|
Name |
Accession |
Description |
Interval |
E-value |
| cit_ly_ligase |
TIGR00124 |
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. ... |
7-339 |
0e+00 |
|
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. The carboxyl end is homologous to a number of cytidyltransferases that also release pyrophosphate. [Energy metabolism, Fermentation, Protein fate, Protein modification and repair]
Pssm-ID: 129230 [Multi-domain] Cd Length: 332 Bit Score: 600.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 7 FTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAY 86
Cdd:TIGR00124 1 FRRVWLENKLKACGIKNFLHQNELSLDAPLEIFIAVYEDEEIIGCGGIAGNVIKCVAIDESLRGEGLALQLMTELENLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 87 ERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQ 166
Cdd:TIGR00124 81 ELGRFHLFIFTKPEYAALFEYCGFKTLAEAKDQGVLLENSATRLKRYCSTLPKPRTPGNKIGSIVMNANPFTNGHRYLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 167 QAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQ 246
Cdd:TIGR00124 161 QAARQCDWLHLFVVKEDASLFSYDERFALVKQGIQDLSNVTVHNGSAYIISRATFPAYFLKEQDVADDCYTEIDLKLFRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 247 YLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTiSAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVP 326
Cdd:TIGR00124 241 KIAPALGITHRFVGTEPLCPVTALYNQKMKYWLEEPN-DAPPIEVVEIQRKLAAGGPISASTVRELLAKGDWAAWAKLVP 319
|
330
....*....|...
gi 1609983865 327 AVTLHYLQNLLEH 339
Cdd:TIGR00124 320 ETTLHFLQNLLEE 332
|
|
| CitC |
COG3053 |
Citrate lyase synthetase CitC [Energy production and conversion]; |
14-344 |
0e+00 |
|
Citrate lyase synthetase CitC [Energy production and conversion];
Pssm-ID: 442287 [Multi-domain] Cd Length: 330 Bit Score: 567.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 14 ENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHL 93
Cdd:COG3053 1 NPKELKAVREFLEQNGLTLDEDIDYTVGIYDDGKLIATGSLAGNVLKCVAVDPDYQGEGLSLQLITELINLAYERGIFHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 94 FIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCD 173
Cdd:COG3053 81 FLYTKPENEKLFESLGFYPIASVDPDVVLLENGPPGIQDYLKKLRKLRQPGGKIGAIVMNANPFTLGHRYLVEQAASECD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 174 WLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALG 253
Cdd:COG3053 161 WLHVFVVSEDRSLFPFEDRLELVKQGTADLPNVTVHPGGDYIISRATFPSYFLKDKGVVDEAQTELDLRIFRKYIAPALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 254 VTHRFVGTEPFCRVTAQYNQDMRYWLETptisaPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:COG3053 241 ITHRFVGTEPFCPVTAIYNQAMKRWLPP-----AGIEVVEIPRKEKDGEAISASRVRKLLAEGDLEAIRKLVPETTYAYL 315
|
330
....*....|.
gi 1609983865 334 QNLLEHSRQDA 344
Cdd:COG3053 316 QSHEAKEIIAK 326
|
|
| Citrate_lyase_ligase |
cd02169 |
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
29-333 |
0e+00 |
|
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.
Pssm-ID: 173920 [Multi-domain] Cd Length: 297 Bit Score: 508.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 29 DLSVDTTVEVFITVTRdekLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQC 108
Cdd:cd02169 1 DLSLDYTVGIFDDAGE---LIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 109 GFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFP 188
Cdd:cd02169 78 GFKELANASDEAVLLENGKPGIEDYLKNLPKPDQPGKKIAAIVMNANPFTLGHRYLVEKAAAENDWVHLFVVSEDKSLFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 189 YEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVT 268
Cdd:cd02169 158 FADRFKLVKKGTKHLKNVTVHSGGDYIISSATFPSYFIKEQDVVIKAQTALDARIFRKYIAPALNITKRYVGEEPFSRVT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609983865 269 AQYNQDMRYWLetptiSAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:cd02169 238 AIYNQTMQEEL-----LSPAIEVIEIERKKYDGQPISASTVRQLLKEGNLEEIAKLVPETTYEFL 297
|
|
| Citrate_ly_lig |
pfam08218 |
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ... |
147-333 |
9.00e-121 |
|
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of citrate lyase ligase EC:6.2.1.22.
Pssm-ID: 429870 Cd Length: 182 Bit Score: 345.86 E-value: 9.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFI 226
Cdd:pfam08218 1 IGAIVMNANPFTLGHRYLVEQAAAECDWLHLFVVSEDKSLFSYEDRFALVKKGTKHLKNVTVHSGGDYIISRATFPSYFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 227 KEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTisappIELVEIERLRYQEMPISA 306
Cdd:pfam08218 81 KEQAVVDESHAEIDLTIFREYIAPALGITHRYVGEEPFCPVTNIYNQQMKQWLPKPG-----IEVVEIPRKEYNGEPISA 155
|
170 180
....*....|....*....|....*..
gi 1609983865 307 SRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:pfam08218 156 SRVRKLLAEGNLEAIANLVPATTLNYL 182
|
|
| Citrate_ly_lig |
smart00764 |
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
147-333 |
3.11e-115 |
|
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.
Pssm-ID: 129003 Cd Length: 182 Bit Score: 331.52 E-value: 3.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFI 226
Cdd:smart00764 1 IAAIVMNANPFTLGHRYLVEQAAAECDWVHLFVVSEDASLFSFDERFALVKKGTKDLDNVTVHSGSDYIISRATFPSYFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 227 KEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMrywleTPTISAPPIELVEIERLRYQEMPISA 306
Cdd:smart00764 81 KEQDVVIKSQTTLDLRIFRKYIAPALGITHRYVGEEPFSPVTAIYNQTM-----KQTLLSPAIEVVEIERKKANGQPISA 155
|
170 180
....*....|....*....|....*..
gi 1609983865 307 SRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:smart00764 156 STVRKLLKEGNLEELAKLVPETTLNFL 182
|
|
| nadD |
PRK00071 |
nicotinate-nucleotide adenylyltransferase; |
142-334 |
5.17e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 234611 [Multi-domain] Cd Length: 203 Bit Score: 40.59 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 142 HPGNKIGciVM--NANPFTNGHRYLIQQAAAQcdwLHL----FLV------KEDSSRFPYEDRLDLVLKGTADIPRLTVh 209
Cdd:PRK00071 1 EMMKRIG--LFggTFDPPHYGHLAIAEEAAER---LGLdevwFLPnpgpphKPQKPLAPLEHRLAMLELAIADNPRFSV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 210 rgSEYIISRATFPcyfikeqsvinhcYTeID-LKIFRQ-------YL---APALGVTHR------------FVG-TEPFC 265
Cdd:PRK00071 75 --SDIELERPGPS-------------YT-IDtLRELRArypdvelVFiigADALAQLPRwkrweeildlvhFVVvPRPGY 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609983865 266 RVTAQYNQDMRYWLEtptiSAPPIELVEIerlryQEMPISASRVRQLLAKNDltAIAPLVPAVTLHYLQ 334
Cdd:PRK00071 139 PLEALALPALQQLLE----AAGAITLLDV-----PLLAISSTAIRERIKEGR--PIRYLLPEAVLDYIE 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cit_ly_ligase |
TIGR00124 |
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. ... |
7-339 |
0e+00 |
|
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. The carboxyl end is homologous to a number of cytidyltransferases that also release pyrophosphate. [Energy metabolism, Fermentation, Protein fate, Protein modification and repair]
Pssm-ID: 129230 [Multi-domain] Cd Length: 332 Bit Score: 600.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 7 FTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAY 86
Cdd:TIGR00124 1 FRRVWLENKLKACGIKNFLHQNELSLDAPLEIFIAVYEDEEIIGCGGIAGNVIKCVAIDESLRGEGLALQLMTELENLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 87 ERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQ 166
Cdd:TIGR00124 81 ELGRFHLFIFTKPEYAALFEYCGFKTLAEAKDQGVLLENSATRLKRYCSTLPKPRTPGNKIGSIVMNANPFTNGHRYLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 167 QAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQ 246
Cdd:TIGR00124 161 QAARQCDWLHLFVVKEDASLFSYDERFALVKQGIQDLSNVTVHNGSAYIISRATFPAYFLKEQDVADDCYTEIDLKLFRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 247 YLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTiSAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVP 326
Cdd:TIGR00124 241 KIAPALGITHRFVGTEPLCPVTALYNQKMKYWLEEPN-DAPPIEVVEIQRKLAAGGPISASTVRELLAKGDWAAWAKLVP 319
|
330
....*....|...
gi 1609983865 327 AVTLHYLQNLLEH 339
Cdd:TIGR00124 320 ETTLHFLQNLLEE 332
|
|
| CitC |
COG3053 |
Citrate lyase synthetase CitC [Energy production and conversion]; |
14-344 |
0e+00 |
|
Citrate lyase synthetase CitC [Energy production and conversion];
Pssm-ID: 442287 [Multi-domain] Cd Length: 330 Bit Score: 567.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 14 ENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHL 93
Cdd:COG3053 1 NPKELKAVREFLEQNGLTLDEDIDYTVGIYDDGKLIATGSLAGNVLKCVAVDPDYQGEGLSLQLITELINLAYERGIFHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 94 FIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCD 173
Cdd:COG3053 81 FLYTKPENEKLFESLGFYPIASVDPDVVLLENGPPGIQDYLKKLRKLRQPGGKIGAIVMNANPFTLGHRYLVEQAASECD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 174 WLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALG 253
Cdd:COG3053 161 WLHVFVVSEDRSLFPFEDRLELVKQGTADLPNVTVHPGGDYIISRATFPSYFLKDKGVVDEAQTELDLRIFRKYIAPALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 254 VTHRFVGTEPFCRVTAQYNQDMRYWLETptisaPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:COG3053 241 ITHRFVGTEPFCPVTAIYNQAMKRWLPP-----AGIEVVEIPRKEKDGEAISASRVRKLLAEGDLEAIRKLVPETTYAYL 315
|
330
....*....|.
gi 1609983865 334 QNLLEHSRQDA 344
Cdd:COG3053 316 QSHEAKEIIAK 326
|
|
| Citrate_lyase_ligase |
cd02169 |
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
29-333 |
0e+00 |
|
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.
Pssm-ID: 173920 [Multi-domain] Cd Length: 297 Bit Score: 508.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 29 DLSVDTTVEVFITVTRdekLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQC 108
Cdd:cd02169 1 DLSLDYTVGIFDDAGE---LIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 109 GFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFP 188
Cdd:cd02169 78 GFKELANASDEAVLLENGKPGIEDYLKNLPKPDQPGKKIAAIVMNANPFTLGHRYLVEKAAAENDWVHLFVVSEDKSLFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 189 YEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVT 268
Cdd:cd02169 158 FADRFKLVKKGTKHLKNVTVHSGGDYIISSATFPSYFIKEQDVVIKAQTALDARIFRKYIAPALNITKRYVGEEPFSRVT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609983865 269 AQYNQDMRYWLetptiSAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:cd02169 238 AIYNQTMQEEL-----LSPAIEVIEIERKKYDGQPISASTVRQLLKEGNLEEIAKLVPETTYEFL 297
|
|
| Citrate_ly_lig |
pfam08218 |
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ... |
147-333 |
9.00e-121 |
|
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of citrate lyase ligase EC:6.2.1.22.
Pssm-ID: 429870 Cd Length: 182 Bit Score: 345.86 E-value: 9.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFI 226
Cdd:pfam08218 1 IGAIVMNANPFTLGHRYLVEQAAAECDWLHLFVVSEDKSLFSYEDRFALVKKGTKHLKNVTVHSGGDYIISRATFPSYFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 227 KEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTisappIELVEIERLRYQEMPISA 306
Cdd:pfam08218 81 KEQAVVDESHAEIDLTIFREYIAPALGITHRYVGEEPFCPVTNIYNQQMKQWLPKPG-----IEVVEIPRKEYNGEPISA 155
|
170 180
....*....|....*....|....*..
gi 1609983865 307 SRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:pfam08218 156 SRVRKLLAEGNLEAIANLVPATTLNYL 182
|
|
| Citrate_ly_lig |
smart00764 |
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
147-333 |
3.11e-115 |
|
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.
Pssm-ID: 129003 Cd Length: 182 Bit Score: 331.52 E-value: 3.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFI 226
Cdd:smart00764 1 IAAIVMNANPFTLGHRYLVEQAAAECDWVHLFVVSEDASLFSFDERFALVKKGTKDLDNVTVHSGSDYIISRATFPSYFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 227 KEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMrywleTPTISAPPIELVEIERLRYQEMPISA 306
Cdd:smart00764 81 KEQDVVIKSQTTLDLRIFRKYIAPALGITHRYVGEEPFSPVTAIYNQTM-----KQTLLSPAIEVVEIERKKANGQPISA 155
|
170 180
....*....|....*....|....*..
gi 1609983865 307 SRVRQLLAKNDLTAIAPLVPAVTLHYL 333
Cdd:smart00764 156 STVRKLLKEGNLEELAKLVPETTLNFL 182
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
147-312 |
2.19e-12 |
|
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.
Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 64.00 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQC-DWLHlFLVKEDSSR-------FPYEDRLDLVLKGTADIPRLTVHRGSEYIISR 218
Cdd:cd02039 1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVI-IIIVSNPPKkkrnkdpFSLHERVEMLKEILKDRLKVVPVDFPEVKILL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 219 ATfpcyfikeqsvinhcyteidlkIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYwletptiSAPPIELVEIERLR 298
Cdd:cd02039 80 AV----------------------VFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKE-------LFLDIEIVEVPRVR 130
|
170
....*....|....
gi 1609983865 299 YQEmPISASRVRQL 312
Cdd:cd02039 131 DGK-KISSTLIREL 143
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
147-205 |
2.12e-11 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 58.86 E-value: 2.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609983865 147 IGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSR-------FPYEDRLDLVLKGTADIPR 205
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNplkgepvFSLEERLEMLKALKYVDEV 66
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
18-110 |
1.11e-08 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 53.07 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 18 MAEIAQFLHENDLSVDttVEVFITVTRDEKLIACGGIAGNI-----IKCVAISESVRGEGLALTLATELINLAYERHSTH 92
Cdd:COG1246 11 VPAILELIRPYALEEE--IGEFWVAEEDGEIVGCAALHPLDedlaeLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKR 88
|
90
....*....|....*...
gi 1609983865 93 LFIYTKTEYEALFRQCGF 110
Cdd:COG1246 89 LFLLTTSAAIHFYEKLGF 106
|
|
| nadD |
PRK00071 |
nicotinate-nucleotide adenylyltransferase; |
142-334 |
5.17e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 234611 [Multi-domain] Cd Length: 203 Bit Score: 40.59 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 142 HPGNKIGciVM--NANPFTNGHRYLIQQAAAQcdwLHL----FLV------KEDSSRFPYEDRLDLVLKGTADIPRLTVh 209
Cdd:PRK00071 1 EMMKRIG--LFggTFDPPHYGHLAIAEEAAER---LGLdevwFLPnpgpphKPQKPLAPLEHRLAMLELAIADNPRFSV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 210 rgSEYIISRATFPcyfikeqsvinhcYTeID-LKIFRQ-------YL---APALGVTHR------------FVG-TEPFC 265
Cdd:PRK00071 75 --SDIELERPGPS-------------YT-IDtLRELRArypdvelVFiigADALAQLPRwkrweeildlvhFVVvPRPGY 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609983865 266 RVTAQYNQDMRYWLEtptiSAPPIELVEIerlryQEMPISASRVRQLLAKNDltAIAPLVPAVTLHYLQ 334
Cdd:PRK00071 139 PLEALALPALQQLLE----AAGAITLLDV-----PLLAISSTAIRERIKEGR--PIRYLLPEAVLDYIE 196
|
|
| NadR |
COG1056 |
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ... |
156-334 |
6.21e-04 |
|
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 440676 [Multi-domain] Cd Length: 162 Bit Score: 39.79 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 156 PFTNGHRYLIQQAAAQCDWLHLFLVKEDSSR-----FPYEDRLDLVLKGT--ADIPRLTVHrgseyiisraTFPcyfike 228
Cdd:COG1056 13 PFHLGHLAVIKWALEEVDELIIGIGSAQESHtprnpFTAGERIEMIRAALkeEGLSRVYIV----------PIP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609983865 229 qsvinhcytEIDLkifrqylaPALGVTH--RFVGtePFCRVTA--QYNQDMRYWLETPTISAPPielveierlrYQEMPI 304
Cdd:COG1056 77 ---------DINN--------NSLWVSHvkSLVP--PFDVVYSnnPLVGRLFKEAGYEVLLPPL----------FEREEY 127
|
170 180 190
....*....|....*....|....*....|
gi 1609983865 305 SASRVRQLLAKNDltAIAPLVPAVTLHYLQ 334
Cdd:COG1056 128 SGTEIRRLMLEGE--DWESLVPPAVAEVIE 155
|
|
| PPAT |
cd02163 |
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ... |
156-209 |
1.43e-03 |
|
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.
Pssm-ID: 173914 [Multi-domain] Cd Length: 153 Bit Score: 38.60 E-value: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1609983865 156 PFTNGHRYLIQQAAAQCDWLHLfLVKEDSSR---FPYEDRLDLVLKGTADIPRLTVH 209
Cdd:cd02163 10 PITNGHLDIIERASKLFDEVIV-AVAVNPSKkplFSLEERVELIREATKHLPNVEVD 65
|
|
| coaD_prev_kdtB |
TIGR01510 |
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ... |
155-219 |
2.80e-03 |
|
pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 273663 [Multi-domain] Cd Length: 155 Bit Score: 38.02 E-value: 2.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609983865 155 NPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSR--FPYEDRLDLVLKGTADIPRLTVHRGSEYIISRA 219
Cdd:TIGR01510 9 DPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKplFSLEERVELIKDATKHLPNVRVDVFDGLLVDYA 75
|
|
| |
