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Conserved domains on  [gi|1755489186|gb|KAB1086570|]
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pyruvate dehydrogenase complex E1 component subunit beta [Neorhizobium galegae]

Protein Classification

pyruvate dehydrogenase complex E1 component subunit beta( domain architecture ID 11485653)

pyruvate dehydrogenase (PDH) complex E1 component subunit beta, together with subunit alpha, forms the E1 component of the PDH complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-464 0e+00

pyruvate dehydrogenase subunit beta; Provisional


:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 974.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  81 GESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 161 NVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 241 YMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHQFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 321 VPKLDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186 401 GYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAVKTVCYK 464
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-464 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 974.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  81 GESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 161 NVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 241 YMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHQFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 321 VPKLDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186 401 GYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAVKTVCYK 464
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 139-463 0e+00

Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 439793 [Multi-domain]  Cd Length: 325  Bit Score: 535.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 299 AIRDPNPVIFLENEILYGHQFEVPKlDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 1755489186 459 KTVCY 463
Cdd:COG0022   320 RELLA 324
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 146-312 1.79e-105

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain]  Cd Length: 167  Bit Score: 310.56  E-value: 1.79e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 146 EALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 226 MQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1755489186 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 143-316 3.32e-52

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: 173.89  E-value: 3.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 143 TVREALRDAMAEEMRRDENVFVMGEEVAeyQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAG-LKPIVEFMT 221
Cdd:pfam02779   4 ATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 222 FNFAMqaidqiINSAAKTLYMSGGQMGAP-IVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAI 300
Cdd:pfam02779  82 SDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAI 155

                         170
                  ....*....|....*...
gi 1755489186 301 R--DPNPVIFLENEILYG 316
Cdd:pfam02779 156 RrdGRKPVVLRLPRQLLR 173
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-123 6.01e-37

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 140.70  E-value: 6.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQDGESS 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1755489186  85 DSIGSAAPAKEAPKVAP---QVEQEEKPTATGSASASVPAQP 123
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPkpsEIAPTAPPSAPKPSPAPQKQSP 123
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 192-316 1.78e-33

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: 122.98  E-value: 1.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  192 VDTPITEHGFAGVGVGAAMAGLKPIVEFMtFNFAMQAIDQIinsaaktlyMSGGQMGA-PIVFR-GPNGAAARVGA-QHS 268
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGNvPVVFRhDGGGGVGEDGPtHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1755489186  269 QDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNP-VIFLENEILYG 316
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-464 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 974.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  81 GESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 161 NVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 241 YMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHQFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 321 VPKLDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186 401 GYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAVKTVCYK 464
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 139-464 0e+00

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 579.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVE 218
Cdd:PRK09212    1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKA 298
Cdd:PRK09212   81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 299 AIRDPNPVIFLENEILYGHQFEVPKlDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIR 378
Cdd:PRK09212  161 AIRDPNPVIFLENEILYGHSHEVPE-EEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:PRK09212  240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAV 319


                  ....*.
gi 1755489186 459 KTVCYK 464
Cdd:PRK09212  320 KKVCYR 325
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 139-463 0e+00

Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 439793 [Multi-domain]  Cd Length: 325  Bit Score: 535.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 299 AIRDPNPVIFLENEILYGHQFEVPKlDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 1755489186 459 KTVCY 463
Cdd:COG0022   320 RELLA 324
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 135-464 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 521.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 135 AGTEMvmtTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLK 214
Cdd:PLN02683   23 AAKEM---TVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 215 PIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKG 294
Cdd:PLN02683  100 PVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 295 LLKAAIRDPNPVIFLENEILYGHQFEVPK--LD-DFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVEL 371
Cdd:PLN02683  180 LLKAAIRDPDPVVFLENELLYGESFPVSAevLDsSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEV 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 372 IDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNV 451
Cdd:PLN02683  260 INLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQV 339

                         330
                  ....*....|...
gi 1755489186 452 GEVVQAVKTVCYK 464
Cdd:PLN02683  340 EDIVRAAKRACYR 352
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 133-462 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 519.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 133 IPAGTEMVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAG 212
Cdd:PTZ00182   26 TESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 213 LKPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADA 292
Cdd:PTZ00182  106 LRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 293 KGLLKAAIRDPNPVIFLENEILYGHQFEVPKLDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELI 372
Cdd:PTZ00182  186 KGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 373 DLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVG 452
Cdd:PTZ00182  266 DLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKE 345

                         330
                  ....*....|
gi 1755489186 453 EVVQAVKTVC 462
Cdd:PTZ00182  346 KVVEAAKRVL 355
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 146-312 1.79e-105

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain]  Cd Length: 167  Bit Score: 310.56  E-value: 1.79e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 146 EALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 226 MQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1755489186 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 139-462 4.58e-104

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 312.83  E-value: 4.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVE 218
Cdd:CHL00144    1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKA 298
Cdd:CHL00144   81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 299 AIRDPNPVIFLENEILYGHQFEVPKlDDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIR 378
Cdd:CHL00144  161 AIRSNNPVIFFEHVLLYNLKEEIPD-NEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:CHL00144  240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319


                  ....
gi 1755489186 459 KTVC 462
Cdd:CHL00144  320 EQII 323
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 143-316 3.32e-52

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: 173.89  E-value: 3.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 143 TVREALRDAMAEEMRRDENVFVMGEEVAeyQGAYKITQGLLQEFGARRVVDTPITEHGFAGVGVGAAMAG-LKPIVEFMT 221
Cdd:pfam02779   4 ATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 222 FNFAMqaidqiINSAAKTLYMSGGQMGAP-IVFRGPNGAAARVGAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAI 300
Cdd:pfam02779  82 SDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAI 155

                         170
                  ....*....|....*...
gi 1755489186 301 R--DPNPVIFLENEILYG 316
Cdd:pfam02779 156 RrdGRKPVVLRLPRQLLR 173
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 332-451 6.26e-46

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: 155.45  E-value: 6.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 332 GKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEI 411
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1755489186 412 ATRVMQQAFDYLDAPILTIAGKDVPMPYAA-NLEKLALPNV 451
Cdd:pfam02780  81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTP 121
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-123 6.01e-37

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 140.70  E-value: 6.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQDGESS 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1755489186  85 DSIGSAAPAKEAPKVAP---QVEQEEKPTATGSASASVPAQP 123
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPkpsEIAPTAPPSAPKPSPAPQKQSP 123
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-131 1.85e-36

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 138.77  E-value: 1.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTEnVKVNTKIAVLLQD 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1755489186  81 GEssdsiGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADP 131
Cdd:PRK11856   80 GE-----AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAA 125
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
139-400 5.84e-35

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


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 132.13  E-value: 5.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVFVMGEEVAEYqgaykitqGLLQEFGAR---RVVDTPITEHGFAGVGVGAAMAGLKP 215
Cdd:COG3958     1 MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGS--------TKLDKFAKAfpdRFFNVGIAEQNMVGVAAGLALAGKIP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 216 IVefMTF-NFA-MQAIDQIINSAAktlYMsggQMGAPIVFRGPNGAAARVGAQHsQ---DYAaWYSQIPGLKVVMPYTAA 290
Cdd:COG3958    73 FV--STFaPFLtGRAYEQIRNDIA---YP---NLNVKIVGSHAGLSYGEDGATH-QaleDIA-LMRALPNMTVIVPADAV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 291 DAKGLLKAAI-----------RDPNPVIFLEneilyGHQFEvpklddfvlpIGKARIHKKGKDVTIVSFGIgMTY-SLKA 358
Cdd:COG3958   143 ETEAAVRAAAehdgpvylrlgRGAVPVVYDE-----DYEFE----------IGKARVLREGKDVTIIATGI-MVAeALEA 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1755489186 359 IAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:COG3958   207 AELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEE 248
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 192-316 1.78e-33

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: 122.98  E-value: 1.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  192 VDTPITEHGFAGVGVGAAMAGLKPIVEFMtFNFAMQAIDQIinsaaktlyMSGGQMGA-PIVFR-GPNGAAARVGA-QHS 268
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGNvPVVFRhDGGGGVGEDGPtHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1755489186  269 QDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRDPNP-VIFLENEILYG 316
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 4-123 2.84e-29

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 120.34  E-value: 2.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTENVKVNTKIAVLLQDGE- 82
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEd 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1755489186  83 --------SSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQP 123
Cdd:PLN02744  194 igkfkdykPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAP 242
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-77 1.17e-28

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 107.85  E-value: 1.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVL 77
Cdd:COG0508     1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEG-DTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 3-77 5.09e-28

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 105.95  E-value: 5.09e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755489186   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTEnVKVNTKIAVL 77
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 150-431 2.57e-22

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: 100.09  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 150 DAMAEEMRRDENVfvmgeeVAeyqgaykIT----QGL-LQEFGAR---RVVDTPITE-HG--FAGvgvGAAMAGLKPIVE 218
Cdd:COG1154   325 DTLVELAEKDPRI------VA-------ITaampEGTgLDKFAERfpdRFFDVGIAEqHAvtFAA---GLATEGLKPVVA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 219 -FMTFnfaMQ-AIDQIINSAAktlymsggQMGAPIVF---R----GPNGAAarvgaqH--SQDYAaWYSQIPGLKVVMPY 287
Cdd:COG1154   389 iYSTF---LQrAYDQVIHDVA--------LQNLPVTFaidRaglvGADGPT------HhgVFDLS-YLRCIPNMVIMAPK 450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 288 TAADAKGLLKAAIRDPNPVIfleneILY----GHQFEVPKLDDfVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELE 363
Cdd:COG1154   451 DENELRHMLYTALAYDGPTA-----IRYprgnGPGVELPAELE-PLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLA 524

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755489186 364 KEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:COG1154   525 AEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFLADAG---LDVPVLRLG 589
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-137 3.90e-20

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 92.20  E-value: 3.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVlLQD 80
Cdd:PRK05704    1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEG-DTVTVGQVLGR-IDE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755489186  81 GESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASvPAQPKV--EAAADPDIPAGT 137
Cdd:PRK05704   79 GAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALS-PAARKLaaENGLDASAVKGT 136
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 183-431 2.51e-19

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 90.53  E-value: 2.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 183 LQEFGAR---RVVDTPITE-HG--FAGvgvGAAMAGLKPIVE-FMTFnfaMQ-AIDQIINSAAktlymsggQMGAPIVF- 253
Cdd:PRK05444  312 LVKFSKRfpdRYFDVGIAEqHAvtFAA---GLATEGLKPVVAiYSTF---LQrAYDQVIHDVA--------LQNLPVTFa 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 254 --R-GPNGAAarvGAQH--SQDYAawY-SQIPGLKVVMPYTAADAKGLLKAAIR-DPNPVIfleneILY--GHQFEVPKL 324
Cdd:PRK05444  378 idRaGLVGAD---GPTHqgAFDLS--YlRCIPNMVIMAPSDENELRQMLYTALAyDDGPIA-----IRYprGNGVGVELP 447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 325 DDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEkegiDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQ 404
Cdd:PRK05444  448 ELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIM 523

                         250       260
                  ....*....|....*....|....*..
gi 1755489186 405 SSVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:PRK05444  524 GGFGSAVLEFLADHG---LDVPVLNLG 547
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 146-308 4.35e-19

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: 84.03  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 146 EALRDAMAEEMRRDENVFVMGEEVAEYqgaykitqGLLQEFGAR---RVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTF 222
Cdd:cd07033     1 KAFGEALLELAKKDPRIVALSADLGGS--------TGLDKFAKKfpdRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 223 nFAMQAIDQIINSAAktlymsggQMGAPIVFRGpNGAAARVGA----QHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKA 298
Cdd:cd07033    73 -FLQRAYDQIRHDVA--------LQNLPVKFVG-THAGISVGEdgptHQGIEDIALLRAIPNMTVLRPADANETAAALEA 142

                         170
                  ....*....|
gi 1755489186 299 AIRDPNPVIF 308
Cdd:cd07033   143 ALEYDGPVYI 152
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 5-158 1.09e-18

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 87.82  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVLLQDGESS 84
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEG-DTVEVGAPLSEIDTGGAPP 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186  85 DSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAgteMVMTTVREALRDAMAEEMRR 158
Cdd:PTZ00144  126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAK---PPPTPVARADPRETRVPMSR 196
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 5-107 2.07e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 86.54  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTEnVKVNTKIAVlLQDGESS 84
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGET-LPVGALLAV-VADAEVS 82

                          90       100
                  ....*....|....*....|...
gi 1755489186  85 DSIGSAAPAKEAPKVAPQVEQEE 107
Cdd:PRK14875   83 DAEIDAFIAPFARRFAPEGIDEE 105
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 150-302 2.47e-18

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; 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 group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.


Pssm-ID: 132915 [Multi-domain]  Cd Length: 154  Bit Score: 81.62  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 150 DAMAEEMRRDENVFVMGEEVAEYQGAYkitqGLLQEFGARRVvDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAI 229
Cdd:cd06586     1 AAFAEVLTAWGVRHVFGYPGDEISSLL----DALREGDKRII-DTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755489186 230 DQIINSAAKtlymsggqmGAPIVFR-GPNGAAARV-GAQHSQDYAAWYSQIPGLKVVMPYTAADAKGLLKAAIRD 302
Cdd:cd06586    76 NGLADAAAE---------HLPVVFLiGARGISAQAkQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA 141
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 3-138 1.74e-17

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 84.01  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTeNVKVNTKIAVLLQDGE 82
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGD-TVESGQVLAILEEGND 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755489186  83 SSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTE 138
Cdd:TIGR01347  80 ATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTG 135
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-133 5.71e-17

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 83.33  E-value: 5.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSpTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVLlqd 80
Cdd:PRK11855    1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVG-DTVSVGGLLAVI--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1755489186  81 gESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDI 133
Cdd:PRK11855   76 -EAAGAAAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDI 127
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 3-145 1.33e-16

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 82.18  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   3 IDILMPALSpTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVllqdge 82
Cdd:PRK11855  120 VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVG-DKVSVGSLLVV------ 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186  83 ssdsIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVR 145
Cdd:PRK11855  192 ----IEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVR 250
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-165 4.18e-16

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 80.18  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVLLQDGE 82
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  83 SSDSIGSA--APAKEAPKVAPQVEQEEKPTATGSASASVPAQPKV-----EAAADPDIPAGT-EMVMTTVReaLRDAMAE 154
Cdd:PLN02226  171 AASQVTPSqkIPETTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSppppkQSAKEPQLPPKErERRVPMTR--LRKRVAT 248

                         170
                  ....*....|.
gi 1755489186 155 EMRRDENVFVM 165
Cdd:PLN02226  249 RLKDSQNTFAL 259
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 1-140 2.63e-14

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 75.05  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAgTENVKVNTKIAVLlqd 80
Cdd:TIGR02927   1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAII--- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755489186  81 GESSDSIGSAAPAKEAPKVAPQVE-QEEKPTATGSASASVPAQPKVEAAADP-DIPAGTEMV 140
Cdd:TIGR02927  77 GEPGEAGSEPAPAAPEPEAAPEPEaPAPAPTPAAEAPAPAAPQAGGSGEATEvKMPELGESV 138
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 4-77 2.68e-14

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 67.62  E-value: 2.68e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186   4 DILMPALSPTMEEGTlSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVL 77
Cdd:pfam00364   2 EIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEG-DTVEVGDPLAKI 73
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 4-66 1.11e-13

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 65.93  E-value: 1.11e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTE 66
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-155 9.39e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 70.42  E-value: 9.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   1 MPIDILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVLlqd 80
Cdd:PRK11854    1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVG-DKVETGALIMIF--- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755489186  81 gESSDSIGSAAPAKEAPKVAPqveqeekptatgsASASVPAQPKVEAAADPDIpAGTEMVMTTVREALRDAMAEE 155
Cdd:PRK11854   75 -ESADGAADAAPAQAEEKKEA-------------APAAAPAAAAAKDVHVPDI-GSDEVEVTEILVKVGDTVEAE 134
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 181-447 1.02e-12

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 70.14  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 181 GLLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTfNFAMQAIDQIInsaaktlyMSGGQMGAPIVF----RGP 256
Cdd:PRK12571  353 DKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLL--------HDVALQNLPVRFvldrAGL 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 257 NGAAarvGAQHSQDY-AAWYSQIPGLKVVMPYTAADAKGLLKAAI---RDPNPVIFLENEilyGHQFEVPKLDDfVLPIG 332
Cdd:PRK12571  424 VGAD---GATHAGAFdLAFLTNLPNMTVMAPRDEAELRHMLRTAAahdDGPIAVRFPRGE---GVGVEIPAEGT-ILGIG 496

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 333 KARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDlPTVIESVKKTGRLVTVEEGYPQSSVGTEIA 412
Cdd:PRK12571  497 KGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVL 575

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1755489186 413 TRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLA 447
Cdd:PRK12571  576 HHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYA 610
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 139-413 2.38e-11

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 65.80  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 139 MVMTTVREALRDAMAEEMRRDENVfvmgeeVAeyqgaykITQGLLQEFG--------ARRVVDTPITEHGFAGVGVGAAM 210
Cdd:PRK12315  275 ASGESYSSVTLDYLLKKIKEGKPV------VA-------INAAIPGVFGlkefrkkyPDQYVDVGIAEQESVAFASGIAA 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 211 AGLKPIVeFMTFNFAMQAIDQI-----INSAAKTLYMSGGQMGApivfrgpngaaARVGAQHSQDYAaWYSQIPGLKVVM 285
Cdd:PRK12315  342 NGARPVI-FVNSTFLQRAYDQLshdlaINNNPAVMIVFGGSISG-----------NDVTHLGIFDIP-MISNIPNLVYLA 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 286 PYTAADAKGLLKAAIRDPN-PVIFL--ENEILYGHqfevPKLDDFVLPigKARIHKKGKDVTIVsfGIGMTYSL-KAIAE 361
Cdd:PRK12315  409 PTTKEELIAMLEWALTQHEhPVAIRvpEHGVESGP----TVDTDYSTL--KYEVTKAGEKVAIL--ALGDFYELgEKVAK 480

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755489186 362 L--EKEGIDVELIDLRTIRPMDLPTvIESVKKTGRLV-TVEEGYPQSSVGTEIAT 413
Cdd:PRK12315  481 KlkEELGIDATLINPKFITGLDEEL-LEKLKEDHELVvTLEDGILDGGFGEKIAR 534
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-222 3.06e-11

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 65.28  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  15 EEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTEnVKVNTKIAVLlqDGESSDSIGSAAPAK 94
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTL--SVAGSTPATAPAPAS 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  95 -EAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVREalrdamaeemrrdenvfvMGEEVAEYQ 173
Cdd:TIGR01348 205 aQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLARE------------------FGVDLSAVK 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1755489186 174 GAYKitQGLLQEFGARRVVDTPI--TEHGFAGVGVGAAMAGLKPIVEFMTF 222
Cdd:TIGR01348 267 GTGI--KGRILREDVQRFVKEPSvrAQAAAASAAGGAPGALPWPNVDFSKF 315
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 4-150 3.56e-11

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 65.42  E-value: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLL------IEAGTENVKVNTKIAVL 77
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRapeddtVEVGTVLAIIGDANAAP 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186  78 LQDGESSDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKveAAADPDIPAGTEMVMTTVREALRD 150
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPA--AAAPVSSGDSGPYVTPLVRKLAKD 278
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-146 1.54e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 63.48  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   4 DILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGTEnVKVNTKIAVLlqdges 83
Cdd:PRK11854  208 DVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRF------ 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186  84 sDSIGSAAPAKEAPKVAPQVEQEEKPTATGSASASVPAQPKVEAAADPDIPAGTEMVMTTVRE 146
Cdd:PRK11854  279 -EVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLARE 340
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-155 1.29e-08

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 57.32  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186   4 DILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVLlqdges 83
Cdd:PRK11854  107 DVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVG-DKVSTGSLIMVF------ 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755489186  84 sdSIGSAAPAkEAPKVAPQVEQEEKPTATGSASasvpaqpKVEAaadPDIpAGTEMVMTTVREALRDAMAEE 155
Cdd:PRK11854  178 --EVAGEAPA-AAPAAAEAAAPAAAPAAAAGVK-------DVNV---PDI-GGDEVEVTEVMVKVGDKVEAE 235
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-155 4.23e-08

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 55.27  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  15 EEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVL-LQDGES--SDSIGSAA 91
Cdd:TIGR01348  12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVG-DTLPVGGVIATLeVGAGAQaqAEAKKEAA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755489186  92 PAKEAPKVAPQVEQEEKPTATGSASasvpaqpkVEAAADPDIPAGTEMVMTTVREALRDAMAEE 155
Cdd:TIGR01348  91 PAPTAGAPAPAAQAQAAPAAGQSSG--------VQEVTVPDIGDIEKVTVIEVLVKVGDTVSAD 146
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 182-401 2.90e-07

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 52.79  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 182 LLQEFGAR---RVVDTPITEHGFAGVGVGAAMAGLKPIVEFMTfNFAMQAIDQIINSA------AKTLYMSGGQMGAPiv 252
Cdd:PLN02234  389 MLNLFESRfptRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVdlqklpVRFAIDRAGLMGAD-- 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 253 frGPNGAAARvgaqhsqdYAAWYSQIPGLKVVMPYTAADAKGLL-KAAIRDPNPVIFLENEilyGHQFEV---PKLDDFV 328
Cdd:PLN02234  466 --GPTHCGAF--------DVTFMACLPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYHR---GNGIGVslpPGNKGVP 532

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186 329 LPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02234  533 LQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 143-401 4.10e-07

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 52.41  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 143 TVREALRDAMAEEMRRDENVFVMgeEVAEYQGAYKITqglLQEFGARRVVDTPITEHGFAGVGVGAAMAGLKPIVeFMTF 222
Cdd:PLN02225  382 TYSDCFVEALVMEAEKDRDIVVV--HAGMEMDASLIT---FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPS 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 223 NFAMQAIDQIIN------SAAKTLYMSGGQMGAPivfrGPngaaARVGAQHsqdyAAWYSQIPGLKVVMPytaADAKGLL 296
Cdd:PLN02225  456 AFLQRAYDQVVHdvdrqrKAVRFVITSAGLVGSD----GP----VQCGAFD----IAFMSSLPNMIAMAP---ADEDELV 520

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186 297 K----AAIRDPNPVIF-LENEILYGHQFEVPKldDFVLPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVEL 371
Cdd:PLN02225  521 NmvatAAYVTDRPVCFrFPRGSIVNMNYLVPT--GLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTV 598

                         250       260       270
                  ....*....|....*....|....*....|
gi 1755489186 372 IDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02225  599 ADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 17-77 1.99e-06

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 45.10  E-value: 1.99e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755489186  17 GTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNTKIAVL 77
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEG-DQVEAGQLLVVI 67
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 329-401 1.25e-05

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 47.59  E-value: 1.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755489186 329 LPIGKARIHKKGKDVTIVSFGIGMTYSLKAIAELEKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02582  532 IEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 19-129 2.94e-04

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 43.17  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755489186  19 LSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAGtENVKVNT---KIAVLLQDGESSDSIGSAAPAKE 95
Cdd:PLN02528   15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG-DIVKVGEtllKIMVEDSQHLRSDSLLLPTDSSN 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1755489186  96 APKVApqvEQEEKptatGSASASVPAQPKVEAAA 129
Cdd:PLN02528   94 IVSLA---ESDER----GSNLSGVLSTPAVRHLA 120
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 9-64 2.84e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 40.21  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755489186   9 ALSPTMEeGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLIEAG 64
Cdd:PRK09282  524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
 
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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