|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
157-597 |
2.39e-161 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 470.14 E-value: 2.39e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 157 TARVGGVLARITEALEEYTHDATFLESPL-EAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGM 235
Cdd:COG0277 11 RAILAGRVLTDPADRAAYARDGNSLYRGRpDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGGVVLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 236 ERFRH-LEIDAANLMAVAGAGVVTGDLDAAAAEHGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVL 314
Cdd:COG0277 91 SRMNRiLEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 315 ADGSVLNLGGKLRKRSSGYRLMALFVGSEGTLGIVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALE 394
Cdd:COG0277 171 ADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 395 LINREALELIRDHLPAGFKSGHEAVLLIEQDGNDQEQVLLQLAEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHIL 471
Cdd:COG0277 251 LMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEVEAQLARLRAILeagGATDVRVAADGAERERLWKARKAALPAL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 472 MALRKNV-FSEDIAVPISKIPEMVHRFHELGLKNGVSLPTVAHAGDGNLHPAFLFD---DDQRHLISPLAAQIFRDAVEL 547
Cdd:COG0277 331 GRLDGGAkLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDpadPEEVERARAAAEEIFDLVAEL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1670799270 548 GGTISAEHGLGALKRDFAILEHGSEAIGWWRRLKDVFDPQGLLNPHKVFP 597
Cdd:COG0277 411 GGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
189-594 |
1.28e-123 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 371.80 E-value: 1.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 189 VLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGMERFRH-LEIDAANLMAVAGAGVVTGDLDAAAAE 267
Cdd:TIGR00387 2 VFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKiLEIDVVNLTAVVQPGVRNLELEQAVEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 268 HGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGKLRKRSSGYRLMALFVGSEGTLG 347
Cdd:TIGR00387 82 HNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 348 IVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIRDHLPAGFKSGHEAVLLIEQDGN 427
Cdd:TIGR00387 162 IVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 428 DqEQVLLQLAEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHILMALRKNVFSEDIAVPISKIPEMVHRFHELGLKN 504
Cdd:TIGR00387 242 H-EAVERDEEKIEQICrknGAVDVQIAQDEEERALLWAGRRNAFKAASKLSPLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 505 GVSLPTVAHAGDGNLHPAFLFDDDQRHLIS---PLAAQIFRDAVELGGTISAEHGLGALKRDFAILEHGSEAIGWWRRLK 581
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMErveEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 1670799270 582 DVFDPQGLLNPHK 594
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
169-597 |
4.01e-86 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 277.81 E-value: 4.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 169 EALEEYTHD--ATFLESPLeAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGMERF-RHLEIDA 245
Cdd:PRK11230 39 EELIPYECDglSAYRTRPL-LVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFnRILDINP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 246 ANLMAVAGAGVVTGDLDAAAAEHGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGK 325
Cdd:PRK11230 118 VGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 326 LRKrSSGYRLMALFVGSEGTLGIVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIR 405
Cdd:PRK11230 198 ALD-SPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRAAE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 406 DHLPAGFKSGHEAVLLIEQDG--NDQEQVLLQLAEMVELMGGVDNRVAQSGAERDGIWRARRQFGHILMALRKNVFSEDI 483
Cdd:PRK11230 277 DFIHAGYPVDAEAILLCELDGveSDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCMDG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 484 AVPISKIPEMVHRFHELGLKNGVSLPTVAHAGDGNLHPAFLFDDDQ---RHLISPLAAQIFRDAVELGGTISAEHGLGAL 560
Cdd:PRK11230 357 TIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEpgeLERAEALGGKILELCVEVGGSITGEHGVGRE 436
|
410 420 430
....*....|....*....|....*....|....*..
gi 1670799270 561 KRDFAILEHGSEAIGWWRRLKDVFDPQGLLNPHKVFP 597
Cdd:PRK11230 437 KINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIP 473
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
359-595 |
1.92e-61 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 204.47 E-value: 1.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 359 RPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIRDHL--PAGFKSGHEAVLLIEQDGNDQEQVLLQL 436
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLgfPKGLPRDAAALLLVEFEGDDEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 437 AEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHILMALRK---NVFSEDIAVPISKIPEMVHRFHELGLKNGVSLPT 510
Cdd:pfam02913 81 EAVEAILeagGAGDVVVATDEAEAERLWAARKYALPLRDALGGagpAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 511 VAHAGDGNLHPAFLFD---DDQRHLISPLAAQIFRDAVELGGTISAEHGLGALKRDFAILEHGSEAIGWWRRLKDVFDPQ 587
Cdd:pfam02913 161 FGHAGDGNLHLYILFDfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 1670799270 588 GLLNPHKV 595
Cdd:pfam02913 241 GILNPGKV 248
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
94-167 |
6.93e-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: 6.93e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 94 VDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
92-167 |
1.56e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 108.62 E-value: 1.56e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670799270 92 SVVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
97-170 |
1.65e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.77 E-value: 1.65e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 97 TLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEA 170
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
94-169 |
1.93e-19 |
|
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: 90.95 E-value: 1.93e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670799270 94 VDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITE 169
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
94-167 |
5.88e-18 |
|
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: 78.41 E-value: 5.88e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 94 VDFTLPRLSDALEEGIVtRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:pfam00364 1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
157-597 |
2.39e-161 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 470.14 E-value: 2.39e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 157 TARVGGVLARITEALEEYTHDATFLESPL-EAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGM 235
Cdd:COG0277 11 RAILAGRVLTDPADRAAYARDGNSLYRGRpDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGGVVLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 236 ERFRH-LEIDAANLMAVAGAGVVTGDLDAAAAEHGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVL 314
Cdd:COG0277 91 SRMNRiLEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 315 ADGSVLNLGGKLRKRSSGYRLMALFVGSEGTLGIVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALE 394
Cdd:COG0277 171 ADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 395 LINREALELIRDHLPAGFKSGHEAVLLIEQDGNDQEQVLLQLAEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHIL 471
Cdd:COG0277 251 LMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEVEAQLARLRAILeagGATDVRVAADGAERERLWKARKAALPAL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 472 MALRKNV-FSEDIAVPISKIPEMVHRFHELGLKNGVSLPTVAHAGDGNLHPAFLFD---DDQRHLISPLAAQIFRDAVEL 547
Cdd:COG0277 331 GRLDGGAkLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDpadPEEVERARAAAEEIFDLVAEL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1670799270 548 GGTISAEHGLGALKRDFAILEHGSEAIGWWRRLKDVFDPQGLLNPHKVFP 597
Cdd:COG0277 411 GGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
189-594 |
1.28e-123 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 371.80 E-value: 1.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 189 VLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGMERFRH-LEIDAANLMAVAGAGVVTGDLDAAAAE 267
Cdd:TIGR00387 2 VFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKiLEIDVVNLTAVVQPGVRNLELEQAVEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 268 HGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGKLRKRSSGYRLMALFVGSEGTLG 347
Cdd:TIGR00387 82 HNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 348 IVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIRDHLPAGFKSGHEAVLLIEQDGN 427
Cdd:TIGR00387 162 IVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 428 DqEQVLLQLAEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHILMALRKNVFSEDIAVPISKIPEMVHRFHELGLKN 504
Cdd:TIGR00387 242 H-EAVERDEEKIEQICrknGAVDVQIAQDEEERALLWAGRRNAFKAASKLSPLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 505 GVSLPTVAHAGDGNLHPAFLFDDDQRHLIS---PLAAQIFRDAVELGGTISAEHGLGALKRDFAILEHGSEAIGWWRRLK 581
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMErveEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 1670799270 582 DVFDPQGLLNPHK 594
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
169-597 |
4.01e-86 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 277.81 E-value: 4.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 169 EALEEYTHD--ATFLESPLeAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGMERF-RHLEIDA 245
Cdd:PRK11230 39 EELIPYECDglSAYRTRPL-LVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFnRILDINP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 246 ANLMAVAGAGVVTGDLDAAAAEHGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGK 325
Cdd:PRK11230 118 VGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 326 LRKrSSGYRLMALFVGSEGTLGIVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIR 405
Cdd:PRK11230 198 ALD-SPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRAAE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 406 DHLPAGFKSGHEAVLLIEQDG--NDQEQVLLQLAEMVELMGGVDNRVAQSGAERDGIWRARRQFGHILMALRKNVFSEDI 483
Cdd:PRK11230 277 DFIHAGYPVDAEAILLCELDGveSDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCMDG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 484 AVPISKIPEMVHRFHELGLKNGVSLPTVAHAGDGNLHPAFLFDDDQ---RHLISPLAAQIFRDAVELGGTISAEHGLGAL 560
Cdd:PRK11230 357 TIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEpgeLERAEALGGKILELCVEVGGSITGEHGVGRE 436
|
410 420 430
....*....|....*....|....*....|....*..
gi 1670799270 561 KRDFAILEHGSEAIGWWRRLKDVFDPQGLLNPHKVFP 597
Cdd:PRK11230 437 KINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIP 473
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
359-595 |
1.92e-61 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 204.47 E-value: 1.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 359 RPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIRDHL--PAGFKSGHEAVLLIEQDGNDQEQVLLQL 436
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLgfPKGLPRDAAALLLVEFEGDDEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 437 AEMVELM---GGVDNRVAQSGAERDGIWRARRQFGHILMALRK---NVFSEDIAVPISKIPEMVHRFHELGLKNGVSLPT 510
Cdd:pfam02913 81 EAVEAILeagGAGDVVVATDEAEAERLWAARKYALPLRDALGGagpAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 511 VAHAGDGNLHPAFLFD---DDQRHLISPLAAQIFRDAVELGGTISAEHGLGALKRDFAILEHGSEAIGWWRRLKDVFDPQ 587
Cdd:pfam02913 161 FGHAGDGNLHLYILFDfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 1670799270 588 GLLNPHKV 595
Cdd:pfam02913 241 GILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
186-597 |
2.73e-55 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 197.15 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 186 EAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRGIVLGM---ERFRHLEIDAANLMAVAGAGVVtgDLD 262
Cdd:PLN02805 135 DVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMslmKSVKALHVEDMDVVVEPGIGWL--ELN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 263 AAAAEHGLMYPPDPASLAisTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGKLRKRSSGYRLMALFVGS 342
Cdd:PLN02805 213 EYLEPYGLFFPLDPGPGA--TIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 343 EGTLGIVTEVIVKLIPRPRHQATAMVGYDTIEAAAEAVRTVLQSGHFPAALELINREALELIRdhlPAGFKSGHEA-VLL 421
Cdd:PLN02805 291 EGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQIRAIN---MANGKNLPEApTLM 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 422 IEQDGND---QEQVLLqLAEMVELMGGVDNRVAQSGAERDGIWRARRQ--FGHILMALRKNVFSEDIAVPISKIPEMVHR 496
Cdd:PLN02805 368 FEFIGTEayaREQTLI-VQKIASKHNGSDFVFAEEPEAKKELWKIRKEalWACFAMEPKYEAMITDVCVPLSHLAELISR 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 497 FHELGLKNGVSLPTVAHAGDGNLHPAFLFD---DDQRHLISPLAAQIFRDAVELGGTISAEHGLGALKRDFAILEHGSEA 573
Cdd:PLN02805 447 SKKELDASPLVCTVIAHAGDGNFHTIILFDpsqEDQRREAERLNHFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEA 526
|
410 420
....*....|....*....|....
gi 1670799270 574 IGWWRRLKDVFDPQGLLNPHKVFP 597
Cdd:PLN02805 527 LQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
186-323 |
2.68e-43 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 151.97 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 186 EAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVGGPVPLGrGIVLGMERF-RHLEIDAANLMAVAGAGVVTGDLDAA 264
Cdd:pfam01565 2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTG-GIVLDLSRLnGILEIDPEDGTATVEAGVTLGDLVRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670799270 265 AAEHGLMYPPDPASLAISTIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLG 323
Cdd:pfam01565 81 LAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
94-167 |
6.93e-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: 6.93e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 94 VDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
92-167 |
1.56e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 108.62 E-value: 1.56e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670799270 92 SVVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
93-280 |
1.10e-25 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 109.88 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 93 VVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEALE 172
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 173 EYTHDAtflESPLEAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLVggpVPLGRGIVlgmerfRHLEIDaanLMAVA 252
Cdd:PRK11856 82 AEAAAA---AEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKA---SPAVRKLA------RELGVD---LSTVK 146
|
170 180 190
....*....|....*....|....*....|..
gi 1670799270 253 GAG----VVTGDLDAAAAEHGLMYPPDPASLA 280
Cdd:PRK11856 147 GSGpggrITKEDVEAAAAAAAPAAAAAAAAAA 178
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
99-225 |
5.93e-24 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 104.53 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 99 PRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITE-----ALEE 173
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEgaaagAAAA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1670799270 174 YTHDATFLESPLEAAVLPGSTEEVA-----AVVKLCAETGTSLTTRgAGSGlVGGPV 225
Cdd:PRK05704 88 AAAAAAAAAAAPAQAQAAAAAEQSNdalspAARKLAAENGLDASAV-KGTG-KGGRV 142
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
97-170 |
1.65e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.77 E-value: 1.65e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 97 TLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEA 170
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
94-169 |
1.93e-19 |
|
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: 90.95 E-value: 1.93e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670799270 94 VDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITE 169
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE 76
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
194-598 |
3.10e-18 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 86.43 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 194 TEEVAAVVKLCAETGTSLTTRGAGS-GLVGGPV---PLG----RGIVlgmerfrhlEIDAANLMAVAGAGVVTGDLDAAA 265
Cdd:PRK11282 4 SAALLERVRQAAADGTPLRIRGGGSkDFYGRALageVLDtrahRGIV---------SYDPTELVITARAGTPLAELEAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 266 AEHGLMYPPDPASLAI-STIGGNVACNSGGPHCLKYGLTADYVVGLTVVLADGSVLNLGGKLRKRSSGY---RLMAlfvG 341
Cdd:PRK11282 75 AEAGQMLPFEPPHFGGgATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQVMKNVAGYdvsRLMA---G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 342 SEGTLGIVTEVIVKLIPRPRHQAT---AMvgydtieAAAEAVRTVLQSGHFPaalelinrealelirdhLPAGFKSGHEA 418
Cdd:PRK11282 152 SLGTLGVLLEVSLKVLPRPRAELTlrlEM-------DAAEALRKLNEWGGQP-----------------LPISASCWDGG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 419 VLlieqdgndqeqvllqlaemvelmggvdnRVAQSGAErDGIWRARRQFGHILMALRKNVFSEDIAvpiskipEMVHRFH 498
Cdd:PRK11282 208 TL----------------------------YLRLSGAE-GAVKAARERLGGEELDDAEAAFWQQLR-------EQTLPFF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 499 ELGLKN-GVSLPTVAHAGDgnLHPAFLFD--DDQRHLISPLAAQIFRD-AVELGGTISAEHGLGALKRDFAILEHGSEAI 574
Cdd:PRK11282 252 DDGRPLwRLSLPSTAPPLD--LPGEQLIDwgGAQRWLKSDADAAAIRAaAAAAGGHATLFRAGDRAGPVFHPLPAPLLRI 329
|
410 420
....*....|....*....|....
gi 1670799270 575 GwwRRLKDVFDPQGLLNPHKVFPE 598
Cdd:PRK11282 330 H--RRLKQAFDPAGIFNPGRLYAE 351
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
94-167 |
5.88e-18 |
|
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: 78.41 E-value: 5.88e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 94 VDFTLPRLSDALEEGIVtRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:pfam00364 1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
98-218 |
1.04e-17 |
|
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: 86.99 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 98 LPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEALEEYTHD 177
Cdd:TIGR02927 7 MPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPGEAGSEP 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1670799270 178 ATFLESPLEAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGS 218
Cdd:TIGR02927 87 APAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEAT 127
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
82-170 |
1.40e-17 |
|
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: 86.22 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGASYSVVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:TIGR02927 115 PAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVG 194
|
....*....
gi 1670799270 162 GVLARITEA 170
Cdd:TIGR02927 195 TVLAIIGDA 203
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
82-167 |
3.03e-15 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 78.71 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGASYSVVDFTLPRLSDAlEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:PRK11855 108 PAAAAAAAGGGVVEVKVPDIGEI-TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVG 186
|
....*.
gi 1670799270 162 GVLARI 167
Cdd:PRK11855 187 SLLVVI 192
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
98-167 |
1.62e-14 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 68.62 E-value: 1.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 98 LPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
94-212 |
4.49e-14 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 75.24 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 94 VDFTLPRLSDaLEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEALEE 173
Cdd:PRK11855 3 IEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAA 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 1670799270 174 YTHDATFLESPLEAAVLPGSTEEVAAVVKLCAETGTSLT 212
Cdd:PRK11855 82 AAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVV 120
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
94-200 |
7.21e-14 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 74.18 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 94 VDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEG-ETARVGGVLARITEALE 172
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEGE 82
|
90 100
....*....|....*....|....*...
gi 1670799270 173 EYThDATFLESPLEAAVLPGSTEEVAAV 200
Cdd:PRK11892 83 SAS-DAGAAPAAAAEAAAAAPAAAAAAA 109
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
82-196 |
2.85e-13 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 72.48 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGasySVVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:PLN02226 83 PFSSESG---DTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPG 159
|
90 100 110
....*....|....*....|....*....|....*
gi 1670799270 162 GVLARITEALEEYTHDATFLESPLEAAVLPGSTEE 196
Cdd:PLN02226 160 TKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAE 194
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
89-195 |
4.14e-13 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 71.64 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 89 ASYSVVDFTLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARIT 168
Cdd:PTZ00144 40 SYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
|
90 100
....*....|....*....|....*..
gi 1670799270 169 EALEEYTHDATFLESPLEAAVLPGSTE 195
Cdd:PTZ00144 120 TGGAPPAAAPAAAAAAKAEKTTPEKPK 146
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
98-196 |
6.28e-13 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 71.42 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 98 LPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEG-ETARVGGVLARITEALEEYTH 176
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEEDIGK 196
|
90 100
....*....|....*....|
gi 1670799270 177 DATFLESPLEAAVLPGSTEE 196
Cdd:PLN02744 197 FKDYKPSSSAAPAAPKAKPS 216
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
97-307 |
7.93e-13 |
|
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: 70.98 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 97 TLPRLSDALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEG-ETARVGGVLARITE------ 169
Cdd:TIGR01349 3 TMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEekedva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 170 -ALEEYTHDATFLESPLEAAVLPGSTEEV----AAVVKLCAETGTSLTTRGAGSGLVGGPVPLGRgivlgmerfRHLEID 244
Cdd:TIGR01349 83 dAFKNYKLESSASPAPKPSEIAPTAPPSApkpsPAPQKQSPEPSSPAPLSDKESGDRIFASPLAK---------KLAKEK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670799270 245 AANLMAVAGAG----VVTGDLDAAaaehglmyppDPASLAISTIGGNVACNSGGPHcLKYGLTADYV 307
Cdd:TIGR01349 154 GIDLSAVAGSGpngrIVKKDIESF----------VPQSPASANQQAAATTPATYPA-AAPVSTGSYE 209
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
108-167 |
4.23e-11 |
|
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: 58.58 E-value: 4.23e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 108 GIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
82-195 |
5.98e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 65.41 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGASYSVVDFTLPRLSDalEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:PRK11854 94 AAPAAAPAAAAAKDVHVPDIGS--DEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTG 171
|
90 100 110
....*....|....*....|....*....|....
gi 1670799270 162 GVLARITEALEEYTHDATFLESPLEAAVLPGSTE 195
Cdd:PRK11854 172 SLIMVFEVAGEAPAAAPAAAEAAAPAAAPAAAAG 205
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
82-170 |
1.94e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 63.87 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGASySVVDFTLPRLSDalEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:PRK11854 196 PAAAPAAAA-GVKDVNVPDIGG--DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTG 272
|
....*....
gi 1670799270 162 GVLARITEA 170
Cdd:PRK11854 273 SLIMRFEVE 281
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
107-201 |
5.24e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 62.33 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 107 EGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARITEalEEYTHDATFLESPLE 186
Cdd:PRK11854 14 EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFES--ADGAADAAPAQAEEK 91
|
90
....*....|....*
gi 1670799270 187 AAVLPGSTEEVAAVV 201
Cdd:PRK11854 92 KEAAPAAAPAAAAAK 106
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
169-322 |
8.11e-09 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440574 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 169 EALEEYThdaTF-LESPLEAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLV--GGPVplgRGIVLGMERFRHLEIDA 245
Cdd:COG0812 1 EPLAPHT---TFrIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLvrDDGF---DGLVIRLGRLKGIEVDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 246 ANLMaVAGAGVVTGDLDAAAAEHGLmyppdpaS----LA-I-STIGGNVACNSGGphclkYGL-TADYVVGLTVVLADGS 318
Cdd:COG0812 75 GVLV-TAGAGENWHDLVRFALEAGL-------SglefLAgIpGTVGGAPVMNAGA-----YGGeIKDVLESVEVLDRTGE 141
|
....
gi 1670799270 319 VLNL 322
Cdd:COG0812 142 VRTL 145
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
104-199 |
1.21e-08 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 57.96 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 104 ALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI-TEALEEYTHDATFLE 182
Cdd:TIGR01348 10 DNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLeVGAGAQAQAEAKKEA 89
|
90
....*....|....*..
gi 1670799270 183 SPLEAAVLPGSTEEVAA 199
Cdd:TIGR01348 90 APAPTAGAPAPAAQAQA 106
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
82-199 |
1.79e-08 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 57.19 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 82 PADPETGASYSVVDFTLPRLSDAlEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVG 161
Cdd:TIGR01348 105 QAAPAAGQSSGVQEVTVPDIGDI-EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTG 183
|
90 100 110
....*....|....*....|....*....|....*...
gi 1670799270 162 GVLArITEALEEYTHDATFLESPLEAAVLPGSTEEVAA 199
Cdd:TIGR01348 184 DLIL-TLSVAGSTPATAPAPASAQPAAQSPAATQPEPA 220
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
191-381 |
6.23e-08 |
|
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 55.29 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 191 PGSTEEVAAVVKLCAETGTSLTTRGAG---SGLVggpvpLGRGIVLGMERF-RHLEIDAANLMAVAGAGVVTGDLDAAAA 266
Cdd:TIGR01678 21 PTSVEEVREVLALAREQKKKVKVVGGGhspSDIA-----CTDGFLIHLDKMnKVLQFDKEKKQITVEAGIRLYQLHEQLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 267 EHGLMYPpDPASLAISTIGGNVACNSGGPHcLKYGLTADYVVGLTVVLADGSVLNLGGKLRKRSSGYRLMALfvgseGTL 346
Cdd:TIGR01678 96 EHGYSMS-NLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLECSEERNADVFQAARVSL-----GCL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670799270 347 GIVTEVIVKLIPRPRHQATAMV--------GYDTIEAAAEAVR 381
Cdd:TIGR01678 169 GIIVTVTIQVVPQFHLQETSFVstlkelldNWDSHWKSSEFFR 211
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
189-322 |
6.97e-07 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 51.27 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 189 VLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLV---GGPvplgRGIVLGMER-FRHLEIDAANLmaVAGAGVVTGDLDAA 264
Cdd:PRK13905 35 VEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLvrdGGI----RGVVIRLGKgLNEIEVEGNRI--TAGAGAPLIKLARF 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670799270 265 AAEHGLmyppdpASL----AI-STIGGNVACNSGGphclkYGL-TADYVVGLTVVLADGSVLNL 322
Cdd:PRK13905 109 AAEAGL------SGLefaaGIpGTVGGAVFMNAGA-----YGGeTADVLESVEVLDRDGEIKTL 161
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
116-167 |
8.71e-06 |
|
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: 45.66 E-value: 8.71e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1670799270 116 KPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
108-167 |
8.75e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 8.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 108 GIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
29-164 |
1.39e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 45.62 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 29 PTPTRSYWPTAPAASTPgstqrsrSRAVTTTPwwarfrprrssrsqrrsrrsgpadPETGASYSVVDFTLPrlsdaleeG 108
Cdd:PRK05641 53 PTPAPAPAPAVPSAPTP-------VAPAAPAP------------------------APASAGENVVTAPMP--------G 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670799270 109 IVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVL 164
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
191-361 |
1.86e-05 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 47.54 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 191 PGSTEEVAAVVKLCAETGTSLttRGAGSGLVGGPVPLGRGIVLGMERF-RHLEIDAANLMAVAGAGVVTGDLDAAAAEHG 269
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRI--RPVGSGLSPNGLAFSREGMVNLALMdKVLEVDKEKKRVTVQAGARVQQVVEALRPHG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 270 LMYPpDPASLAISTIGGNVacnSGGPHclkyGLTA------DYVVGLTVVL-ADGSVlnlggKLRKRSSG--YRLMALFV 340
Cdd:PLN02465 181 LTLQ-NYASIREQQIGGFI---QVGAH----GTGArippidEQVVSMKLVTpAKGTI-----ELSKEDDPelFRLARCGL 247
|
170 180
....*....|....*....|.
gi 1670799270 341 GSegtLGIVTEVIVKLIPRPR 361
Cdd:PLN02465 248 GG---LGVVAEVTLQCVPAHR 265
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
107-217 |
9.46e-05 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 45.10 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 107 EGIVT----RWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI-----------TEAL 171
Cdd:PLN02528 8 EGIAEcellRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKImvedsqhlrsdSLLL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1670799270 172 EEYTHDATFLESPLEAAVLPGSTEEVAAVVKLCAETGTSLTT-RGAG 217
Cdd:PLN02528 88 PTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDiLGTG 134
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
118-167 |
3.80e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 43.56 E-value: 3.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1670799270 118 GEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:PRK14042 544 GDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
108-167 |
4.02e-04 |
|
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: 43.53 E-value: 4.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 108 GIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
116-164 |
5.22e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.00 E-value: 5.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1670799270 116 KPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVL 164
Cdd:PRK14040 541 TEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
184-367 |
6.52e-04 |
|
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 42.54 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 184 PLEAAVLPGSTEEVAAVVKLCAETGTSL--TTRGAGS-GLVGGPVPLGRGIVLGMERFRH-LEIDAANLMAVAGAGVVTG 259
Cdd:TIGR01677 31 RAANVAYPKTEAELVSVVAAATAAGRKMkvVTRYSHSiPKLACPDGSDGALLISTKRLNHvVAVDATAMTVTVESGMSLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 260 DLDAAAAEHGLMYPPDPASLAIsTIGGNVACNSGGPHCL-KYGLTADYVVGLTVVLAdGSVLNLGGKLRKRSSG---YRL 335
Cdd:TIGR01677 111 ELIVEAEKAGLALPYAPYWWGL-TVGGMMGTGAHGSSLWgKGSAVHDYVVGIRLVVP-ASAAEGFAKVRILSEGdtpNEF 188
|
170 180 190
....*....|....*....|....*....|..
gi 1670799270 336 MALFVgSEGTLGIVTEVIVKLIPRPRHQATAM 367
Cdd:TIGR01677 189 NAAKV-SLGVLGVISQVTLALQPMFKRSVTYT 219
|
|
| murB |
PRK13906 |
UDP-N-acetylmuramate dehydrogenase; |
166-302 |
8.06e-04 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184386 [Multi-domain] Cd Length: 307 Bit Score: 41.73 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 166 RITEALEEYTHDATFLESplEAAVLPGSTEEVAAVVKLCAETGTSLTTRGAGSGLV---GGPvplgRGIVLGMERFRHLE 242
Cdd:PRK13906 20 KVDEPLKRYTYTKTGGNA--DFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIireGGI----RGIVISLLSLDHIE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670799270 243 IDAANLMAVAGAGVVtgDLDAAAAEHGLMyPPDPASLAISTIGGNVACNSGG-----PHCLKYGL 302
Cdd:PRK13906 94 VSDDAIIAGSGAAII--DVSRVARDYALT-GLEFACGIPGSIGGAVYMNAGAyggevKDCIDYAL 155
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
108-167 |
3.64e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.51 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670799270 108 GIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEAPADGILAEIVVGEGETARVGGVLARI 167
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
104-141 |
7.36e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 7.36e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1670799270 104 ALEEGIVTRWLKKPGEPVRQGEPLVEIETDKVNSELEA 141
Cdd:COG1566 50 AKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQ 87
|
|
| |
