAFEADAkGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 419 EGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLA 498
Cdd:COG0021  399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 499 SLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVfDGVEKGGYVVQGAENEADGILIATGS 578
Cdd:COG0021  479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLADAEGTPDVILIATGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 579 EVGLALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSA 658
Cdd:COG0021  558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
                        650       660
                 ....*....|....*....|..
gi 695721597 659 PSDIVLRELGMSVENIVDKYLE 680
Cdd:COG0021  638 PAKVLFEEFGFTVENVVAAAKE 659
tktlase_bact TIGR00232
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ...
28-677 0e+00

transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 272974 [Multi-domain]  Cd Length: 653  Bit Score: 933.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   28 VNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDVSMDD 107
Cdd:TIGR00232   4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNP-TNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  108 LKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEA 187
Cdd:TIGR00232  83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  188 ASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  268 IGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:TIGR00232 243 IGFGSPNkAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  347 FSDGFSNKVPNTLGDILPQY-GEDDSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFqPESYEGRNIWF 425
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFkVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYIHY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  426 GVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPN 505
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  506 VQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPiskEKVFDGVEKGGYVVQGAENeADGILIATGSEVGLALK 585
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE---ESSLEKVLKGGYVLKDSKG-PDLILIATGSEVQLAVE 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  586 AKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELkKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVLR 665
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
                         650
                  ....*....|..
gi 695721597  666 ELGMSVENIVDK 677
Cdd:TIGR00232 637 EFGFTVENVVAK 648
PLN02790 PLN02790
transketolase
32-677 0e+00

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 925.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  32 RTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKTHmNWVNRDRFVLSAGHGSALLYSLAHLAGYD-VSMDDLKN 110
Cdd:PLN02790   2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNP-YWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 111 FREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEAASL 190
Cdd:PLN02790  81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 191 AGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFN-LEEIDKAIVQAKAESDKPTIIEIKTTIG 269
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNTdYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 270 YGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKEClQDKGVKAENKWNEMFEAYKKEYSDLAQKFS 348
Cdd:PLN02790 241 YGSPNkANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSKH-TKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 349 DGFSNKVPNTLGDILPQYGEDDSI-ATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRNIWFGV 427
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGV 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 428 REFGMACAMNGIMLHG-GTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNV 506
Cdd:PLN02790 400 REHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNI 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 507 QVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQG--AENEADGILIATGSEVGLAL 584
Cdd:PLN02790 480 LMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS---IEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 585 KAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVL 664
Cdd:PLN02790 557 KAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILY 636
                        650
                 ....*....|...
gi 695721597 665 RELGMSVENIVDK 677
Cdd:PLN02790 637 KEFGFTVENVVAA 649
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
23-356 5.21e-177

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 507.31  E-value: 5.21e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   23 VDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYD 102
Cdd:pfam00456   1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNP-NDPKWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  103 VSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEG 182
Cdd:pfam00456  80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  183 VASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTII 262
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  263 EIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWN-YPPFTVPEEVSQRFKECLQDkGVKAENKWNEMFEAYKKEY 340
Cdd:pfam00456 240 KCRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAY 318
                         330
                  ....*....|....*.
gi 695721597  341 SDLAQKFSDGFSNKVP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
29-294 3.11e-137

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 402.27  E-value: 3.11e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  29 NTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDvSMDDL 108
Cdd:cd02012    1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPA-DPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 109 KNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAA 188
Cdd:cd02012   79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGF----------DYRVYVLLGDGELQEGSVWEAA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 189 SLAGHLKLGKLIALYDSNGISLDGKTSA-SFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:cd02012  149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
                        250       260
                 ....*....|....*....|....*...
gi 695721597 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAK 294
Cdd:cd02012  228 KGKGVPFmENTAKWHGKPLGEEEVELAK 255
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
423-541 6.81e-34

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 126.06  E-value: 6.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   423 IWFGVREFGMACAMNGIMLHGGtRIFGSTFFVFSDYLKAAIRLSAIQKLpVIYVLTHDS-VAVGKDGPTHEPIEQLASLR 501
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 695721597   502 TIPNVQVFRPADGNETSAAWKVALEtLDKPTILVLSRQNL 541
Cdd:smart00861  96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSL 134
 
Name Accession Description Interval E-value
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
21-680 0e+00

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 1203.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:COG0021    1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPA-NPKWPNRDRFVLSAGHGSMLLYSLLHLTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:COG0021   80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPT 260
Cdd:COG0021  160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 261 IIEIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLqDKGVKAENKWNEMFEAYKKE 339
Cdd:COG0021  240 LIICKTIIGYGSPNkQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAG-ERGAAAEAEWNERFAAYAAA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 340 YSDLAQKFSDGFSNKVPNTLGDILPQYGEDD-SIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESY 418
Cdd:COG0021  319 YPELAAELERRLAGELPEDWDAALPAFEADAkGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 419 EGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLA 498
Cdd:COG0021  399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 499 SLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVfDGVEKGGYVVQGAENEADGILIATGS 578
Cdd:COG0021  479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLADAEGTPDVILIATGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 579 EVGLALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSA 658
Cdd:COG0021  558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
                        650       660
                 ....*....|....*....|..
gi 695721597 659 PSDIVLRELGMSVENIVDKYLE 680
Cdd:COG0021  638 PAKVLFEEFGFTVENVVAAAKE 659
tktlase_bact TIGR00232
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ...
28-677 0e+00

transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 272974 [Multi-domain]  Cd Length: 653  Bit Score: 933.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   28 VNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDVSMDD 107
Cdd:TIGR00232   4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNP-TNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  108 LKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEA 187
Cdd:TIGR00232  83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  188 ASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  268 IGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:TIGR00232 243 IGFGSPNkAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  347 FSDGFSNKVPNTLGDILPQY-GEDDSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFqPESYEGRNIWF 425
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFkVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYIHY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  426 GVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPN 505
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  506 VQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPiskEKVFDGVEKGGYVVQGAENeADGILIATGSEVGLALK 585
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE---ESSLEKVLKGGYVLKDSKG-PDLILIATGSEVQLAVE 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  586 AKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELkKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVLR 665
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
                         650
                  ....*....|..
gi 695721597  666 ELGMSVENIVDK 677
Cdd:TIGR00232 637 EFGFTVENVVAK 648
PLN02790 PLN02790
transketolase
32-677 0e+00

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 925.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  32 RTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKTHmNWVNRDRFVLSAGHGSALLYSLAHLAGYD-VSMDDLKN 110
Cdd:PLN02790   2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNP-YWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 111 FREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEAASL 190
Cdd:PLN02790  81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 191 AGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFN-LEEIDKAIVQAKAESDKPTIIEIKTTIG 269
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNTdYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 270 YGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKEClQDKGVKAENKWNEMFEAYKKEYSDLAQKFS 348
Cdd:PLN02790 241 YGSPNkANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSKH-TKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 349 DGFSNKVPNTLGDILPQYGEDDSI-ATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRNIWFGV 427
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGV 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 428 REFGMACAMNGIMLHG-GTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNV 506
Cdd:PLN02790 400 REHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNI 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 507 QVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQG--AENEADGILIATGSEVGLAL 584
Cdd:PLN02790 480 LMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS---IEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 585 KAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVL 664
Cdd:PLN02790 557 KAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILY 636
                        650
                 ....*....|...
gi 695721597 665 RELGMSVENIVDK 677
Cdd:PLN02790 637 KEFGFTVENVVAA 649
PRK05899 PRK05899
transketolase; Reviewed
24-680 0e+00

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 919.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  24 DQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDV 103
Cdd:PRK05899   8 LQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPK-NPKWPNRDRFVLSAGHGSMLLYSLLHLAGYDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 104 SMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGV 183
Cdd:PRK05899  87 SIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLMEGI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 184 ASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAeSDKPTIIE 263
Cdd:PRK05899 167 SHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKA-STKPTLII 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 264 IKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYppftvpeevsqrfkeclqdkgvkaenkwnemfeaykkeysd 342
Cdd:PRK05899 245 AKTIIGKGAPNkEGTHKVHGAPLGAEEIAAAKKELGWDY----------------------------------------- 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 343 laqkfsdgfsnkvpntlgdilpqygeddsiatRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRN 422
Cdd:PRK05899 284 --------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDYSGRY 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 423 IWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRT 502
Cdd:PRK05899 332 IHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRA 411
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 503 IPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPisKEKVFDGVEKGGYVVqgaENEADGILIATGSEVGL 582
Cdd:PRK05899 412 IPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLE--RTAQEEGVAKGGYVL---RDDPDVILIATGSEVHL 486
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 583 ALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDI 662
Cdd:PRK05899 487 ALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAPADE 566
                        650
                 ....*....|....*...
gi 695721597 663 VLRELGMSVENIVDKYLE 680
Cdd:PRK05899 567 LFKEFGFTVENIVAAAKE 584
PTZ00089 PTZ00089
transketolase; Provisional
21-677 0e+00

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 847.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:PTZ00089   3 GAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPK-DPRWINRDRFVLSNGHASALLYSMLHLTG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:PTZ00089  82 YDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDG-FNLEEIDKAIVQAKAESDKP 259
Cdd:PTZ00089 162 EGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGnTDFDGLRKAIEEAKKSKGKP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 260 TIIEIKTTIGYGSENQGTHKVHGSPLGEEGVAHAKEVYNWNypP---FTVPEEVSQRFKEcLQDKGVKAENKWNEMFEAY 336
Cdd:PTZ00089 242 KLIIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLD--PekkFHVSEEVRQFFEQ-HVEKKKENYEAWKKRFAKY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 337 KKEYSDLAQKFSDGFSNKVPNTLGDILPQYGEDDS-IATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQP 415
Cdd:PTZ00089 319 TAAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 416 ESYEGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIE 495
Cdd:PTZ00089 399 ASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 496 QLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQGAENEADGILIA 575
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSS---IEGVLKGAYIVVDFTNSPQLILVA 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 576 TGSEVGLALKAKEELqKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHgvmIGIDEFG 655
Cdd:PTZ00089 556 SGSEVSLCVEAAKAL-SKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH---VGISGFG 631
                        650       660
                 ....*....|....*....|..
gi 695721597 656 MSAPSDIVLRELGMSVENIVDK 677
Cdd:PTZ00089 632 ASAPANALYKHFGFTVENVVEK 653
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
23-356 5.21e-177

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 507.31  E-value: 5.21e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   23 VDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYD 102
Cdd:pfam00456   1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNP-NDPKWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  103 VSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEG 182
Cdd:pfam00456  80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  183 VASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTII 262
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  263 EIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWN-YPPFTVPEEVSQRFKECLQDkGVKAENKWNEMFEAYKKEY 340
Cdd:pfam00456 240 KCRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAY 318
                         330
                  ....*....|....*.
gi 695721597  341 SDLAQKFSDGFSNKVP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
29-294 3.11e-137

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 402.27  E-value: 3.11e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  29 NTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDvSMDDL 108
Cdd:cd02012    1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPA-DPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 109 KNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAA 188
Cdd:cd02012   79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGF----------DYRVYVLLGDGELQEGSVWEAA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 189 SLAGHLKLGKLIALYDSNGISLDGKTSA-SFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:cd02012  149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
                        250       260
                 ....*....|....*....|....*...
gi 695721597 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAK 294
Cdd:cd02012  228 KGKGVPFmENTAKWHGKPLGEEEVELAK 255
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
31-288 1.31e-66

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 220.33  E-value: 1.31e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  31 LRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYS-LAHlAGYdVSMDDLK 109
Cdd:COG3959   15 IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPK-NPDWPDRDRFILSKGHAAPALYAvLAE-KGY-FPKEELA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 110 NFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAmaeahLGKKFNREgypvmDHYTYALIGDGDLMEGVASEAAS 189
Cdd:COG3959   92 TFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMA-----LAAKLDGK-----DYRVYVLLGDGELQEGQVWEAAM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 190 LAGHLKLGKLIALYDSNGISLDGKTSASF-TENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTTI 268
Cdd:COG3959  162 AAAHYKLDNLIAIVDRNGLQIDGPTEDVMsLEPLAEKWEAFGWHVIEV-DGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240
                        250       260
                 ....*....|....*....|.
gi 695721597 269 GYG-SENQGTHKVHGSPLGEE 288
Cdd:COG3959  241 GKGvSFMENRPKWHGKAPNDE 261
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
370-541 4.10e-60

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 199.31  E-value: 4.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  370 DSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPEsyeGRNIWFGVREFGMACAMNGIMLHGG-TRIF 448
Cdd:pfam02779   1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQGA---GRVIDTGIAEQAMVGFANGMALHGPlLPPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  449 GSTFFVFSDYLKAAIR-LSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALET 527
Cdd:pfam02779  78 EATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRR 157
                         170
                  ....*....|....*
gi 695721597  528 LD-KPTILVLSRQNL 541
Cdd:pfam02779 158 DGrKPVVLRLPRQLL 172
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
376-538 5.04e-60

Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.


Pssm-ID: 132916 [Multi-domain]  Cd Length: 156  Bit Score: 198.43  E-value: 5.04e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 376 AASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGdfqpesYEGRNIWFGVREFGMACAMNGIMLHGgTRIFGSTFFVF 455
Cdd:cd07033    1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKK------FPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 456 SDYLKAAIR-LSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETlDKPTIL 534
Cdd:cd07033   74 LQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY-DGPVYI 152

                 ....
gi 695721597 535 VLSR 538
Cdd:cd07033  153 RLPR 156
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
423-541 6.81e-34

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 126.06  E-value: 6.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   423 IWFGVREFGMACAMNGIMLHGGtRIFGSTFFVFSDYLKAAIRLSAIQKLpVIYVLTHDS-VAVGKDGPTHEPIEQLASLR 501
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 695721597   502 TIPNVQVFRPADGNETSAAWKVALEtLDKPTILVLSRQNL 541
Cdd:smart00861  96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSL 134
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
370-677 3.39e-29

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 118.27  E-value: 3.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 370 DSIATRAASQKAINALAKEVSSLWGGAADLASSNKTviageGDFQpESYEGRNIWFGVRE---FGMACAMNgimlHGGTR 446
Cdd:COG3958    2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKL-----DKFA-KAFPDRFFNVGIAEqnmVGVAAGLA----LAGKI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 447 IFGSTFFVFSdYLKAA--IRLS-AIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKV 523
Cdd:COG3958   72 PFVSTFAPFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 524 ALETlDKPTILVLSRQNLdtlpiskEKVFDGVEK----GGYVV-QGaeneADGILIATGSEVGLALKAKEELQKKGKDVI 598
Cdd:COG3958  151 AAEH-DGPVYLRLGRGAV-------PVVYDEDYEfeigKARVLrEG----KDVTIIATGIMVAEALEAAELLAKEGISAR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 599 VVSLPS-----WERFEAQSEEYKNTVippelkkrmTIEAGTTYG-----WAKYAGDHG----VMIGI-DEFGMSAPSDIV 663
Cdd:COG3958  219 VINMHTikpldEEAILKAARKTGAVV---------TAEEHSIIGglgsaVAEVLAENYpvplRRIGVpDRFGESGSPEEL 289
                        330
                 ....*....|....
gi 695721597 664 LRELGMSVENIVDK 677
Cdd:COG3958  290 LEKYGLDAEGIVAA 303
dxs TIGR00204
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ...
19-679 6.16e-19

1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 129308 [Multi-domain]  Cd Length: 617  Bit Score: 90.99  E-value: 6.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   19 PYDQVDQLgVNTLRTLSIDAIQrANSGHPGLPMGAAPMAYVLwtrHLKIN-PKthmnwvnrDRFVLSAGHGSallYSLAH 97
Cdd:TIGR00204  14 SIDELEKL-CDELRRYLLESVS-ASGGHLASGLGTVELTVAL---HYVFNtPK--------DQFIWDVGHQA---YPHKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597   98 LAGYDVSMDDLKNFRewksNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAeahlgkkFNREGypvMDHYTYALIGDG 177
Cdd:TIGR00204  78 LTGRREKFSTLRQKK----GLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVA-------AEKKG---ADRKTVCVIGDG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  178 DLMEGVASEAASLAGHLKLGKLIALYDSN-GIS-------------LDGKTSASFTENV--------------------- 222
Cdd:TIGR00204 144 AITAGMAFEALNHAGDLKTDMIVILNDNEmSISenvgalsnhlaqlRSGSLYQSLRDGLkkifsklppiknylakrtees 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  223 -------GARFEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYGSEnqgthKVHGSPLGEEGVahake 295
Cdd:TIGR00204 224 mkglvvpGTFFEELGFNYIGPVDGHDLLELIETLKNAK-KLKGPVFLHIQTKKGKGYK-----PAEKDPIGWHGV----- 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  296 vynwnyPPFTVpeevsqrfkeclqDKGVKAENKwnEMFEAYKKEYSDLAQKfsdgfsnkvpntlgdilpqygeddsiatr 375
Cdd:TIGR00204 293 ------GPFDL-------------STGCLPKSK--SALPSYSKIFSDTLCE----------------------------- 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  376 aasqkainaLAKEVSSLWGGAADLASSNKTViagegDFQPEsyegrniwFGVREFGMACA------MNGIMLHGGTRIFG 449
Cdd:TIGR00204 323 ---------LAKKDNKIVGITPAMPEGSGLD-----KFSRK--------FPDRYFDVAIAeqhavtFAAGMAIEGYKPFV 380
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  450 StffVFSDYLKAA----IRLSAIQKLPVIYVLTHDSVaVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVAL 525
Cdd:TIGR00204 381 A---IYSTFLQRAydqvVHDVCIQKLPVLFAIDRAGI-VGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGY 456
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  526 ETLDKPTILVLSRQN---------LDTLPISKEKVfdgVEKGGyvvqgaeneaDGILIATGSEVGLALKAKEELQKKGKD 596
Cdd:TIGR00204 457 HYDDGPIAVRYPRGNavgveltpePEKLPIGKSEV---LRKGE----------KILILGFGTLVPEALEVAESLNEKGIE 523
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  597 VIVVSLpsweRFEAQSEEYKNTVIPPELKKRMTIEAGTTYGW-----AKYAGDHGVM-----IGI-DEFGMSAPSDIVLR 665
Cdd:TIGR00204 524 ATVVDA----RFVKPLDEELILEIAASHEKLVTVEENAIMGGagsavLEFLMDQNKLvpvkrLGIpDFFIPHGTQEEVLA 599
                         730
                  ....*....|....
gi 695721597  666 ELGMSVENIVDKYL 679
Cdd:TIGR00204 600 ELGLDTAGMEAKIL 613
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
141-677 7.13e-17

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 84.36  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 141 ISMAVGMAMAEAHLGKKfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNGISLDgktsasftE 220
Cdd:PRK05444 123 ISAALGMAKARDLKGGE---------DRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSIS--------P 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 221 NVGA--------R----FEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYG---SENQGThKVHGSpl 285
Cdd:PRK05444 185 NVGAlsnylarlRsstlFEELGFNYIGPIDGHDLDALIETLKNAK-DLKGPVLLHVVTKKGKGyapAEADPI-KYHGV-- 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 286 geegvahakevynwnyPPFTVpeevsqrfkeclqDKGVKaenkwnemfeayKKEYSDLAQKFSDGFSnkvpNTLGDILpq 365
Cdd:PRK05444 261 ----------------GKFDP-------------ETGEQ------------PKSSKPGKPSYTKVFG----ETLCELA-- 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 366 yGEDDSIAtraasqkAINALAKEVSSLwggaadlassnktviageGDFQ---PESYegrniwF--GVRE-----F--GMA 433
Cdd:PRK05444 294 -EKDPKIV-------AITAAMPEGTGL------------------VKFSkrfPDRY------FdvGIAEqhavtFaaGLA 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 434 CamngimlhGGTRIFG---STFF------VFSDYlkaairlsAIQKLPVIYVLthDSvA--VGKDGPTHEPIEQLASLRT 502
Cdd:PRK05444 342 T--------EGLKPVVaiySTFLqraydqVIHDV--------ALQNLPVTFAI--DR-AglVGADGPTHQGAFDLSYLRC 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 503 IPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVFDgVEKGGYVVQGaeneADGILIATGSEVGL 582
Cdd:PRK05444 403 IPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGVGVELPELEPLP-IGKGEVLREG----EDVAILAFGTMLAE 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 583 ALKAKEELqkkgKDVIVVSLpsweRF---------EAQSEEYKNTVippelkkrmTIEAGTTYGWA-----KYAGDHGVM 648
Cdd:PRK05444 478 ALKAAERL----ASATVVDA----RFvkpldeellLELAAKHDLVV---------TVEEGAIMGGFgsavlEFLADHGLD 540
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 695721597 649 -----IGI-DEFGMSAPSDIVLRELGMSVENIVDK 677
Cdd:PRK05444 541 vpvlnLGLpDEFIDHGSREELLAELGLDAEGIARR 575
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
467-680 1.96e-15

Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440768 [Multi-domain]  Cd Length: 623  Bit Score: 80.06  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 467 AIQKLPVIYVLthDSvA--VGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALEtLDKPTIL---------V 535
Cdd:COG1154  406 ALQNLPVTFAI--DR-AglVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALA-YDGPTAIryprgngpgV 481
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 536 LSRQNLDTLPISK-EKVFDGvekggyvvqgaeneADGILIATGSEVGLALKAKEELQKKGKDVIVVSLpsweRFeaqsee 614
Cdd:COG1154  482 ELPAELEPLPIGKgEVLREG--------------KDVAILAFGTMVAEALEAAERLAAEGISATVVDA----RF------ 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 615 ykntVIP--PELKKRM--------TIEAGTT---YGWA--KYAGDHGV-----MIGI-DEFGMSAPSDIVLRELGMSVEN 673
Cdd:COG1154  538 ----VKPldEELILELarehdlvvTVEEGVLaggFGSAvlEFLADAGLdvpvlRLGLpDRFIEHGSRAELLAELGLDAEG 613

                 ....*..
gi 695721597 674 IVDKYLE 680
Cdd:COG1154  614 IARAILE 620
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
133-271 6.19e-15

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 73.73  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 133 TTGPLGQGISMAVGMAMAEAHLGKKFNregypvmdhyTYALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLDg 212
Cdd:cd02007   73 GTGHSSTSISAALGMAVARDLKGKKRK----------VIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSIS- 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695721597 213 ktsasftENVGAR---FEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYG 271
Cdd:cd02007  141 -------PNVGTPgnlFEELGFRYIGPVDGHNIEALIKVLKEVK-DLKGPVLLHVVTKKGKG 194
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
141-676 7.63e-14

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 74.76  E-value: 7.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 141 ISMAVGMAMAEAhLGKKfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLDGKTSA---- 216
Cdd:PRK12571 125 ISAALGFAKARA-LGQP---------DGDVVAVIGDGSLTAGMAYEALNNAGAAD-RRLIVILNDNEMSIAPPVGAlaay 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 217 --------------SFTENVGAR-------------------------FEAYGWQYILVEDGFNLEEIDKAIVQAKAESD 257
Cdd:PRK12571 194 lstlrssdpfarlrAIAKGVEERlpgplrdgarrarelvtgmigggtlFEELGFTYVGPIDGHDMEALLSVLRAARARAD 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 258 KPTIIEIKTTIGYGsenqgthkvhgsplgeegvahakevynwnYPPftvpeevsqrfKECLQDKgvkaenkwnemFEAYK 337
Cdd:PRK12571 274 GPVLVHVVTEKGRG-----------------------------YAP-----------AEADEDK-----------YHAVG 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 338 KeysdlaqkfsdgfsnkvpntlgdILPQYGEDDSIATRAAS-----QKAINALAKEVSSLWGGAADLASSnktviAGEGD 412
Cdd:PRK12571 303 K-----------------------FDVVTGLQKKSAPSAPSytsvfGEELTKEAAEDSDIVAITAAMPLG-----TGLDK 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 413 FQpESYEGRNIWFGVRE-FGMACAMNgiMLHGGTRIFgstFFVFSDYLKAA----IRLSAIQKLPVIYVLTHDSVaVGKD 487
Cdd:PRK12571 355 LQ-KRFPNRVFDVGIAEqHAVTFAAG--LAAAGLKPF---CAVYSTFLQRGydqlLHDVALQNLPVRFVLDRAGL-VGAD 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 488 GPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVFDGVEKGGYVVQGaen 567
Cdd:PRK12571 428 GATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGTILGIGKGRVPREG--- 504
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 568 eADGILIATGSEVGLALKAKEELQKKGKDVIVVSlPSW-----ERFEAQSEEYKNTVIppelkkrmTIEAGTTYGW---- 638
Cdd:PRK12571 505 -PDVAILSVGAHLHECLDAADLLEAEGISVTVAD-PRFvkpldEALTDLLVRHHIVVI--------VEEQGAMGGFgahv 574
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 695721597 639 AKYAGDHGVM--------IGI-DEFGMSAPSDIVLRELGMSVENIVD 676
Cdd:PRK12571 575 LHHLADTGLLdgglklrtLGLpDRFIDHASREEMYAEAGLTAPDIAA 621
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
559-674 1.14e-13

Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.


Pssm-ID: 460693 [Multi-domain]  Cd Length: 124  Bit Score: 68.01  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  559 GYVVQGAENEaDGILIATGSEVGLALKAKEELQKKGKDVIVVSLPSWERFEAQS-----EEYKNTVIPPELKKRMTIEAG 633
Cdd:pfam02780   1 GKAEILREGD-DVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 695721597  634 TTYGWAKYAGDHG----VMIGIDEFGMSAPSDIVLRELGMSVENI 674
Cdd:pfam02780  80 VAAALAEEAFDGLdapvLRVGGPDFPEPGSADELEKLYGLTPEKI 124
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
121-266 1.64e-12

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 66.12  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 121 HPEYGCTDGVEATTGPLGQGISMAVGMAMAEAhlgkkfnregypvmDHYTYALIGDGDLMEGVAsEAASlAGHLKLgKLI 200
Cdd:cd00568   32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTGQ-ELAT-AVRYGL-PVI 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695721597 201 ALYDSNGISLDGKTSAS------------FTENVGARFEAYGWQYILVEDgfnLEEIDKAIVQAKAeSDKPTIIEIKT 266
Cdd:cd00568   95 VVVFNNGGYGTIRMHQEafyggrvsgtdlSNPDFAALAEAYGAKGVRVED---PEDLEAALAEALA-AGGPALIEVKT 168
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
141-676 1.49e-10

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 64.26  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 141 ISMAVGMAMAEAHLGKKFNregypVMdhytyALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLD--------- 211
Cdd:PRK12315 119 IALATGLAKARDLKGEKGN-----II-----AVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhgglykn 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 212 --------GKTSASFtenvgarFEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYGSEnqgthkvhgs 283
Cdd:PRK12315 188 lkelrdtnGQSENNL-------FKAMGLDYRYVEDGNDIESLIEAFKEVK-DIDHPIVLHIHTLKGKGYQ---------- 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 284 PLGEEgvahaKEVYNWNYpPFTVpeevsqrfkECLQDKgvkaenkwnemFEAYKKEYSDLAQKFsdgfsnkvpntlgdIL 363
Cdd:PRK12315 250 PAEEN-----KEAFHWHM-PFDL---------ETGQSK-----------VPASGESYSSVTLDY--------------LL 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 364 PQYGEDDSIAtraasqkAINAlakevsslwggaadlasSNKTVIaGEGDFQPEsYEGRNIWFGVREfGMACAMNGIMLHG 443
Cdd:PRK12315 290 KKIKEGKPVV-------AINA-----------------AIPGVF-GLKEFRKK-YPDQYVDVGIAE-QESVAFASGIAAN 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 444 GTRIFgstFFVFSDYLKAAI-RLS---AIQKLPVIYVLTHDSVAvGKDgPTHEPIEQLASLRTIPNVQVFRPADGNETSA 519
Cdd:PRK12315 343 GARPV---IFVNSTFLQRAYdQLShdlAINNNPAVMIVFGGSIS-GND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIA 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 520 AWKVALETLDKPtilVLSRQNLDTLPISKEKVFDGVEKGGYVVQGAENEAdgiLIATGSEVGLALKAKEELQKK-GKDVI 598
Cdd:PRK12315 418 MLEWALTQHEHP---VAIRVPEHGVESGPTVDTDYSTLKYEVTKAGEKVA---ILALGDFYELGEKVAKKLKEElGIDAT 491
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 599 VV-----SLPSWERFEAQSEEYKnTVIppelkkrmTIEAGTTYGW-----AKYAGDHGVMI---GID-EFGMSAPSDIVL 664
Cdd:PRK12315 492 LInpkfiTGLDEELLEKLKEDHE-LVV--------TLEDGILDGGfgekiARYYGNSDMKVlnyGAKkEFNDRVPVEELY 562
                        570
                 ....*....|..
gi 695721597 665 RELGMSVENIVD 676
Cdd:PRK12315 563 KRNHLTPEQIVE 574
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
38-236 5.29e-08

Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.


Pssm-ID: 238975 [Multi-domain]  Cd Length: 386  Bit Score: 55.39  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  38 AIQRANS------GHPGLPMGAAPMAYVLWTrHLKinpKTHMNWVNRDRfVLSAGHGSALLYSLAHLAGyDVSMDDLKNF 111
Cdd:cd02017   18 MVHRANKkdlgigGHIATFASAATLYEVGFN-HFF---RARGEGGGGDL-VYFQGHASPGIYARAFLEG-RLTEEQLDNF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 112 REWKSNtPGHPEY----GCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKfnreGYPVM-DHYTYALIGDGDLMEGVASE 186
Cdd:cd02017   92 RQEVGG-GGLSSYphpwLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDR----GLKDTsDQKVWAFLGDGEMDEPESLG 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695721597 187 AASLAGHLKLGKLIALYDSNGISLDGKTSASFT--ENVGARFEAYGWQYILV 236
Cdd:cd02017  167 AIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKiiQELEGIFRGAGWNVIKV 218
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
132-266 1.44e-07

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 53.65  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 132 ATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNGISLD 211
Cdd:cd02000  101 GGNGIVGGQVPLAAGAALALKYRGE----------DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAIS 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695721597 212 GKTS-ASFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKA---ESDKPTIIEIKT 266
Cdd:cd02000  170 TPTSrQTAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVErarAGGGPTLIEAVT 227
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
87-266 2.63e-05

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 45.28  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  87 HGSALLYSLAHLAGYDVSMDD--LKNFREWKSNTPG---HPEYGCTdgveatTGPLGQGISMAVGMAMAEAhlgkkfnre 161
Cdd:cd02002    2 TPEYLAAALAAALPEDAIIVDeaVTNGLPLRDQLPLtrpGSYFTLR------GGGLGWGLPAAVGAALANP--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 162 gypvmDHYTYALIGDGDLMEGVasEAASLAGHLKLGKLIALYDSNGISldgkTSASFTENVGA----------------- 224
Cdd:cd02002   67 -----DRKVVAIIGDGSFMYTI--QALWTAARYGLPVTVVILNNRGYG----ALRSFLKRVGPegpgenapdgldlldpg 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 695721597 225 -RF----EAYGWQYILVEDGfnlEEIDKAIVQAKAEsDKPTIIEIKT 266
Cdd:cd02002  136 iDFaaiaKAFGVEAERVETP---EELDEALREALAE-GGPALIEVVV 178
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
135-346 6.56e-04

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 42.31  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  135 GPLGQGISMAVGMAMAEAHLGKKfnregypvmdHYTYALIGDGDLMEGVASEAASLAGHLKLgKLIALYDSN--GISLDG 212
Cdd:pfam00676 101 GILGAQVPLGAGIALAAKYRGKK----------EVAITLYGDGAANQGDFFEGLNFAALWKL-PVIFVCENNqyGISTPA 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597  213 KTSASfTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKA---ESDKPTIIEIKTtigygsenqgtHKVHGSPLGEEG 289
Cdd:pfam00676 170 ERASA-STTYADRARGYGIPGLHV-DGMDPLAVYQASKFAAErarTGKGPFLIELVT-----------YRYGGHSMSDDP 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 695721597  290 VAH--AKEVYNWNYPPftvpeEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:pfam00676 237 STYrtRDEYEEVRKKK-----DPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKK 290
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
133-267 8.36e-04

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 42.05  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 133 TTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNG--ISl 210
Cdd:COG1071  125 GSGIVGGQLPHAVGAALAAKLRGE----------DEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGyaIS- 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695721597 211 dgkTS---ASFTENVGARFEAYGWQYILVeDGFNLEE----IDKAIVQAKAEsDKPTIIEIKTT 267
Cdd:COG1071  193 ---TPverQTAVETIADRAAGYGIPGVRV-DGNDVLAvyaaVKEAVERARAG-EGPTLIEAKTY 251
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
134-271 2.53e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 40.85  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 134 TGPLGQGISMAVGMAMAEAHLGkkfnregypvMDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDSNGISLDGK 213
Cdd:PLN02234 176 TGHSSTTLSAGLGMAVGRDLKG----------MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTA 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 214 TSASFTENVGA---------------------RFEAYGWQYILVEDGFNLEEIDKAIVQAKA-ESDKPTIIEIKTTIGYG 271
Cdd:PLN02234 246 NLDGPTQPVGAlscalsrlqsncgmiretsstLFEELGFHYVGPVDGHNIDDLVSILETLKStKTIGPVLIHVVTEKGRG 325
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
468-599 6.55e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 39.88  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 468 IQKLPVIYVLTHDSVaVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQN--LDTLP 545
Cdd:PLN02582 446 LQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNgiGVQLP 524
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695721597 546 ISKEKVFDGVEKGGYVVQGAENEadgiLIATGSEVGLALKAKEELQKKGKDVIV 599
Cdd:PLN02582 525 PNNKGIPIEVGKGRILLEGERVA----LLGYGTAVQSCLAAASLLERHGLSATV 574
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
125-224 9.22e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 39.11  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695721597 125 GCTDGVEATTGPLGQG-----ISMAVGMAMAEAHLGKKFNregypvmdhyTYALIGDGDLMEGVASEAASLAGHLKLGKL 199
Cdd:PLN02582 129 GFTKRAESEYDCFGTGhssttISAGLGMAVGRDLKGKKNN----------VVAVIGDGAMTAGQAYEAMNNAGYLDSDMI 198
                         90       100
                 ....*....|....*....|....*
gi 695721597 200 IALYDSNGISLDGKTSASFTENVGA 224
Cdd:PLN02582 199 VILNDNKQVSLPTATLDGPAPPVGA 223
 
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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