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Conserved domains on  [gi|1533361987|gb|RRY09803|]
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pyruvate dehydrogenase complex E1 component subunit beta [Brucella anthropi]

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
 1-463 0e+00

pyruvate dehydrogenase subunit beta; Provisional


:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLLGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVREALRDAMAEEMRRDP 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 161 NVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFAMQAIDQIVNSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 241 YMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFD 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 321 VPKLDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987 401 GFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAVKAVTY 463
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCY 463
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-463 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLLGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVREALRDAMAEEMRRDP 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 161 NVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFAMQAIDQIVNSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 241 YMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFD 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 321 VPKLDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987 401 GFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAVKAVTY 463
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCY 463
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: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 139 MVSTTVREALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 219 FMTFNFAMQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 299 AIRDPNPVIFLENEILYGHHFDVPKlDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 379 PMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 1533361987 459 KAVTY 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 5.23e-106

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: 311.72  E-value: 5.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 146 EALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 226 MQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1533361987 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 143-316 2.47e-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: 174.28  E-value: 2.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 143 TVREALRDAMAEEMRRDPNVFVMGEEVAeyQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAG-LRPIVEFMT 221
Cdd:pfam02779   4 ATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 222 FNFAMqaidqiVNSAAKTLYMSGGQMGAP-MVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAI 300
Cdd:pfam02779  82 SDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAI 155

                         170
                  ....*....|....*...
gi 1533361987 301 R--DPNPVIFLENEILYG 316
Cdd:pfam02779 156 RrdGRKPVVLRLPRQLLR 173
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 4-131 1.64e-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: 142.24  E-value: 1.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLLGDGES 83
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533361987  84 ASDI----------GSAPAAKAEAPSSEAKEEPKAEEKKADS------VPAAPKAPALEVASDP 131
Cdd:TIGR01349  81 VADAfknyklessaSPAPKPSEIAPTAPPSAPKPSPAPQKQSpepsspAPLSDKESGDRIFASP 144
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 192-316 1.82e-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: 120.28  E-value: 1.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  192 VDTPITEHGFAGVGVGAAFAGLRPIVEFMtFNFAMQAIDQIvnsaaktlyMSGGQMGA-PMVFRGPSGAAARV--AAQHS 268
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGNvPVVFRHDGGGGVGEdgPTHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1533361987  269 QCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNP-VIFLENEILYG 316
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-463 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLLGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVREALRDAMAEEMRRDP 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEEMRRDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 161 NVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFAMQAIDQIVNSAAKTL 240
Cdd:PRK11892  161 DVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAAKTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 241 YMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGHHFD 320
Cdd:PRK11892  241 YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILYGQSFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 321 VPKLDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEE 400
Cdd:PRK11892  321 VPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEE 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987 401 GFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAVKAVTY 463
Cdd:PRK11892  401 GWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCY 463
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 139-463 0e+00

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 583.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 139 MVSTTVREALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVE 218
Cdd:PRK09212    1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 219 FMTFNFAMQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKA 298
Cdd:PRK09212   81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 299 AIRDPNPVIFLENEILYGHHFDVPKlDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIR 378
Cdd:PRK09212  161 AIRDPNPVIFLENEILYGHSHEVPE-EEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 379 PMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAV 458
Cdd:PRK09212  240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAV 319


                  ....*
gi 1533361987 459 KAVTY 463
Cdd:PRK09212  320 KKVCY 324
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: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 139 MVSTTVREALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVE 218
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 219 FMTFNFAMQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKA 298
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 299 AIRDPNPVIFLENEILYGHHFDVPKlDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIR 378
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 379 PMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAV 458
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*
gi 1533361987 459 KAVTY 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: 525.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 133 IPAGTEMVSTTVREALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAG 212
Cdd:PTZ00182   26 TESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 213 LRPIVEFMTFNFAMQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADA 292
Cdd:PTZ00182  106 LRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 293 KGLLKAAIRDPNPVIFLENEILYGHHFDVPKLDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEII 372
Cdd:PTZ00182  186 KGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 373 DLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVA 452
Cdd:PTZ00182  266 DLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKE 345

                         330
                  ....*....|
gi 1533361987 453 EVVEAVKAVT 462
Cdd:PTZ00182  346 KVVEAAKRVL 355
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 135-463 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 517.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 135 AGTEMvstTVREALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLR 214
Cdd:PLN02683   23 AAKEM---TVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 215 PIVEFMTFNFAMQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKG 294
Cdd:PLN02683  100 PVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 295 LLKAAIRDPNPVIFLENEILYGHHFDVPK--LD-DFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEI 371
Cdd:PLN02683  180 LLKAAIRDPDPVVFLENELLYGESFPVSAevLDsSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEV 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 372 IDLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTV 451
Cdd:PLN02683  260 INLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQV 339

                         330
                  ....*....|..
gi 1533361987 452 AEVVEAVKAVTY 463
Cdd:PLN02683  340 EDIVRAAKRACY 351
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 146-312 5.23e-106

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: 311.72  E-value: 5.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 146 EALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFA 225
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 226 MQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1533361987 306 VIFLENE 312
Cdd:cd07036   161 VIFLEHK 167
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 146-459 2.20e-103

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 311.29  E-value: 2.20e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 146 EALRDAMAEEMRRDPNVFVMGEEVAEYQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFA 225
Cdd:CHL00144    8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 226 MQAIDQIVNSAAKTLYMSGGQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNP 305
Cdd:CHL00144   88 LLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 306 VIFLENEILYGHHFDVPKlDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTV 385
Cdd:CHL00144  168 VIFFEHVLLYNLKEEIPD-NEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTI 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533361987 386 VESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPTVAEVVEAVK 459
Cdd:CHL00144  247 SKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAVE 320
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 143-316 2.47e-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: 174.28  E-value: 2.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 143 TVREALRDAMAEEMRRDPNVFVMGEEVAeyQGAYKVTQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAG-LRPIVEFMT 221
Cdd:pfam02779   4 ATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 222 FNFAMqaidqiVNSAAKTLYMSGGQMGAP-MVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAI 300
Cdd:pfam02779  82 SDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAI 155

                         170
                  ....*....|....*...
gi 1533361987 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 ...
 332-454 5.50e-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: 155.83  E-value: 5.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 332 GKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEI 411
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1533361987 412 ATRVMQQAFDYLDAPILTIAGKDVPMPYAA-NLEKLALPTVAEV 454
Cdd:pfam02780  81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-129 1.86e-38

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 144.16  E-value: 1.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVLLGD 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVAS 129
Cdd:PRK11856   80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKAS 128
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 4-131 1.64e-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: 142.24  E-value: 1.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLLGDGES 83
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533361987  84 ASDI----------GSAPAAKAEAPSSEAKEEPKAEEKKADS------VPAAPKAPALEVASDP 131
Cdd:TIGR01349  81 VADAfknyklessaSPAPKPSEIAPTAPPSAPKPSPAPQKQSpepsspAPLSDKESGDRIFASP 144
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 192-316 1.82e-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: 120.28  E-value: 1.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  192 VDTPITEHGFAGVGVGAAFAGLRPIVEFMtFNFAMQAIDQIvnsaaktlyMSGGQMGA-PMVFRGPSGAAARV--AAQHS 268
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGNvPVVFRHDGGGGVGEdgPTHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1533361987  269 QCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNP-VIFLENEILYG 316
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-77 2.03e-30

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: 112.47  E-value: 2.03e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVL 77
Cdd:COG0508     1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 3-77 4.34e-30

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: 111.73  E-value: 4.34e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533361987   3 VEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVL 77
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 4-131 1.98e-26

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 111.87  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEGVKVNTPIAVLL---GD 80
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVeeeED 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPA-APKAPALEVASDP 131
Cdd:PLN02744  194 IGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSpEPKASKPSAPPSS 245
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 150-431 1.28e-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: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 150 DAMAEEMRRDPNVfvmgeeVAeyqgaykVT----QGL-LDEFGSK---RVVDTPITE-HG--FAGvgvGAAFAGLRPIVE 218
Cdd:COG1154   325 DTLVELAEKDPRI------VA-------ITaampEGTgLDKFAERfpdRFFDVGIAEqHAvtFAA---GLATEGLKPVVA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 219 -FMTFnfaMQ-AIDQIVNSAAktlymsggQMGAPMVF---R----GPSGAAarvaaqHSQCY-AAWYSHIPGLKVVMPYT 288
Cdd:COG1154   389 iYSTF---LQrAYDQVIHDVA--------LQNLPVTFaidRaglvGADGPT------HHGVFdLSYLRCIPNMVIMAPKD 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 289 AADAKGLLKAAIRDPNPVIfleneILY----GHHFDVPKLDDfVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQ 364
Cdd:COG1154   452 ENELRHMLYTALAYDGPTA-----IRYprgnGPGVELPAELE-PLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAA 525

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533361987 365 QGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:COG1154   526 EGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFLADAG---LDVPVLRLG 589
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 4-98 6.50e-20

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 91.16  E-value: 6.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVlLGDGES 83
Cdd:PRK14875    4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGET-LPVGALLAV-VADAEV 81

                          90
                  ....*....|....*
gi 1533361987  84 ASDIGSAPAAKAEAP 98
Cdd:PRK14875   82 SDAEIDAFIAPFARR 96
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 183-431 4.33e-19

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 89.76  E-value: 4.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 183 LDEFGSK---RVVDTPITE-HG--FAGvgvGAAFAGLRPIVE-FMTFnfaMQ-AIDQIVNSAAktlymsggQMGAPMVF- 253
Cdd:PRK05444  312 LVKFSKRfpdRYFDVGIAEqHAvtFAA---GLATEGLKPVVAiYSTF---LQrAYDQVIHDVA--------LQNLPVTFa 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 254 --R----GPSGAAarvaaqHSQCY-AAWYSHIPGLKVVMPYTAADAKGLLKAAIR-DPNPVIfleneILY--GHHFDVPK 323
Cdd:PRK05444  378 idRaglvGADGPT------HQGAFdLSYLRCIPNMVIMAPSDENELRQMLYTALAyDDGPIA-----IRYprGNGVGVEL 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 324 LDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAqqgiDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEGFP 403
Cdd:PRK05444  447 PELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAI 522

                         250       260
                  ....*....|....*....|....*...
gi 1533361987 404 QSSVGTEIATRVMQQAfdyLDAPILTIA 431
Cdd:PRK05444  523 MGGFGSAVLEFLADHG---LDVPVLNLG 547
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 146-308 1.91e-18

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: 82.10  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 146 EALRDAMAEEMRRDPNVFVMGEEVAEYqgaykvtqGLLDEFGSK---RVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTF 222
Cdd:cd07033     1 KAFGEALLELAKKDPRIVALSADLGGS--------TGLDKFAKKfpdRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 223 nFAMQAIDQIVNSAAktlymsggQMGAPMVFRGpSGAAARVAA----QHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKA 298
Cdd:cd07033    73 -FLQRAYDQIRHDVA--------LQNLPVKFVG-THAGISVGEdgptHQGIEDIALLRAIPNMTVLRPADANETAAALEA 142

                         170
                  ....*....|
gi 1533361987 299 AIRDPNPVIF 308
Cdd:cd07033   143 ALEYDGPVYI 152
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-137 2.17e-18

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 86.81  E-value: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVlLGD 80
Cdd:PRK05704    1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEG-DTVTVGQVLGR-IDE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSV--PAAPKApALEVASDPDIPAGT 137
Cdd:PRK05704   79 GAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAlsPAARKL-AAENGLDASAVKGT 136
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 3-161 3.04e-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: 83.24  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   3 VEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVLLGDGE 82
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEEGND 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533361987  83 SASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVREalrDAMAEEMRRDPN 161
Cdd:TIGR01347  80 ATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE---DIIKKTEAPASA 155
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 150-302 9.04e-17

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: 77.39  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 150 DAMAEEMRRDPNVFVMGEEVAEYQGAYkvtqGLLDEfGSKRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTFNFAMQAI 229
Cdd:cd06586     1 AAFAEVLTAWGVRHVFGYPGDEISSLL----DALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533361987 230 DQIVNSAAKtlymsggqmGAPMVFRG--PSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRD 302
Cdd:cd06586    76 NGLADAAAE---------HLPVVFLIgaRGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA 141
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 3-77 3.04e-16

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: 73.02  E-value: 3.04e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533361987   3 VEILMPALSPTMEEGkLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVL 77
Cdd:pfam00364   1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-133 5.70e-16

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 80.25  E-value: 5.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSpTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVLLGD 80
Cdd:PRK11855    1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVG-DTVSVGGLLAVIEAA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEekkadsvPAAPKAPALEVASD---PDI 133
Cdd:PRK11855   79 GAAAAAAAPAAAAAPAAAAAAAPAPAAAA-------PAAAAAAAGGGVVEvkvPDI 127
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 3-145 1.31e-15

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 79.10  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   3 VEILMPALSpTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVllgdge 82
Cdd:PRK11855  120 VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV------ 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987  83 sasdIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVR 145
Cdd:PRK11855  192 ----IEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVR 250
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 4-66 3.91e-15

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: 70.16  E-value: 3.91e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTE 66
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 5-158 4.35e-15

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 77.03  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   5 ILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVLLGDGESA 84
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEG-DTVEVGAPLSEIDTGGAPP 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533361987  85 SDIGSAPAAKAEA---PSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPdiPAGTEMVSTTVREALRDAMAeEMRR 158
Cdd:PTZ00144  126 AAAPAAAAAAKAEkttPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAA--KPPPTPVARADPRETRVPMS-RMRQ 199
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-155 5.19e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 71.19  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTmeEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVLlgd 80
Cdd:PRK11854    1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVG-DKVETGALIMIF--- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533361987  81 gESASDIGSAPAAKAEAPSseakeepkaeekkADSVPAAPKAPALEVASDPDIpAGTEMVSTTVREALRDAMAEE 155
Cdd:PRK11854   75 -ESADGAADAAPAQAEEKK-------------EAAPAAAPAAAAAKDVHVPDI-GSDEVEVTEILVKVGDTVEAE 134
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-165 3.59e-11

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 65.16  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   3 VEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVLLGDGE 82
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  83 SASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAA--PKAPA-----LEVASDPDIPAgTEMVSTTVREALRDAMAEE 155
Cdd:PLN02226  171 AASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAekPKAPSsppppKQSAKEPQLPP-KERERRVPMTRLRKRVATR 249

                         170
                  ....*....|
gi 1533361987 156 MRRDPNVFVM 165
Cdd:PLN02226  250 LKDSQNTFAL 259
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 1-141 4.16e-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: 65.03  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   1 MPVEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEgTEGVKVNTPIAVLLGD 80
Cdd:TIGR02927   1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533361987  81 GESASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSvPAAPKAPALEVASDPDIPAGTEMVS 141
Cdd:TIGR02927  80 GEAGSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPA-PAAPQAGGSGEATEVKMPELGESVT 139
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 189-447 8.27e-11

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 64.36  E-value: 8.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 189 KRVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTfNFAMQAIDQIVnsaaktlyMSGGQMGAPMVF-------RGPSGAAa 261
Cdd:PRK12571  361 NRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLL--------HDVALQNLPVRFvldraglVGADGAT- 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 262 rvaaqHSQCY-AAWYSHIPGLKVVMPYTAADAKGLLKAAI---RDPNPVIFLENEilyGHHFDVPKLDDfVLPIGKARIH 337
Cdd:PRK12571  431 -----HAGAFdLAFLTNLPNMTVMAPRDEAELRHMLRTAAahdDGPIAVRFPRGE---GVGVEIPAEGT-ILGIGKGRVP 501

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 338 KQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDiPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQ 417
Cdd:PRK12571  502 REGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHLAD 580

                         250       260       270
                  ....*....|....*....|....*....|
gi 1533361987 418 QAFDYLDAPILTIAGKDVPMPYAANLEKLA 447
Cdd:PRK12571  581 TGLLDGGLKLRTLGLPDRFIDHASREEMYA 610
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 4-135 1.39e-10

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: 63.49  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEgTEGVKVNTPIAVlLGDGES 83
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAI-IGDANA 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1533361987  84 ASDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPA 135
Cdd:TIGR02927 206 APAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAA 257
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-146 3.95e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 61.94  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   4 EILMPALSPTmeEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVLlgdges 83
Cdd:PRK11854  208 DVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRF------ 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987  84 aSDIGSAPAAKAEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPDIPAGTEMVSTTVRE 146
Cdd:PRK11854  279 -EVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLARE 340
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 131-413 1.68e-09

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 60.02  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 131 PDIPAGTEMVSTTVREALRDAMAEEMR------RDPNVFVMGEEVAEYqgaykvtqglldefgSKRVVDTPITEHGFAGV 204
Cdd:PRK12315  271 SKVPASGESYSSVTLDYLLKKIKEGKPvvainaAIPGVFGLKEFRKKY---------------PDQYVDVGIAEQESVAF 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 205 GVGAAFAGLRPIVeFMTFNFAMQAIDQI-----VNSAAKTLYMSGGQMGAPMVfrgpsgaaarvaaQHSQCYA-AWYSHI 278
Cdd:PRK12315  336 ASGIAANGARPVI-FVNSTFLQRAYDQLshdlaINNNPAVMIVFGGSISGNDV-------------THLGIFDiPMISNI 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 279 PGLKVVMPYTAADAKGLLKAAIRDPN-PVIFL--ENEILYGHhfdvPKLDDFVLPigKARIHKQGKDATIVSFGIGMTYA 355
Cdd:PRK12315  402 PNLVYLAPTTKEELIAMLEWALTQHEhPVAIRvpEHGVESGP----TVDTDYSTL--KYEVTKAGEKVAILALGDFYELG 475

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 356 VKAAEELAQQ-GIDVEIIDLRTIRPMDIPTvVESVKKTGRLV-TVEEGFPQSSVGTEIAT 413
Cdd:PRK12315  476 EKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVvTLEDGILDGGFGEKIAR 534
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 3-155 1.11e-08

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 57.32  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987   3 VEILMPALSPTmeEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVLlgdgE 82
Cdd:PRK11854  106 KDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VSTGSLIMVF----E 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987  83 SASDIGSAPAAKAEAPSseakeepkaeekkadSVPAAPKAPALEVASDPDIpAGTEMVSTTVREALRDAMAEE 155
Cdd:PRK11854  179 VAGEAPAAAPAAAEAAA---------------PAAAPAAAAGVKDVNVPDI-GGDEVEVTEVMVKVGDKVEAE 235
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 182-401 5.93e-08

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 55.10  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 182 LLDEFGSK---RVVDTPITEHGFAGVGVGAAFAGLRPIVEFMTfNFAMQAIDQIVNSA------AKTLYMSGGQMGAPmv 252
Cdd:PLN02234  389 MLNLFESRfptRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVdlqklpVRFAIDRAGLMGAD-- 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 253 frGPSGAAArvaaqhsqCYAAWYSHIPGLKVVMPYTAADAKGLL-KAAIRDPNPVIFLENEilyGHHFDV---PKLDDFV 328
Cdd:PLN02234  466 --GPTHCGA--------FDVTFMACLPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYHR---GNGIGVslpPGNKGVP 532

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987 329 LPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEG 401
Cdd:PLN02234  533 LQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 17-77 1.00e-07

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: 48.95  E-value: 1.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533361987  17 GKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVL 77
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEG-DQVEAGQLLVVI 67
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-222 5.20e-07

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: 52.18  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  15 EEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGTEgVKVNTPIAVLlgDGESASDIGSAPAAK 94
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTL--SVAGSTPATAPAPAS 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  95 AEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASDPD-IPAGTEMVSTTVREalrdamaeemrrdpnvfvMGEEVAEYQ 173
Cdd:TIGR01348 205 AQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAkVDHAAPAVRRLARE------------------FGVDLSAVK 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1533361987 174 GAYKvtQGLLDEFGSKRVVDTPITEHGFAGVGVGAAFAGLRPI--VEFMTF 222
Cdd:TIGR01348 267 GTGI--KGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWpnVDFSKF 315
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-155 1.70e-06

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: 50.26  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  15 EEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVLlgdgesasDIGSAPAAK 94
Cdd:TIGR01348  12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVG-DTLPVGGVIATL--------EVGAGAQAQ 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533361987  95 AEAPSSEAKEEPKAEEKKADSVPAAPKAPALEVASD---PDIPAGTEMVSTTVREALRDAMAEE 155
Cdd:TIGR01348  83 AEAKKEAAPAPTAGAPAPAAQAQAAPAAGQSSGVQEvtvPDIGDIEKVTVIEVLVKVGDTVSAD 146
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 190-401 4.21e-06

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 49.33  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 190 RVVDTPITEHGFAGVGVGAAFAGLRPIVeFMTFNFAMQAIDQIVN------SAAKTLYMSGGQMGAPmvfrGPSgaaarv 263
Cdd:PLN02225  424 RFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPSAFLQRAYDQVVHdvdrqrKAVRFVITSAGLVGSD----GPV------ 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 264 aaqhsQCYA---AWYSHIPGLKVVMPytaADAKGLLK----AAIRDPNPVIF-LENEILYGHHFDVPKldDFVLPIGKAR 335
Cdd:PLN02225  493 -----QCGAfdiAFMSSLPNMIAMAP---ADEDELVNmvatAAYVTDRPVCFrFPRGSIVNMNYLVPT--GLPIEIGRGR 562

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533361987 336 IHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEG 401
Cdd:PLN02225  563 VLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 9-64 4.08e-05

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 45.99  E-value: 4.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1533361987   9 ALSPTMEeGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEG 64
Cdd:PRK09282  524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 329-401 5.73e-05

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 45.66  E-value: 5.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533361987 329 LPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEG 401
Cdd:PLN02582  532 IEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 25-77 2.42e-04

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 41.03  E-value: 2.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533361987  25 KEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVL 77
Cdd:COG0511    84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENG-QPVEYGQPLFVI 135
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 25-77 3.54e-04

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 42.13  E-value: 3.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533361987  25 KEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTPIAVL 77
Cdd:PLN02983  221 KVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDG-KPVSVDTPLFVI 272
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
342-429 1.33e-03

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 40.91  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987 342 DATIVSFGIGMTY--AVKAAEELAQQGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGT---EIATRVM 416
Cdd:PRK09622  267 DAEVAIVALGTTYesAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKNLKALAILDRSSPAGAMGAlfnEVTSAVY 346

                          90
                  ....*....|...
gi 1533361987 417 QqaFDYLDAPILT 429
Cdd:PRK09622  347 Q--TQGTKHPVVS 357
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 17-65 2.05e-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: 40.83  E-value: 2.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1533361987   17 GKLSKWLKKEGDKVTSGDVIAEIETDKatME--VEAVDEGTIGKILVDEGT 65
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGD 1133
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 22-56 4.27e-03

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 36.36  E-value: 4.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1533361987  22 WLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTI 56
Cdd:cd06848    35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEV 69
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 16-118 4.75e-03

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 39.32  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533361987  16 EGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKILVDEGtEGVKVNTP---IAVLLGDGESASDIGSaPA 92
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG-DIVKVGETllkIMVEDSQHLRSDSLLL-PT 89

                          90       100
                  ....*....|....*....|....*.
gi 1533361987  93 AKAEAPSSEAKEEPKAEEKKADSVPA 118
Cdd:PLN02528   90 DSSNIVSLAESDERGSNLSGVLSTPA 115
 
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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