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Conserved domains on  [gi|1434617175|ref|WP_114356183|]
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MULTISPECIES: pyruvate dehydrogenase complex E1 component subunit beta [Rhodopseudomonas]

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
 1-469 0e+00

pyruvate dehydrogenase subunit beta; Provisional


:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIATILGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  81 GESAADADKASDPAVQNKVSQSAPPSAEPEAAQAKSaaapaQHAPEAPTVSAAADPDIPAGTEMVTVTIREALRDAMAEE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPA-----PAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 161 MRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINS 240
Cdd:PRK11892  156 MRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 241 AAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLEHEMLY 320
Cdd:PRK11892  236 AAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 321 GQSFEVPKLDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRA 400
Cdd:PRK11892  316 GQSFDVPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRL 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434617175 401 VTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAAKAVCYR 469
Cdd:PRK11892  396 VTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-469 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIATILGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  81 GESAADADKASDPAVQNKVSQSAPPSAEPEAAQAKSaaapaQHAPEAPTVSAAADPDIPAGTEMVTVTIREALRDAMAEE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPA-----PAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 161 MRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINS 240
Cdd:PRK11892  156 MRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 241 AAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLEHEMLY 320
Cdd:PRK11892  236 AAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 321 GQSFEVPKLDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRA 400
Cdd:PRK11892  316 GQSFDVPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRL 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434617175 401 VTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAAKAVCYR 469
Cdd:PRK11892  396 VTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 144-469 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: 570.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 144 MVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVE 223
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 304 AIRDPNPVIFLEHEMLYGQSFEVPKlDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLR 383
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 384 PLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAA 463
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*.
gi 1434617175 464 KAVCYR 469
Cdd:COG0022   320 RELLAY 325
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 151-317 6.85e-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: 6.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 151 EALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFA 230
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 231 MQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNP 310
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1434617175 311 VIFLEHE 317
Cdd:cd07036   161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 146-322 3.50e-54

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: 178.90  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 146 TVTIREALRDAMAEEMRRDPDVFVMGEEVGeyQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAG-LKPIVEF 224
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 225 MTFNFAMqaidqiINSAAKTLYMSGGQLGC-SIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:pfam02779  80 TFSDFLN------RADDAIRHGAALGKLPVpFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153

                         170       180
                  ....*....|....*....|.
gi 1434617175 304 AIR--DPNPVIFLEHEMLYGQ 322
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLRP 174
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-140 7.75e-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: 148.79  E-value: 7.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   5 VLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIATILGDGESA 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175  85 ADADK----ASDPAVQNKVSQSAPPSAE-PEAAQAKSAAAPAQHAPEAPTVSAAADPDIPA 140
Cdd:TIGR01349  82 ADAFKnyklESSASPAPKPSEIAPTAPPsAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFA 142
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 197-321 2.24e-31

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: 117.20  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  197 IDTPITEHGFAGVGVGAAMAGLKPIVEFMtFNFAMQAIDQIinsaaktlyMSGGQLG-CSIVFR-GPNGAASRVAA-QHS 273
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGnVPVVFRhDGGGGVGEDGPtHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1434617175  274 QDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNP-VIFLEHEMLYG 321
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
 
Name Accession Description Interval E-value
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-469 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 970.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIATILGD 80
Cdd:PRK11892    1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  81 GESAADADKASDPAVQNKVSQSAPPSAEPEAAQAKSaaapaQHAPEAPTVSAAADPDIPAGTEMVTVTIREALRDAMAEE 160
Cdd:PRK11892   81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPA-----PAAPAAPAAEVAADPDIPAGTEMVTMTVREALRDAMAEE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 161 MRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINS 240
Cdd:PRK11892  156 MRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 241 AAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLEHEMLY 320
Cdd:PRK11892  236 AAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENEILY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 321 GQSFEVPKLDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRA 400
Cdd:PRK11892  316 GQSFDVPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRL 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434617175 401 VTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAAKAVCYR 469
Cdd:PRK11892  396 VTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVKAVCYR 464
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 144-469 0e+00

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 614.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 144 MVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVE 223
Cdd:PRK09212    1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:PRK09212   81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 304 AIRDPNPVIFLEHEMLYGQSFEVPKlDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLR 383
Cdd:PRK09212  161 AIRDPNPVIFLENEILYGHSHEVPE-EEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 384 PLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAA 463
Cdd:PRK09212  240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAV 319


                  ....*.
gi 1434617175 464 KAVCYR 469
Cdd:PRK09212  320 KKVCYR 325
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 144-469 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: 570.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 144 MVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVE 223
Cdd:COG0022     1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:COG0022    81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 304 AIRDPNPVIFLEHEMLYGQSFEVPKlDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLR 383
Cdd:COG0022   161 AIRDDDPVIFLEHKRLYRLKGEVPE-EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 384 PLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAA 463
Cdd:COG0022   240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAV 319


                  ....*.
gi 1434617175 464 KAVCYR 469
Cdd:COG0022   320 RELLAY 325
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 124-467 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 556.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 124 APEAPTVSAAADPDIPAGTEMVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITE 203
Cdd:PTZ00182   12 RLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 204 HGFAGVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQI 283
Cdd:PTZ00182   92 QGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 284 PGLKVVAPYSAADAKGLLKAAIRDPNPVIFLEHEMLYGQSFEVPKLDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKA 363
Cdd:PTZ00182  172 PGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 364 ADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMP 443
Cdd:PTZ00182  252 AEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFP 331

                         330       340
                  ....*....|....*....|....
gi 1434617175 444 YAANLEKLALPSVAEVVEAAKAVC 467
Cdd:PTZ00182  332 YAKNLEPAYLPDKEKVVEAAKRVL 355
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 128-469 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 542.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 128 PTVSAAADPDIPAGTEMvtvTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFA 207
Cdd:PLN02683   11 PAAAAAARGYASAAKEM---TVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 208 GVGVGAAMAGLKPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLK 287
Cdd:PLN02683   88 GIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 288 VVAPYSAADAKGLLKAAIRDPNPVIFLEHEMLYGQSFEVPK--LD-DYVIPIGKARIVREGSDVTLISWSHGMTYTLKAA 364
Cdd:PLN02683  168 VLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAevLDsSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 365 DELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPY 444
Cdd:PLN02683  248 EILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPY 327

                         330       340
                  ....*....|....*....|....*
gi 1434617175 445 AANLEKLALPSVAEVVEAAKAVCYR 469
Cdd:PLN02683  328 AANLERLALPQVEDIVRAAKRACYR 352
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 144-467 2.17e-121

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 357.51  E-value: 2.17e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 144 MVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVE 223
Cdd:CHL00144    1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFNFAMQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:CHL00144   81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 304 AIRDPNPVIFLEHEMLYGQSFEVPKlDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLR 383
Cdd:CHL00144  161 AIRSNNPVIFFEHVLLYNLKEEIPD-NEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 384 PLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAFDYLDAPVTRVSGKDVPMPYAANLEKLALPSVAEVVEAA 463
Cdd:CHL00144  240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319


                  ....
gi 1434617175 464 KAVC 467
Cdd:CHL00144  320 EQII 323
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 151-317 6.85e-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: 6.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 151 EALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFA 230
Cdd:cd07036     1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 231 MQAIDQIINSAAKTLYMSGGQLGCSIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNP 310
Cdd:cd07036    81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                  ....*..
gi 1434617175 311 VIFLEHE 317
Cdd:cd07036   161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 146-322 3.50e-54

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: 178.90  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 146 TVTIREALRDAMAEEMRRDPDVFVMGEEVGeyQGAYKVTQGLLQEFGDRRVIDTPITEHGFAGVGVGAAMAG-LKPIVEF 224
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 225 MTFNFAMqaidqiINSAAKTLYMSGGQLGC-SIVFRGPNGAASRVAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKA 303
Cdd:pfam02779  80 TFSDFLN------RADDAIRHGAALGKLPVpFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153

                         170       180
                  ....*....|....*....|.
gi 1434617175 304 AIR--DPNPVIFLEHEMLYGQ 322
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLRP 174
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 337-459 2.92e-51

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: 169.70  E-value: 2.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 337 GKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAEL 416
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1434617175 417 SARIMEHAFDYLDAPVTRVSGKDVPMPYAA-NLEKLALPSVAEV 459
Cdd:pfam02780  81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
144-466 3.17e-43

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


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 154.47  E-value: 3.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 144 MVTVTIREALRDAMAEEMRRDPDVFVMGEEVGEYQGaykvTQGLLQEFGDRrVIDTPITEHGFAGVGVGAAMAGLKPIVe 223
Cdd:COG3958     1 MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTK----LDKFAKAFPDR-FFNVGIAEQNMVGVAAGLALAGKIPFV- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 fMTF-NFA-MQAIDQIINSAAktlYMsggQLGCSIVF------RGPNGAAsrvaaQHS-QDYsAWYSQIPGLKVVAPYSA 294
Cdd:COG3958    75 -STFaPFLtGRAYEQIRNDIA---YP---NLNVKIVGshaglsYGEDGAT-----HQAlEDI-ALMRALPNMTVIVPADA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 295 ADAKGLLKAAI-----------RDPNPVIFLEhemlygqsfevpkldDYVIPIGKARIVREGSDVTLISwsHG-MTYT-L 361
Cdd:COG3958   142 VETEAAVRAAAehdgpvylrlgRGAVPVVYDE---------------DYEFEIGKARVLREGKDVTIIA--TGiMVAEaL 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 362 KAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHafdyLDAPVTRVSGKDVP 441
Cdd:COG3958   205 EAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEVLAEN----YPVPLRRIGVPDRF 280

                         330       340
                  ....*....|....*....|....*...
gi 1434617175 442 MPYAAN---LEKLALpSVAEVVEAAKAV 466
Cdd:COG3958   281 GESGSPeelLEKYGL-DAEGIVAAAKEL 307
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-140 7.75e-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: 148.79  E-value: 7.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   5 VLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIATILGDGESA 84
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175  85 ADADK----ASDPAVQNKVSQSAPPSAE-PEAAQAKSAAAPAQHAPEAPTVSAAADPDIPA 140
Cdd:TIGR01349  82 ADAFKnyklESSASPAPKPSEIAPTAPPsAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFA 142
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-134 2.25e-35

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 135.69  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTnDVAVNTPIATILGD 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGD-VVPVGSVIAVIEEE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1434617175  81 GESAADADKASDPAVQnkVSQSAPPSAEPEAAQAKSAAAPAQHAPEAPTVSAAA 134
Cdd:PRK11856   80 GEAEAAAAAEAAPEAP--APEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAV 131
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 197-321 2.24e-31

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: 117.20  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  197 IDTPITEHGFAGVGVGAAMAGLKPIVEFMtFNFAMQAIDQIinsaaktlyMSGGQLG-CSIVFR-GPNGAASRVAA-QHS 273
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQI---------RSAGASGnVPVVFRhDGGGGVGEDGPtHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1434617175  274 QDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPNP-VIFLEHEMLYG 321
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 3-77 2.78e-29

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: 109.42  E-value: 2.78e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434617175   3 IQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTnDVAVNTPIATI 77
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGD-TVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-77 3.12e-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: 109.39  E-value: 3.12e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTnDVAVNTPIATI 77
Cdd:COG0508     1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVI 76
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 155-434 7.47e-26

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: 110.87  E-value: 7.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 155 DAMAEEMRRDPDVFV----MGEEVGeyqgaykvtqglLQEFGDR---RVIDTPITE-HG--FAGvgvGAAMAGLKPIVE- 223
Cdd:COG1154   325 DTLVELAEKDPRIVAitaaMPEGTG------------LDKFAERfpdRFFDVGIAEqHAvtFAA---GLATEGLKPVVAi 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFnfaMQ-AIDQII------NsaaktlymsggqLGcsIVF---R----GPNGAAsrvaaqH--SQDYSaWYSQIPGLK 287
Cdd:COG1154   390 YSTF---LQrAYDQVIhdvalqN------------LP--VTFaidRaglvGADGPT------HhgVFDLS-YLRCIPNMV 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 288 VVAPYSAADAKGLLKAAIRDPNPVIFLehemlY--GQSFEVPkLDDYV--IPIGKARIVREGSDVTLISWSHGMTYTLKA 363
Cdd:COG1154   446 IMAPKDENELRHMLYTALAYDGPTAIR-----YprGNGPGVE-LPAELepLPIGKGEVLREGKDVAILAFGTMVAEALEA 519

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175 364 ADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAfdyLDAPVTR 434
Cdd:COG1154   520 AERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFLADAG---LDVPVLR 587
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 7-136 9.29e-25

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 107.25  E-value: 9.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   7 MPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNDVAVNTPIA-TILGDGESAA 85
Cdd:PLN02744  117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAiTVEEEEDIGK 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1434617175  86 DAD-KASDPAvqnkvsQSAPPSAEPEAAQAKSAAAPAQHAPEAPTVSAAADP 136
Cdd:PLN02744  197 FKDyKPSSSA------APAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAP 242
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 155-434 1.60e-22

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 100.54  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 155 DAMAEEMRRDPDVFV----MGEEVGeyqgaykvtqglLQEFGDR---RVIDTPITE-HG--FAGvgvGAAMAGLKPIVE- 223
Cdd:PRK05444  287 ETLCELAEKDPKIVAitaaMPEGTG------------LVKFSKRfpdRYFDVGIAEqHAvtFAA---GLATEGLKPVVAi 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 224 FMTFnfaMQ-AIDQIINSAAktlymsggQLGCSIVF---R----GPNGAAsrvaaqH--SQDYSawY-SQIPGLKVVAPY 292
Cdd:PRK05444  352 YSTF---LQrAYDQVIHDVA--------LQNLPVTFaidRaglvGADGPT------HqgAFDLS--YlRCIPNMVIMAPS 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 293 SAADAKGLLK---------AAIRDPNpviflehemlyGQSFEVPKLDDYVIPIGKARIVREGSDVTLISWSHGMTYTLKA 363
Cdd:PRK05444  413 DENELRQMLYtalayddgpIAIRYPR-----------GNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKA 481

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175 364 ADELAkdgiSAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAELSARIMEHAfdyLDAPVTR 434
Cdd:PRK05444  482 AERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHG---LDVPVLN 545
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 151-313 2.65e-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: 84.42  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 151 EALRDAMAEEMRRDPDVFVMGEEVGEYQGAYKvtqgLLQEFGDRrVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFnFA 230
Cdd:cd07033     1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK----FAKKFPDR-FIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 231 MQAIDQIINSAAK-----TLYMSGGqlGCSIvfrGPNGaasrvAAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAI 305
Cdd:cd07033    75 QRAYDQIRHDVALqnlpvKFVGTHA--GISV---GEDG-----PTHQGIEDIALLRAIPNMTVLRPADANETAAALEAAL 144


                  ....*...
gi 1434617175 306 RDPNPVIF 313
Cdd:cd07033   145 EYDGPVYI 152
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 5-93 7.40e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 85.00  E-value: 7.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   5 VLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTnDVAVNTPIATILGDGESA 84
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEVSD 83


                  ....*....
gi 1434617175  85 ADADKASDP 93
Cdd:PRK14875   84 AEIDAFIAP 92
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 155-307 3.08e-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: 78.54  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 155 DAMAEEMRRDPDVFVMGEEVGEYQGAYkvtqGLLQEfGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTFNFAMQAI 234
Cdd:cd06586     1 AAFAEVLTAWGVRHVFGYPGDEISSLL----DALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434617175 235 DQIINSAAKTLYMsggqlgcsIVFRGPNGAASRV-AAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLLKAAIRD 307
Cdd:cd06586    76 NGLADAAAEHLPV--------VFLIGARGISAQAkQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA 141
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-110 3.27e-17

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 83.35  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATIlGD 80
Cdd:PRK05704    1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDT-VTVGQVLGRI-DE 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1434617175  81 GESAADADKASDPAVQNKVSQSAPPSAEPE 110
Cdd:PRK05704   79 GAAAGAAAAAAAAAAAAAAAPAQAQAAAAA 108
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 4-77 1.69e-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: 73.79  E-value: 1.69e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434617175   4 QVLMPALSPTMEKGnLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATI 77
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 3-143 2.51e-16

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: 80.55  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   3 IQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATILGDGE 82
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEEGND 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434617175  83 SAADADKASDPAVQNKVSQSAPPSAEPEAAQAksaaapaqHAPEAPTVSA---AADPDIPAGTE 143
Cdd:TIGR01347  80 ATAAPPAKSGEEKEETPAASAAAAPTAAANRP--------SLSPAARRLAkehGIDLSAVPGTG 135
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 8-163 4.12e-16

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 80.11  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   8 PALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATILGDGESAADA 87
Cdd:PTZ00144   50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-VEVGAPLSEIDTGGAPPAAA 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434617175  88 DKASDPAVQNKVSQSAPPSAEPEaaQAKSAAAPAQHAPEAPTVSAAADPdiPAGTEMVTVTIREALRDAMAeEMRR 163
Cdd:PTZ00144  129 PAAAAAAKAEKTTPEKPKAAAPT--PEPPAASKPTPPAAAKPPEPAPAA--KPPPTPVARADPRETRVPMS-RMRQ 199
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 4-65 1.65e-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: 70.93  E-value: 1.65e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434617175   4 QVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGT 65
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGT 62
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 155-417 3.91e-15

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 77.84  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 155 DAMAEEMRRDPDVFVM------GEEVGEYQGAYKvtqgllqefgdRRVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTfN 228
Cdd:PRK12571  327 EELTKEAAEDSDIVAItaamplGTGLDKLQKRFP-----------NRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-T 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 229 FAMQAIDQIINSAAKTlymsggQLGCSIV-----FRGPNGAAsrvaaqHSQDYS-AWYSQIPGLKVVAPYSAADAKGLLK 302
Cdd:PRK12571  395 FLQRGYDQLLHDVALQ------NLPVRFVldragLVGADGAT------HAGAFDlAFLTNLPNMTVMAPRDEAELRHMLR 462

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 303 AAIRDPNPVIFLEHEMLYGQSFEVPKLDDyVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTL 382
Cdd:PRK12571  463 TAAAHDDGPIAVRFPRGEGVGVEIPAEGT-ILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFV 541

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1434617175 383 RPLDtETIIASVKKTGRAVTVEEGWQQNGIGAELS 417
Cdd:PRK12571  542 KPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVL 575
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-138 5.65e-15

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 77.17  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEkGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATILGD 80
Cdd:PRK11855    1 MAIEFKVPDIGEVVE-VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGLLAVIEAA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434617175  81 GESAADADKASDPAvqnkvsqSAPPSAEPEAAQAKsaaapaqhAPEAPTVSAAAD------PDI 138
Cdd:PRK11855   79 GAAAAAAAPAAAAA-------PAAAAAAAPAPAAA--------APAAAAAAAGGGvvevkvPDI 127
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 3-150 7.32e-15

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 76.79  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   3 IQVLMPALSPTMEkGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATIlgdgE 82
Cdd:PRK11855  120 VEVKVPDIGEITE-VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVI----E 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434617175  83 SAADADKASDPAVQNKVSQSAPPSAEPEAAqaksaaapaqhAPEAPTVSAAADPDIPAGTEMVTVTIR 150
Cdd:PRK11855  194 VAAAAPAAAAAPAAAAPAAAAAAAPAPAPA-----------AAAAPAAAAPAAAAAPGKAPHASPAVR 250
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 4-136 7.31e-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: 67.34  E-value: 7.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   4 QVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEgTNDVAVNTPIATIlGDGES 83
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAII-GDANA 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434617175  84 AADADKASDPAVQNKVSQSAPPSAEPEAAQAKSAAAPAQHAPEAPTVSAAADP 136
Cdd:TIGR02927 206 APAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAP 258
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 1-146 3.40e-11

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


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 65.42  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEgTNDVAVNTPIAtILGD 80
Cdd:TIGR02927   1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLA-IIGE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434617175  81 GESAADADKASDPAvqnkvSQSAPPSAEPEAAQAKSAAAPAQHAPEAPTVSAAADPDIPAGTEMVT 146
Cdd:TIGR02927  79 PGEAGSEPAPAAPE-----PEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKMPELGESVT 139
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-108 1.39e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 63.48  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   1 MPIQVLMPALSPTmeKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIAtILGD 80
Cdd:PRK11854    1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVG-DKVETGALIM-IFES 76

                          90       100
                  ....*....|....*....|....*...
gi 1434617175  81 GESAADADKASDPAVQNKVSQSAPPSAE 108
Cdd:PRK11854   77 ADGAADAAPAQAEEKKEAAPAAAPAAAA 104
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-170 3.73e-10

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 61.69  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   3 IQVLMPALSPTMEKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIAtILGDGE 82
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGTKVA-IISKSE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  83 SAADADKASDPAVQNKVSQSAPPS---AEPEAAQAKSAAAPAQHAPEAPTVSAAADPDIPAGTEMVTVTIREaLRDAMAE 159
Cdd:PLN02226  170 DAASQVTPSQKIPETTDPKPSPPAedkQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPPKERERRVPMTR-LRKRVAT 248

                         170
                  ....*....|.
gi 1434617175 160 EMRRDPDVFVM 170
Cdd:PLN02226  249 RLKDSQNTFAL 259
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 189-417 4.77e-10

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 61.56  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 189 QEFGDRRViDTPITEHGFAGVGVGAAMAGLKPIVeFMTFNFAMQAIDQI-----INSAAKTLYMSGGQLGcsivfrgpng 263
Cdd:PRK12315  316 KKYPDQYV-DVGIAEQESVAFASGIAANGARPVI-FVNSTFLQRAYDQLshdlaINNNPAVMIVFGGSIS---------- 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 264 aASRVAAQHSQDYsAWYSQIPGLKVVAPYSAADAKGLLKAAIRDPN-PVIFL--EHEMLYGQsfevPKLDDYVIPigKAR 340
Cdd:PRK12315  384 -GNDVTHLGIFDI-PMISNIPNLVYLAPTTKEELIAMLEWALTQHEhPVAIRvpEHGVESGP----TVDTDYSTL--KYE 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 341 IVREGSDVTLIS----WSHGMtytlKAADELAKD-GISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEGWQQNGIGAE 415
Cdd:PRK12315  456 VTKAGEKVAILAlgdfYELGE----KVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELVVTLEDGILDGGFGEK 531


                  ..
gi 1434617175 416 LS 417
Cdd:PRK12315  532 IA 533
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 195-406 5.26e-09

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 58.57  E-value: 5.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 195 RVIDTPITEHGFAGVGVGAAMAGLKPIVEFMTfNFAMQAIDQIINSA------AKTLYMSGGQLGCSivfrGPNgaasrv 268
Cdd:PLN02234  400 RCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVdlqklpVRFAIDRAGLMGAD----GPT------ 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 269 aaqHSQDYSAWY-SQIPGLKVVAPYSAADAKGLL-KAAIRDPNPVIFLEHEMlYGQSFEVPKLDDYV-IPIGKARIVREG 345
Cdd:PLN02234  469 ---HCGAFDVTFmACLPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYHRG-NGIGVSLPPGNKGVpLQIGRGRILRDG 544

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175 346 SDVTLISWSHGMTYTLKAADELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEG 406
Cdd:PLN02234  545 ERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 17-77 1.92e-08

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: 50.88  E-value: 1.92e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175  17 GNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATI 77
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 5-148 7.20e-08

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 55.01  E-value: 7.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   5 VLMPALSPTmeKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATIlgdgESA 84
Cdd:PRK11854  209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVG-DKVKTGSLIMRF----EVE 281

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434617175  85 ADADKASDPAVQNKVSQSAPPSAEPeaaqaksaaapaqhAPEAPTVSAAADPDIPAGTEMVTVT 148
Cdd:PRK11854  282 GAAPAAAPAKQEAAAPAPAAAKAEA--------------PAAAPAAKAEGKSEFAENDAYVHAT 331
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 138-406 8.06e-08

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 54.91  E-value: 8.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 138 IPAGTEMVTVTIREALrdamAEEMRRDPDVFVMGEEVGEYQGaykvtqglLQEFGDR---RVIDTPITEHGFAGVGVGAA 214
Cdd:PLN02582  351 VKAKTQSYTTYFAEAL----IAEAEVDKDVVAIHAAMGGGTG--------LNLFARRfptRCFDVGIAEQHAVTFAAGLA 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 215 MAGLKPIVEFMTFnFAMQAIDQIINSA------AKTLYMSGGQLGCSivfrGPNgaasrvaaqHSQDYSAWY-SQIPGLK 287
Cdd:PLN02582  419 CEGLKPFCAIYSS-FLQRGYDQVVHDVdlqklpVRFAMDRAGLVGAD----GPT---------HCGAFDVTYmACLPNMV 484

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 288 VVAPYSAADAKGLL-KAAIRDPNPVIFlEHEMLYGQSFEVPKLDDYV-IPIGKARIVREGSDVTLISWSHGMTYTLKAAD 365
Cdd:PLN02582  485 VMAPSDEAELFHMVaTAAAIDDRPSCF-RYPRGNGIGVQLPPNNKGIpIEVGKGRILLEGERVALLGYGTAVQSCLAAAS 563

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1434617175 366 ELAKDGISAEVIDLRTLRPLDTETIIASVKKTGRAVTVEEG 406
Cdd:PLN02582  564 LLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 148-406 9.16e-08

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 54.72  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 148 TIREALRDAMAEEMRRDPDVFVMgeEVGEYQGAYKVTqglLQEFGDRRVIDTPITEHGFAGVGVGAAMAGLKPIVeFMTF 227
Cdd:PLN02225  382 TYSDCFVEALVMEAEKDRDIVVV--HAGMEMDASLIT---FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPS 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 228 NFAMQAIDQIIN------SAAKTLYMSGGQLGCSivfrGPngaasrvaAQHSQDYSAWYSQIPGLKVVAPYSAADAKGLL 301
Cdd:PLN02225  456 AFLQRAYDQVVHdvdrqrKAVRFVITSAGLVGSD----GP--------VQCGAFDIAFMSSLPNMIAMAPADEDELVNMV 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175 302 -KAAIRDPNPVIF-LEHEMLYGQSFEVPKldDYVIPIGKARIVREGSDVTLISWSHGMTYTLKAADELAKDGISAEVIDL 379
Cdd:PLN02225  524 aTAAYVTDRPVCFrFPRGSIVNMNYLVPT--GLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADA 601

                         250       260
                  ....*....|....*....|....*..
gi 1434617175 380 RTLRPLDTETIIASVKKTGRAVTVEEG 406
Cdd:PLN02225  602 RFCKPLDIKLVRDLCQNHKFLITVEEG 628
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 4-110 3.92e-07

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 52.31  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175   4 QVLMPALSPTmeKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATIlGDGES 83
Cdd:PRK11854  107 DVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVG-DKVSTGSLIMVF-EVAGE 182

                          90       100
                  ....*....|....*....|....*..
gi 1434617175  84 AAdadkASDPAVQNKVSQSAPPSAEPE 110
Cdd:PRK11854  183 AP----AAAPAAAEAAAPAAAPAAAAG 205
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-160 7.58e-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: 48.33  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  15 EKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATILGDGESAADADKASDPA 94
Cdd:TIGR01348  12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVG-DTLPVGGVIATLEVGAGAQAQAEAKKEAA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434617175  95 VQNKVSQSAPPSAEPEaaqaksaaapaqhAPEAPTVSAAAD---PDIPAGTEMVTVTIREALRDAMAEE 160
Cdd:TIGR01348  91 PAPTAGAPAPAAQAQA-------------APAAGQSSGVQEvtvPDIGDIEKVTVIEVLVKVGDTVSAD 146
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 15-227 1.23e-05

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: 47.56  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  15 EKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATILGDGES--AADADKASD 92
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVG-DSVPTGDLILTLSVAGSTpaTAPAPASAQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434617175  93 PAVQNKVSQSAPPSAEPeaaqaksaaAPAQHAPEAPTVSAAADPD-IPAGTEMVTVTIREalrdamaeemrrdpdvfvMG 171
Cdd:TIGR01348 207 PAAQSPAATQPEPAAAP---------AAAKAQAPAPQQAGTQNPAkVDHAAPAVRRLARE------------------FG 259

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434617175 172 EEVGEYQGAYKvtQGLLQEFGDRRVIDTPI--TEHGFAGVGVGAAMAGLKPIVEFMTF 227
Cdd:TIGR01348 260 VDLSAVKGTGI--KGRILREDVQRFVKEPSvrAQAAAASAAGGAPGALPWPNVDFSKF 315
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
17-77 1.13e-04

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 44.54  E-value: 1.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1434617175  17 GNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATI 77
Cdd:PRK14040  533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG-DAVAVGDTLLTL 592
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 17-64 2.48e-04

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 39.39  E-value: 2.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1434617175  17 GNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEG 64
Cdd:PRK08225   10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEG 57
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 9-64 3.14e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 43.29  E-value: 3.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434617175   9 ALSPTMeKGNLSKWLKKEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEG 64
Cdd:PRK09282  524 AVTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 25-77 5.46e-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: 39.88  E-value: 5.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434617175  25 KEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGTNdVAVNTPIATI 77
Cdd:COG0511    84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQP-VEYGQPLFVI 135
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 25-77 2.45e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434617175  25 KEGDKVKSGDVIAEIETDKATMEVEAADEGTLGKILIPEGtNDVAVNTPIATI 77
Cdd:PLN02983  221 KVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDG-KPVSVDTPLFVI 272
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 17-65 3.88e-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: 40.06  E-value: 3.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1434617175   17 GNLSKWLKKEGDKVKSGDVIAEIETDKatME--VEAADEGTLGKILIPEGT 65
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMK--MEttITAPRDGTVKEVLVKEGD 1133
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 17-65 9.34e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 38.58  E-value: 9.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1434617175   17 GNLSKWLKKEGDKVKSGDVIAEIETDKatME--VEAADEGTLGKILIPEGT 65
Cdd:PRK12999  1085 GSVVTVLVKEGDEVKAGDPLAVIEAMK--MEttITAPVDGTVKRVLVKAGD 1133
 
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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