NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2127527159|ref|WP_227702746|]
View 

pyruvate dehydrogenase complex E1 component subunit beta [Rhizobium petrolearium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 976.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLAD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 161 DVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 241 YMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 321 VPKLDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159 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: 976.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLAD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 161 DVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 241 YMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 321 VPKLDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159 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: 538.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 299 AIRDPNPVIFLENEILYGHHFEVPKlDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 2127527159 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 8.80e-107

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: 313.65  E-value: 8.80e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 146 EALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 226 MQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 2127527159 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 141-316 6.20e-53

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: 175.82  E-value: 6.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAeyQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAG-LRPIVEF 219
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 220 MTFNFAMqaidqiINSAAKTLYMSGGQMGAP-IVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:pfam02779  80 TFSDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153

                         170       180
                  ....*....|....*....|
gi 2127527159 299 AIR--DPNPVIFLENEILYG 316
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLR 173
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-131 3.02e-40

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: 149.56  E-value: 3.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLADGESA 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2127527159  85 ADIGSEASAETPKAAAPQvPQEEKPTETGSASAPVPA-QPIAPTASDP 131
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPK-PSEIAPTAPPSAPKPSPApQKQSPEPSSP 128
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 141-316 1.95e-32

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: 119.90  E-value: 1.95e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  141 TMTVREALRDAMAEEMrrdedvfvmgeevaeyqgaykitqgllqefgprrvVDTPITEHGFAGVGVGAAMAGLRPIVEFM 220
Cdd:smart00861   2 KIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIF 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  221 tFNFAMQAIDQIinsaaktlyMSGGQMGA-PIVFR-GPNGAAARVAA-QHSQDYAAWYSHVPGLKVVMPYTAADAKGLLK 297
Cdd:smart00861  47 -FTFFDRAKDQI---------RSAGASGNvPVVFRhDGGGGVGEDGPtHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLR 116

                          170       180
                   ....*....|....*....|
gi 2127527159  298 AAIRDPNP-VIFLENEILYG 316
Cdd:smart00861 117 AAIRDDGPvVIRLERKSLYR 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: 976.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLAD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 161 DVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFAMQAIDQIINSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 241 YMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFE 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 321 VPKLDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159 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: 584.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVE 218
Cdd:PRK09212    1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:PRK09212   81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 299 AIRDPNPVIFLENEILYGHHFEVPKlDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIR 378
Cdd:PRK09212  161 AIRDPNPVIFLENEILYGHSHEVPE-EEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:PRK09212  240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAV 319


                  ....*.
gi 2127527159 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: 538.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 299 AIRDPNPVIFLENEILYGHHFEVPKlDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 2127527159 459 KTVCY 463
Cdd:COG0022   320 RELLA 324
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: 523.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 133 IPAGTEMVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAG 212
Cdd:PTZ00182   26 TESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 213 LRPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADA 292
Cdd:PTZ00182  106 LRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 293 KGLLKAAIRDPNPVIFLENEILYGHHFEVPKLDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELI 372
Cdd:PTZ00182  186 KGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 373 DLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVG 452
Cdd:PTZ00182  266 DLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKE 345

                         330
                  ....*....|
gi 2127527159 453 EVVQAVKTVC 462
Cdd:PTZ00182  346 KVVEAAKRVL 355
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 142-464 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 520.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 142 MTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMT 221
Cdd:PLN02683   27 MTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 222 FNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIR 301
Cdd:PLN02683  107 FNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 302 DPNPVIFLENEILYGHHFEVPK--LD-DFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIR 378
Cdd:PLN02683  187 DPDPVVFLENELLYGESFPVSAevLDsSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIR 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:PLN02683  267 PLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQVEDIVRAA 346


                  ....*.
gi 2127527159 459 KTVCYK 464
Cdd:PLN02683  347 KRACYR 352
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 146-312 8.80e-107

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: 313.65  E-value: 8.80e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 146 EALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 226 MQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 2127527159 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 139-462 1.80e-102

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 308.98  E-value: 1.80e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVE 218
Cdd:CHL00144    1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:CHL00144   81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 299 AIRDPNPVIFLENEILYGHHFEVPKlDDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIR 378
Cdd:CHL00144  161 AIRSNNPVIFFEHVLLYNLKEEIPD-NEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 379 PMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVGEVVQAV 458
Cdd:CHL00144  240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319


                  ....
gi 2127527159 459 KTVC 462
Cdd:CHL00144  320 EQII 323
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 141-316 6.20e-53

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: 175.82  E-value: 6.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAeyQGAYKITQGLLQEFGPRRVVDTPITEHGFAGVGVGAAMAG-LRPIVEF 219
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 220 MTFNFAMqaidqiINSAAKTLYMSGGQMGAP-IVFRGPNGAAARVAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKA 298
Cdd:pfam02779  80 TFSDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153

                         170       180
                  ....*....|....*....|
gi 2127527159 299 AIR--DPNPVIFLENEILYG 316
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLR 173
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 332-451 5.00e-44

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: 150.44  E-value: 5.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 332 GKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEI 411
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2127527159 412 ATRVMQQAFDYLDAPILTIAGKDVPMPYAA-NLEKLALPNV 451
Cdd:pfam02780  81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTP 121
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-131 3.02e-40

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: 149.56  E-value: 3.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLADGESA 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2127527159  85 ADIGSEASAETPKAAAPQvPQEEKPTETGSASAPVPA-QPIAPTASDP 131
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPK-PSEIAPTAPPSAPKPSPApQKQSPEPSSP 128
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-129 2.36e-39

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 146.47  E-value: 2.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTEnVKVNTKIAVLLAD 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTAS 129
Cdd:PRK11856   80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKAS 128
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 141-316 1.95e-32

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: 119.90  E-value: 1.95e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  141 TMTVREALRDAMAEEMrrdedvfvmgeevaeyqgaykitqgllqefgprrvVDTPITEHGFAGVGVGAAMAGLRPIVEFM 220
Cdd:smart00861   2 KIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIF 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  221 tFNFAMQAIDQIinsaaktlyMSGGQMGA-PIVFR-GPNGAAARVAA-QHSQDYAAWYSHVPGLKVVMPYTAADAKGLLK 297
Cdd:smart00861  47 -FTFFDRAKDQI---------RSAGASGNvPVVFRhDGGGGVGEDGPtHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLR 116

                          170       180
                   ....*....|....*....|
gi 2127527159  298 AAIRDPNP-VIFLENEILYG 316
Cdd:smart00861 117 AAIRDDGPvVIRLERKSLYR 136
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-77 8.29e-29

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: 108.23  E-value: 8.29e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVL 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 1.52e-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: 107.49  E-value: 1.52e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127527159   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTEnVKVNTKIAVL 77
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 4-129 5.63e-28

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 116.49  E-value: 5.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTENVKVNTKIAVLLADGES 83
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEED 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2127527159  84 AADIG-----SEASAETPKAA-APQVPQEEKPTETGSASAPVPAQPIAPTAS 129
Cdd:PLN02744  194 IGKFKdykpsSSAAPAAPKAKpSPPPPKEEEVEKPASSPEPKASKPSAPPSS 245
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 150-431 1.35e-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: 100.86  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 150 DAMAEEMRRDEDVfvmgeeVAeyqgaykIT------QGLL---QEFgPRRVVDTPITE-HG--FAGvgvGAAMAGLRPIV 217
Cdd:COG1154   325 DTLVELAEKDPRI------VA-------ITaampegTGLDkfaERF-PDRFFDVGIAEqHAvtFAA---GLATEGLKPVV 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 218 E-FMTFnfaMQ-AIDQIINSAAktlymsggQMGAPIVF---R----GPNGAAarvaaqH--SQDYAaWYSHVPGLKVVMP 286
Cdd:COG1154   388 AiYSTF---LQrAYDQVIHDVA--------LQNLPVTFaidRaglvGADGPT------HhgVFDLS-YLRCIPNMVIMAP 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 287 YTAADAKGLLKAAIRDPNPVIfleneILY----GHHFEVPKLDDfVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEEL 362
Cdd:COG1154   450 KDENELRHMLYTALAYDGPTA-----IRYprgnGPGVELPAELE-PLPIGKGEVLREGKDVAILAFGTMVAEALEAAERL 523

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127527159 363 SKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:COG1154   524 AAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFLADAG---LDVPVLRLG 589
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-137 5.05e-22

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 97.60  E-value: 5.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLLAD 80
Cdd:PRK05704    1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEG-DTVTVGQVLGRIDEG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGT 137
Cdd:PRK05704   80 AAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGT 136
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 5-122 3.92e-19

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 88.85  E-value: 3.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTEnVKVNTKIAVlLADGESA 84
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGET-LPVGALLAV-VADAEVS 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2127527159  85 adiGSEASAETPKAAAPQVPQEEkpTETGSASAPVPAQ 122
Cdd:PRK14875   83 ---DAEIDAFIAPFARRFAPEGI--DEEDAGPAPRKAR 115
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 146-308 4.27e-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: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 146 EALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKitqglLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFnFA 225
Cdd:cd07033     1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK-----FAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 226 MQAIDQIINSAAktlymsggQMGAPIVFR--------GPNGaaarvAAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLK 297
Cdd:cd07033    75 QRAYDQIRHDVA--------LQNLPVKFVgthagisvGEDG-----PTHQGIEDIALLRAIPNMTVLRPADANETAAALE 141

                         170
                  ....*....|.
gi 2127527159 298 AAIRDPNPVIF 308
Cdd:cd07033   142 AALEYDGPVYI 152
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 3-138 1.61e-18

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: 87.10  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTeNVKVNTKIAVlLADGE 82
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGD-TVESGQVLAI-LEEGN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2127527159  83 SAADIGSEASAEtPKAAAPQVPQEEKPTETGSA--SAPVPAQPIAPTASDPDIPAGTE 138
Cdd:TIGR01347  79 DATAAPPAKSGE-EKEETPAASAAAAPTAAANRpsLSPAARRLAKEHGIDLSAVPGTG 135
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 150-302 1.75e-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: 82.01  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 150 DAMAEEMRRDEDVFVMGEEVAEYQGAYkitqGLLQEfGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTFNFAMQAI 229
Cdd:cd06586     1 AAFAEVLTAWGVRHVFGYPGDEISSLL----DALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127527159 230 DQIINSAAKtlymsggqmGAPIVFR-GPNGAAARV-AAQHSQDYAAWYSHVPGLKVVMPYTAADAKGLLKAAIRD 302
Cdd:cd06586    76 NGLADAAAE---------HLPVVFLiGARGISAQAkQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA 141
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 5-158 1.76e-18

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 87.05  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   5 ILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLLADGESA 84
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEG-DTVEVGAPLSEIDTGGAPP 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127527159  85 ADIGSEASAETPKAAAPQVPQEEKPTETG-SASAPVPAQPIAPTASDPDIPAGTEMVTMTVREALRDAMAeEMRR 158
Cdd:PTZ00144  126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPpAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPMS-RMRQ 199
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 184-431 4.68e-18

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 86.67  E-value: 4.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 184 QEFgPRRVVDTPITE-HG--FAGvgvGAAMAGLRPIVE-FMTFnfaMQ-AIDQIINSAAktlymsggQMGAPIVF---R- 254
Cdd:PRK05444  317 KRF-PDRYFDVGIAEqHAvtFAA---GLATEGLKPVVAiYSTF---LQrAYDQVIHDVA--------LQNLPVTFaidRa 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 255 ---GPNGAAarvaaqH--SQDYAawY-SHVPGLKVVMPYTAADAKGLLKAAIR-DPNPVIfleneILY--GHHFEVPKLD 325
Cdd:PRK05444  382 glvGADGPT------HqgAFDLS--YlRCIPNMVIMAPSDENELRQMLYTALAyDDGPIA-----IRYprGNGVGVELPE 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 326 DFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSkegiDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQS 405
Cdd:PRK05444  449 LEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMG 524

                         250       260
                  ....*....|....*....|....*.
gi 2127527159 406 SVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:PRK05444  525 GFGSAVLEFLADHG---LDVPVLNLG 547
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-133 6.83e-18

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 86.03  E-value: 6.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSpTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLLAD 80
Cdd:PRK11855    1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVG-DTVSVGGLLAVIEAA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2127527159  81 GESAAdigseasAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASD---PDI 133
Cdd:PRK11855   79 GAAAA-------AAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEvkvPDI 127
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 3-145 1.10e-15

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 79.10  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   3 IDILMPALSpTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVlladge 82
Cdd:PRK11855  120 VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVG-DKVSVGSLLVV------ 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127527159  83 saadIGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGTEMVTMTVR 145
Cdd:PRK11855  192 ----IEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVR 250
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 1-141 5.87e-15

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: 76.97  E-value: 5.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAgTENVKVNTKIAVLLAD 80
Cdd:TIGR02927   1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159  81 GESaadiGSEASAETPKAAAPQVPQEEKPTETGSASAPVPAQPIAP---TASDPDIPAGTEMVT 141
Cdd:TIGR02927  80 GEA----GSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGgsgEATEVKMPELGESVT 139
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 4-77 8.20e-15

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: 69.17  E-value: 8.20e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159   4 DILMPALSPTMEEGTlSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVL 77
Cdd:pfam00364   2 EIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEG-DTVEVGDPLAKI 73
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-165 2.23e-14

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 74.79  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   3 IDILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLLADGE 82
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  83 SAADIG-SEASAETPkAAAPQVPQEEKpTETGSASAPVPAQPIAP--------TASDPDIPAG--TEMVTMTvreALRDA 151
Cdd:PLN02226  171 AASQVTpSQKIPETT-DPKPSPPAEDK-QKPKVESAPVAEKPKAPssppppkqSAKEPQLPPKerERRVPMT---RLRKR 245

                         170
                  ....*....|....
gi 2127527159 152 MAEEMRRDEDVFVM 165
Cdd:PLN02226  246 VATRLKDSQNTFAL 259
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 4-66 2.60e-14

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: 67.85  E-value: 2.60e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127527159   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTE 66
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 4-150 1.20e-12

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: 70.04  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   4 DILMPALSPTMEEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAgTENVKVNTKIAVL---LAD 80
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIgdaNAA 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127527159  81 GESAADIGSEASAETPKAAAPQV-PQEEKPTETGSASAPVPAQPIAPTASDPDIP-AGTEMVTMTVREALRD 150
Cdd:TIGR02927 207 PAEPAEEEAPAPSEAGSEPAPDPaARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSgDSGPYVTPLVRKLAKD 278
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-104 1.46e-12

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 69.65  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   1 MPIDILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLlaD 80
Cdd:PRK11854    1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVG-DKVETGALIMIF--E 75

                          90       100
                  ....*....|....*....|....
gi 2127527159  81 GESAADIGSEASAETPKAAAPQVP 104
Cdd:PRK11854   76 SADGAADAAPAQAEEKKEAAPAAA 99
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 150-447 2.30e-12

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 68.98  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 150 DAMAEEMRRDEDVfvMGEEVAEYQGAykitqGL--LQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTfNFAMQ 227
Cdd:PRK12571  327 EELTKEAAEDSDI--VAITAAMPLGT-----GLdkLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQR 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 228 AIDQIInsaaktlyMSGGQMGAPIVF-------RGPNGAAarvaaqHSQDY-AAWYSHVPGLKVVMPYTAADAKGLLKAA 299
Cdd:PRK12571  399 GYDQLL--------HDVALQNLPVRFvldraglVGADGAT------HAGAFdLAFLTNLPNMTVMAPRDEAELRHMLRTA 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 300 I---RDPNPVIFLENEilyGHHFEVPKLDDfVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRT 376
Cdd:PRK12571  465 AahdDGPIAVRFPRGE---GVGVEIPAEGT-ILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRF 540

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127527159 377 IRPMDlPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLA 447
Cdd:PRK12571  541 VKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYA 610
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 132-413 3.12e-12

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 68.49  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 132 DIPAGTEMVTMTVR---EALRDAMAEEMRRDEDVfvmgeeVAeyqgaykITQGLLQEFG--------PRRVVDTPITEHG 200
Cdd:PRK12315  265 DLETGQSKVPASGEsysSVTLDYLLKKIKEGKPV------VA-------INAAIPGVFGlkefrkkyPDQYVDVGIAEQE 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 201 FAGVGVGAAMAGLRPIVeFMTFNFAMQAIDQI-----INSAAKTLYMSGGQMGApivfrgpngaaARVAAQHSQDYAaWY 275
Cdd:PRK12315  332 SVAFASGIAANGARPVI-FVNSTFLQRAYDQLshdlaINNNPAVMIVFGGSISG-----------NDVTHLGIFDIP-MI 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 276 SHVPGLKVVMPYTAADAKGLLKAAIRDPN-PVIFL--ENEILYGHhfevPKLDDFVLPigKARIHKTGKDATVVSFGIGM 352
Cdd:PRK12315  399 SNIPNLVYLAPTTKEELIAMLEWALTQHEhPVAIRvpEHGVESGP----TVDTDYSTL--KYEVTKAGEKVAILALGDFY 472

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127527159 353 TYAVKAVEELSKE-GIDVELIDLRTIRPMDLPTvIESVKKTGRLV-TVEEGYPQSSVGTEIAT 413
Cdd:PRK12315  473 ELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVvTLEDGILDGGFGEKIAR 534
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-222 4.45e-12

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: 67.98  E-value: 4.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  15 EEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTEnVKVNTKIAVLLADGESAADIGSEASAE 94
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  95 tPKAAAPQVPQEEKPTETGSASAPVPAQPIAPTASDPDIPAGTEMVTMTVREalrdamaeemrrdedvfvMGEEVAEYQG 174
Cdd:TIGR01348 207 -PAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLARE------------------FGVDLSAVKG 267

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2127527159 175 AYKitQGLLQEFGPRRVVDTPI--TEHGFAGVGVGAAMAGLRPIVEFMTF 222
Cdd:TIGR01348 268 TGI--KGRILREDVQRFVKEPSvrAQAAAASAAGGAPGALPWPNVDFSKF 315
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-121 8.95e-11

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 63.87  E-value: 8.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   4 DILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGTEnVKVNTKIAVLLADGES 83
Cdd:PRK11854  208 DVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAA 284

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2127527159  84 AADIGSEASAETPKAAAPQV-PQEEKPTETGSASAPVPA 121
Cdd:PRK11854  285 PAAAPAKQEAAAPAPAAAKAeAPAAAPAAKAEGKSEFAE 323
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-155 2.22e-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: 56.42  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  15 EEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLlvpagteNVKVNTKIAVlladGESAADIGSEASAe 94
Cdd:TIGR01348  12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEI-------KVKVGDTLPV----GGVIATLEVGAGA- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159  95 tpkaaapQVPQEEKPTETGSASAPVPA----QPIAPTASD---------PDIPAGTEMVTMTVREALRDAMAEE 155
Cdd:TIGR01348  80 -------QAQAEAKKEAAPAPTAGAPApaaqAQAAPAAGQssgvqevtvPDIGDIEKVTVIEVLVKVGDTVSAD 146
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-101 2.44e-08

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 56.16  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159   4 DILMPALSPTmeEGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVLLADGES 83
Cdd:PRK11854  107 DVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVG-DKVSTGSLIMVFEVAGEA 183

                          90
                  ....*....|....*...
gi 2127527159  84 AADIGSEASAETPKAAAP 101
Cdd:PRK11854  184 PAAAPAAAEAAAPAAAPA 201
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 143-401 1.98e-07

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 53.57  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 143 TVREALRDAMAEEMRRDEDVFVMgeEVAEYQGAYKITqglLQEFGPRRVVDTPITEHGFAGVGVGAAMAGLRPIVeFMTF 222
Cdd:PLN02225  382 TYSDCFVEALVMEAEKDRDIVVV--HAGMEMDASLIT---FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPS 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 223 NFAMQAIDQIIN------SAAKTLYMSGGQMGAPivfrGPngaaarvaAQHSQDYAAWYSHVPGLKVVMPytaADAKGLL 296
Cdd:PLN02225  456 AFLQRAYDQVVHdvdrqrKAVRFVITSAGLVGSD----GP--------VQCGAFDIAFMSSLPNMIAMAP---ADEDELV 520

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 297 K----AAIRDPNPVIF-LENEILYGHHFEVPKldDFVLPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVEL 371
Cdd:PLN02225  521 NmvatAAYVTDRPVCFrFPRGSIVNMNYLVPT--GLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTV 598

                         250       260       270
                  ....*....|....*....|....*....|
gi 2127527159 372 IDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02225  599 ADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 188-401 7.87e-07

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 51.64  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 188 PRRVVDTPITEHGFAGVGVGAAMAGLRPIVEFMTfNFAMQAIDQIINSA------AKTLYMSGGQMGAPivfrGPNGAAA 261
Cdd:PLN02234  398 PTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVdlqklpVRFAIDRAGLMGAD----GPTHCGA 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 262 RvaaqhsqdYAAWYSHVPGLKVVMPYTAADAKGLL-KAAIRDPNPVIFLENEilyGHHFEV---PKLDDFVLPIGKARIH 337
Cdd:PLN02234  473 F--------DVTFMACLPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYHR---GNGIGVslpPGNKGVPLQIGRGRIL 541

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127527159 338 KTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02234  542 RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 17-77 1.34e-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: 45.48  E-value: 1.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127527159  17 GTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNTKIAVL 77
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEG-DQVEAGQLLVVI 67
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
342-429 5.81e-04

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 42.06  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 342 DATVVSFGIGMTY--AVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGT---EIATRVM 416
Cdd:PRK09622  267 DAEVAIVALGTTYesAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKNLKALAILDRSSPAGAMGAlfnEVTSAVY 346

                          90
                  ....*....|...
gi 2127527159 417 QqaFDYLDAPILT 429
Cdd:PRK09622  347 Q--TQGTKHPVVS 357
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 329-401 2.04e-03

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 40.65  E-value: 2.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127527159 329 LPIGKARIHKTGKDATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEG 401
Cdd:PLN02582  532 IEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 105-198 2.21e-03

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 39.03  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 105 QEEKPTETGSASAPVPAQPIAPTASDPdIPAGT--EMVTMTV------REALrdaMAEEMRRDEDVFVMGEEVAEYQGAY 176
Cdd:pfam14572  37 KEAESDEVDGRQSPPPYRSRTVSRSLG-LPEIIpkEKPPMTVvgdvggRIAI---IVDDMIDDVDSFVAAAELLKERGAY 112

                          90       100
                  ....*....|....*....|....*.
gi 2127527159 177 KI----TQGLLQEFGPRRVVDTPITE 198
Cdd:pfam14572 113 KIyvmaTHGLLSSDAPRLLEASPIDE 138
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 19-118 2.61e-03

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 40.09  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159  19 LSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAGtENVKVNT---KIAVLLADGESAADIGSEASAET 95
Cdd:PLN02528   15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG-DIVKVGEtllKIMVEDSQHLRSDSLLLPTDSSN 93

                          90       100
                  ....*....|....*....|...
gi 2127527159  96 PKAAApqVPQEEKPTETGSASAP 118
Cdd:PLN02528   94 IVSLA--ESDERGSNLSGVLSTP 114
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 9-64 7.16e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.67  E-value: 7.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2127527159   9 ALSPTMEeGTLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGVIGKLLVPAG 64
Cdd:PRK09282  524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 17-65 9.57e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 38.52  E-value: 9.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2127527159   17 GTLSKWLKKEGDKVTSGDVIAEIETDKatME--VEAVDEGVIGKLLVPAGT 65
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGD 1133
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
 342-432 9.62e-03

Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.


Pssm-ID: 407280 [Multi-domain]  Cd Length: 102  Bit Score: 35.70  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127527159 342 DATVVSFGIGMTYAVKAVEELSKEGIDVELIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVG---TEIATRVmqq 418
Cdd:pfam17147   2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAGVKKVVVLDRNISFGSPGqlgTEVKAAL--- 78

                          90
                  ....*....|....
gi 2127527159 419 aFDYLDAPILTIAG 432
Cdd:pfam17147  79 -YDSDPPVVNFIAG 91
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH