|
Name |
Accession |
Description |
Interval |
E-value |
| CitC |
COG3053 |
Citrate lyase synthetase CitC [Energy production and conversion]; |
16-333 |
0e+00 |
|
Citrate lyase synthetase CitC [Energy production and conversion];
Pssm-ID: 442287 [Multi-domain] Cd Length: 330 Bit Score: 538.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 16 HPERLSQIRYLLADSGLGLDNDITLFVEAWSGPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHL 95
Cdd:COG3053 1 NPKELKAVREFLEQNGLTLDEDIDYTVGIYDDGKLIATGSLAGNVLKCVAVDPDYQGEGLSLQLITELINLAYERGIFHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 96 FLCTRPCNRERFARSGFWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCD 175
Cdd:COG3053 81 FLYTKPENEKLFESLGFYPIASVDPDVVLLENGPPGIQDYLKKLRKLRQPGGKIGAIVMNANPFTLGHRYLVEQAASECD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 176 ALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALG 255
Cdd:COG3053 161 WLHVFVVSEDRSLFPFEDRLELVKQGTADLPNVTVHPGGDYIISRATFPSYFLKDKGVVDEAQTELDLRIFRKYIAPALG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 771212307 256 ITHRFIGSEPFCDITRQYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHLETHY 333
Cdd:COG3053 241 ITHRFVGTEPFCPVTAIYNQAMKRWLPPAgIEVVEIPRKEKDGEAISASRVRKLLAEGDLEAIRKLVPETTYAYLQSHE 319
|
|
| Citrate_lyase_ligase |
cd02169 |
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
32-329 |
1.19e-148 |
|
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: 420.52 E-value: 1.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 32 LGLDNDITLFVEAwsgPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLFLCTRPCNRERFARSG 111
Cdd:cd02169 2 LSLDYTVGIFDDA---GELIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 112 FWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPF 191
Cdd:cd02169 79 FKELANASDEAVLLENGKPGIEDYLKNLPKPDQPGKKIAAIVMNANPFTLGHRYLVEKAAAENDWVHLFVVSEDKSLFSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 192 SARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITR 271
Cdd:cd02169 159 ADRFKLVKKGTKHLKNVTVHSGGDYIISSATFPSYFIKEQDVVIKAQTALDARIFRKYIAPALNITKRYVGEEPFSRVTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 771212307 272 QYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHL 329
Cdd:cd02169 239 IYNQTMQEELLSPaIEVIEIERKKYDGQPISASTVRQLLKEGNLEEIAKLVPETTYEFL 297
|
|
| cit_ly_ligase |
TIGR00124 |
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. ... |
19-330 |
6.75e-129 |
|
[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: 371.85 E-value: 6.75e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 19 RLSQIRYLLADSGLGLDNDITLFVEAWSGPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLFLC 98
Cdd:TIGR00124 11 KACGIKNFLHQNELSLDAPLEIFIAVYEDEEIIGCGGIAGNVIKCVAIDESLRGEGLALQLMTELENLAYELGRFHLFIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 99 TRPCNRERFARSGFWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCDALH 178
Cdd:TIGR00124 91 TKPEYAALFEYCGFKTLAEAKDQGVLLENSATRLKRYCSTLPKPRTPGNKIGSIVMNANPFTNGHRYLIEQAARQCDWLH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 179 LFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALGITH 258
Cdd:TIGR00124 171 LFVVKEDASLFSYDERFALVKQGIQDLSNVTVHNGSAYIISRATFPAYFLKEQDVADDCYTEIDLKLFRYKIAPALGITH 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 771212307 259 RFIGSEPFCDITRQYNQTLHDLL-----ASHIEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHLE 330
Cdd:TIGR00124 251 RFVGTEPLCPVTALYNQKMKYWLeepndAPPIEVVEIQRKLAAGGPISASTVRELLAKGDWAAWAKLVPETTLHFLQ 327
|
|
| Citrate_ly_lig |
smart00764 |
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
149-329 |
6.19e-102 |
|
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: 297.62 E-value: 6.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFL 228
Cdd:smart00764 1 IAAIVMNANPFTLGHRYLVEQAAAECDWVHLFVVSEDASLFSFDERFALVKKGTKDLDNVTVHSGSDYIISRATFPSYFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 229 KETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITRQYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRR 307
Cdd:smart00764 81 KEQDVVIKSQTTLDLRIFRKYIAPALGITHRYVGEEPFSPVTAIYNQTMKQTLLSPaIEVVEIERKKANGQPISASTVRK 160
|
170 180
....*....|....*....|..
gi 771212307 308 LLKTQQFSRIREIVPDSTFAHL 329
Cdd:smart00764 161 LLKEGNLEELAKLVPETTLNFL 182
|
|
| Citrate_ly_lig |
pfam08218 |
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ... |
149-329 |
1.96e-97 |
|
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: 286.15 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFL 228
Cdd:pfam08218 1 IGAIVMNANPFTLGHRYLVEQAAAECDWLHLFVVSEDKSLFSYEDRFALVKKGTKHLKNVTVHSGGDYIISRATFPSYFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 229 KETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITRQYNQTLHDLL-ASHIEVVEMPRIKATGNAISASEVRR 307
Cdd:pfam08218 81 KEQAVVDESHAEIDLTIFREYIAPALGITHRYVGEEPFCPVTNIYNQQMKQWLpKPGIEVVEIPRKEYNGEPISASRVRK 160
|
170 180
....*....|....*....|..
gi 771212307 308 LLKTQQFSRIREIVPDSTFAHL 329
Cdd:pfam08218 161 LLAEGNLEAIANLVPATTLNYL 182
|
|
| nadD |
PRK00071 |
nicotinate-nucleotide adenylyltransferase; |
155-335 |
1.06e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 234611 [Multi-domain] Cd Length: 203 Bit Score: 42.51 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 155 NANPFTLGHRHLVEQAAQR--CDALhLFVV------REDASFFPFSARLEMVRAGVAHLPNVVVH------EGSQYIIS- 219
Cdd:PRK00071 12 TFDPPHYGHLAIAEEAAERlgLDEV-WFLPnpgpphKPQKPLAPLEHRLAMLELAIADNPRFSVSdielerPGPSYTIDt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 220 ----RATFP-------------AYFLKetgkvqqaWSEIDVlIFRdfIAPALGIThRfigsePFCDITRQYNQTLHDLLA 282
Cdd:PRK00071 91 lrelRARYPdvelvfiigadalAQLPR--------WKRWEE-ILD--LVHFVVVP-R-----PGYPLEALALPALQQLLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 771212307 283 SH--IEVVEMPRIkatgnAISASEVRRLLKTQQFsrIREIVPDSTFAHLETH--YRA 335
Cdd:PRK00071 154 AAgaITLLDVPLL-----AISSTAIRERIKEGRP--IRYLLPEAVLDYIEKHglYRS 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CitC |
COG3053 |
Citrate lyase synthetase CitC [Energy production and conversion]; |
16-333 |
0e+00 |
|
Citrate lyase synthetase CitC [Energy production and conversion];
Pssm-ID: 442287 [Multi-domain] Cd Length: 330 Bit Score: 538.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 16 HPERLSQIRYLLADSGLGLDNDITLFVEAWSGPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHL 95
Cdd:COG3053 1 NPKELKAVREFLEQNGLTLDEDIDYTVGIYDDGKLIATGSLAGNVLKCVAVDPDYQGEGLSLQLITELINLAYERGIFHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 96 FLCTRPCNRERFARSGFWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCD 175
Cdd:COG3053 81 FLYTKPENEKLFESLGFYPIASVDPDVVLLENGPPGIQDYLKKLRKLRQPGGKIGAIVMNANPFTLGHRYLVEQAASECD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 176 ALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALG 255
Cdd:COG3053 161 WLHVFVVSEDRSLFPFEDRLELVKQGTADLPNVTVHPGGDYIISRATFPSYFLKDKGVVDEAQTELDLRIFRKYIAPALG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 771212307 256 ITHRFIGSEPFCDITRQYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHLETHY 333
Cdd:COG3053 241 ITHRFVGTEPFCPVTAIYNQAMKRWLPPAgIEVVEIPRKEKDGEAISASRVRKLLAEGDLEAIRKLVPETTYAYLQSHE 319
|
|
| Citrate_lyase_ligase |
cd02169 |
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
32-329 |
1.19e-148 |
|
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: 420.52 E-value: 1.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 32 LGLDNDITLFVEAwsgPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLFLCTRPCNRERFARSG 111
Cdd:cd02169 2 LSLDYTVGIFDDA---GELIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 112 FWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPF 191
Cdd:cd02169 79 FKELANASDEAVLLENGKPGIEDYLKNLPKPDQPGKKIAAIVMNANPFTLGHRYLVEKAAAENDWVHLFVVSEDKSLFSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 192 SARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITR 271
Cdd:cd02169 159 ADRFKLVKKGTKHLKNVTVHSGGDYIISSATFPSYFIKEQDVVIKAQTALDARIFRKYIAPALNITKRYVGEEPFSRVTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 771212307 272 QYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHL 329
Cdd:cd02169 239 IYNQTMQEELLSPaIEVIEIERKKYDGQPISASTVRQLLKEGNLEEIAKLVPETTYEFL 297
|
|
| cit_ly_ligase |
TIGR00124 |
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. ... |
19-330 |
6.75e-129 |
|
[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: 371.85 E-value: 6.75e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 19 RLSQIRYLLADSGLGLDNDITLFVEAWSGPQLVGCAGLAANVIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLFLC 98
Cdd:TIGR00124 11 KACGIKNFLHQNELSLDAPLEIFIAVYEDEEIIGCGGIAGNVIKCVAIDESLRGEGLALQLMTELENLAYELGRFHLFIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 99 TRPCNRERFARSGFWPIAQSGNNAVLMENTPQGIERYCRSLRAKRKCGENIGAIVMNANPFTLGHRHLVEQAAQRCDALH 178
Cdd:TIGR00124 91 TKPEYAALFEYCGFKTLAEAKDQGVLLENSATRLKRYCSTLPKPRTPGNKIGSIVMNANPFTNGHRYLIEQAARQCDWLH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 179 LFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFLKETGKVQQAWSEIDVLIFRDFIAPALGITH 258
Cdd:TIGR00124 171 LFVVKEDASLFSYDERFALVKQGIQDLSNVTVHNGSAYIISRATFPAYFLKEQDVADDCYTEIDLKLFRYKIAPALGITH 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 771212307 259 RFIGSEPFCDITRQYNQTLHDLL-----ASHIEVVEMPRIKATGNAISASEVRRLLKTQQFSRIREIVPDSTFAHLE 330
Cdd:TIGR00124 251 RFVGTEPLCPVTALYNQKMKYWLeepndAPPIEVVEIQRKLAAGGPISASTVRELLAKGDWAAWAKLVPETTLHFLQ 327
|
|
| Citrate_ly_lig |
smart00764 |
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
149-329 |
6.19e-102 |
|
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: 297.62 E-value: 6.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFL 228
Cdd:smart00764 1 IAAIVMNANPFTLGHRYLVEQAAAECDWVHLFVVSEDASLFSFDERFALVKKGTKDLDNVTVHSGSDYIISRATFPSYFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 229 KETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITRQYNQTLHDLLASH-IEVVEMPRIKATGNAISASEVRR 307
Cdd:smart00764 81 KEQDVVIKSQTTLDLRIFRKYIAPALGITHRYVGEEPFSPVTAIYNQTMKQTLLSPaIEVVEIERKKANGQPISASTVRK 160
|
170 180
....*....|....*....|..
gi 771212307 308 LLKTQQFSRIREIVPDSTFAHL 329
Cdd:smart00764 161 LLKEGNLEELAKLVPETTLNFL 182
|
|
| Citrate_ly_lig |
pfam08218 |
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ... |
149-329 |
1.96e-97 |
|
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: 286.15 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDASFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRATFPAYFL 228
Cdd:pfam08218 1 IGAIVMNANPFTLGHRYLVEQAAAECDWLHLFVVSEDKSLFSYEDRFALVKKGTKHLKNVTVHSGGDYIISRATFPSYFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 229 KETGKVQQAWSEIDVLIFRDFIAPALGITHRFIGSEPFCDITRQYNQTLHDLL-ASHIEVVEMPRIKATGNAISASEVRR 307
Cdd:pfam08218 81 KEQAVVDESHAEIDLTIFREYIAPALGITHRYVGEEPFCPVTNIYNQQMKQWLpKPGIEVVEIPRKEYNGEPISASRVRK 160
|
170 180
....*....|....*....|..
gi 771212307 308 LLKTQQFSRIREIVPDSTFAHL 329
Cdd:pfam08218 161 LLAEGNLEAIANLVPATTLNYL 182
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
149-308 |
9.88e-18 |
|
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: 78.64 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDA-------SFFPFSARLEMVRAGVAHLPNVVVHEGSQYIISRA 221
Cdd:cd02039 1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPpkkkrnkDPFSLHERVEMLKEILKDRLKVVPVDFPEVKILLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 222 TfpayflketgkvqqawseidvlIFRDFIAPALGITHRFIGSEPFCDITRQYNQTLHDLLaSHIEVVEMPRIKaTGNAIS 301
Cdd:cd02039 81 V----------------------VFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKELF-LDIEIVEVPRVR-DGKKIS 136
|
....*..
gi 771212307 302 ASEVRRL 308
Cdd:cd02039 137 STLIREL 143
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
149-207 |
1.30e-09 |
|
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: 53.85 E-value: 1.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 771212307 149 IGAIVMNANPFTLGHRHLVEQAAQRCDALHLFVVREDA-------SFFPFSARLEMVRAGVAHLPN 207
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFvnplkgePVFSLEERLEMLKALKYVDEV 66
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
22-118 |
3.17e-09 |
|
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: 54.61 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 22 QIRYLLADSGLgLDNDITLFVeAWSGPQLVGCAGLAAN-----VIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLF 96
Cdd:COG1246 13 AILELIRPYAL-EEEIGEFWV-AEEDGEIVGCAALHPLdedlaELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF 90
|
90 100
....*....|....*....|..
gi 771212307 97 LCTRPCNRERFARSGFWPIAQS 118
Cdd:COG1246 91 LLTTSAAIHFYEKLGFEEIDKE 112
|
|
| PPAT |
cd02163 |
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ... |
158-211 |
2.62e-06 |
|
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: 46.69 E-value: 2.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 771212307 158 PFTLGHRHLVEQAAQRCDALHLFVVREDA--SFFPFSARLEMVRAGVAHLPNVVVH 211
Cdd:cd02163 10 PITNGHLDIIERASKLFDEVIVAVAVNPSkkPLFSLEERVELIREATKHLPNVEVD 65
|
|
| nadD |
PRK00071 |
nicotinate-nucleotide adenylyltransferase; |
155-335 |
1.06e-04 |
|
nicotinate-nucleotide adenylyltransferase;
Pssm-ID: 234611 [Multi-domain] Cd Length: 203 Bit Score: 42.51 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 155 NANPFTLGHRHLVEQAAQR--CDALhLFVV------REDASFFPFSARLEMVRAGVAHLPNVVVH------EGSQYIIS- 219
Cdd:PRK00071 12 TFDPPHYGHLAIAEEAAERlgLDEV-WFLPnpgpphKPQKPLAPLEHRLAMLELAIADNPRFSVSdielerPGPSYTIDt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 220 ----RATFP-------------AYFLKetgkvqqaWSEIDVlIFRdfIAPALGIThRfigsePFCDITRQYNQTLHDLLA 282
Cdd:PRK00071 91 lrelRARYPdvelvfiigadalAQLPR--------WKRWEE-ILD--LVHFVVVP-R-----PGYPLEALALPALQQLLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 771212307 283 SH--IEVVEMPRIkatgnAISASEVRRLLKTQQFsrIREIVPDSTFAHLETH--YRA 335
Cdd:PRK00071 154 AAgaITLLDVPLL-----AISSTAIRERIKEGRP--IRYLLPEAVLDYIEKHglYRS 203
|
|
| NadR |
COG1056 |
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ... |
158-330 |
1.65e-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: 41.33 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 158 PFTLGHRHLVEQAAQRCDALHLFVVREDASFF---PFSA--RLEMVRAGVAHLPNVVVhegsqYIIsraTFP-AYFlket 231
Cdd:COG1056 13 PFHLGHLAVIKWALEEVDELIIGIGSAQESHTprnPFTAgeRIEMIRAALKEEGLSRV-----YIV---PIPdINN---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 232 gkvQQAWSEIDVLIFRDFiapalgitHRFIGSEPFcditrqynqTLHDLLASHIEVVEMPRIKATGnaISASEVRRLLKT 311
Cdd:COG1056 81 ---NSLWVSHVKSLVPPF--------DVVYSNNPL---------VGRLFKEAGYEVLLPPLFEREE--YSGTEIRRLMLE 138
|
170
....*....|....*....
gi 771212307 312 QQfsRIREIVPDSTFAHLE 330
Cdd:COG1056 139 GE--DWESLVPPAVAEVIE 155
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
35-119 |
1.29e-03 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 38.53 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771212307 35 DNDITLFVEAWSGPQLVGCAGLAANVIKC---------VAVNEQLRGENLSARLLAEVENAALECGHFHLFLCTRPCNRE 105
Cdd:COG3153 35 DPAAGLSLVAEDDGEIVGHVALSPVDIDGegpalllgpLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP 114
|
90
....*....|....
gi 771212307 106 RFARSGFWPIAQSG 119
Cdd:COG3153 115 FYERFGFRPAGELG 128
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
44-112 |
1.79e-03 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 37.50 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 771212307 44 AWSGPQLVGCAGLAAN-------VIKCVAVNEQLRGENLSARLLAEVENAALECGHFHLFLCTRPCN---RERFARSGF 112
Cdd:pfam00583 38 AEEDGELVGFASLSIIddeppvgEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNlaaIALYEKLGF 116
|
|
| coaD_prev_kdtB |
TIGR01510 |
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ... |
157-210 |
6.88e-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: 36.87 E-value: 6.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 771212307 157 NPFTLGHRHLVEQAAQRCDALHLFVVREDA--SFFPFSARLEMVRAGVAHLPNVVV 210
Cdd:TIGR01510 9 DPVTNGHLDIIKRAAALFDEVIVAVAKNPSkkPLFSLEERVELIKDATKHLPNVRV 64
|
|
| |
