|
Name |
Accession |
Description |
Interval |
E-value |
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
389-831 |
0e+00 |
|
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100097 Cd Length: 441 Bit Score: 533.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 389 IFEGATVRGLTNVELTPEFAAKLGAAYGSILPKDSFVLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYKL 468
Cdd:cd05805 1 LFGGRGVSGLINVDITPEFATRLGAAYGSTLPPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 469 TTFGESGGIHFRQSPDDPMATDILFYDAEGIEISSATAKNIERIFFKENFRRVHYTDPGGISEIPRIYDYYHEGFLHALD 548
Cdd:cd05805 81 RFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENAFFREDFRRAHVDEIGDITEPPDFVEYYIRGLLRALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 549 RKAIAKAAPKVVVDLNHSSAGEVLPALLNELGCEVIELNSQVTENCTgKGPEQDAKSMDQLSRIVVTLGAKAGFWMGPSG 628
Cdd:cd05805 161 TSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAP-RTDTERQRSLDRLGRIVKALGADFGVIIDPNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 629 ERLLLVDECGQAFSnIEALTTLAALVCKAERE-GSLVVPVSAPSAIEQLAAEAGMQVKRTKTDPRSIIESAKERQVrFAA 707
Cdd:cd05805 240 ERLILVDEAGRVIS-DDLLTALVSLLVLKSEPgGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALENVV-LAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 708 SMDGRFAFPSFQYNFDALHTVAKILELLVRTGLTLGQTRQMLPRRFYEHVEVSCSQEFKGGIMRKMSEDSVDQEASFIDG 787
Cdd:cd05805 318 DGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDELPRFYVLHKEVPCPWEAKGRVMRRLIEEAPDKSIELIDG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1224025872 788 VRIQMNQDWALVLPDQYRPVTHIIAESAELSTARRLVESYRLKV 831
Cdd:cd05805 398 VKIYEDDGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
387-834 |
2.14e-111 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 347.96 E-value: 2.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 387 KSIFEGATVRGLTNVELTPEFAAKLGAAYGSILPKD--SFVLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVL 464
Cdd:COG1109 4 KKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKggPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 465 RYKLTTFGESGGIHFRQSPDDPMATDILFYDAEGIEISSATAKNIERIFFKENFRRVHYTDPGGISEIPRIYDYYHEGFL 544
Cdd:COG1109 84 AFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAYIEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 545 HALDrKAIAKAAPKVVVDLNHSSAGEVLPALLNELGCEVIELNSQVTENCTGKGPEQDAKSMDQLSRIVVTLGAKAGFWM 624
Cdd:COG1109 164 SLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPEPENLEDLIEAVKETGADLGIAF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 625 GPSGERLLLVDECGQAFSNIEALTTLAALVCKAEREGSLVVPVSAPSAIEQLAAEAGMQVKRTKTDPRSIIESAKERQVR 704
Cdd:COG1109 243 DGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 705 FAASMDGRFAFPSFQYNFDALHTVAKILELLVRTGLTLGQTRQMLPRRFYEHVEVSCSQEFK-GGIMRKMSEDSVDQ-EA 782
Cdd:COG1109 323 LGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKiGAVMEKLREAVEDKeEL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 783 SFIDGVRIQMNQD-WALVLPDQYRPVTHIIAESAELSTARRLVESYRLKVERW 834
Cdd:COG1109 403 DTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-242 |
2.58e-94 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 295.14 E-value: 2.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYVTPLE 81
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 82 DFGTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEKPgw 160
Cdd:COG1208 81 PLGTGGALKRALPLLgDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 161 GEVFSDTINTGIYVLEPEVLDMIPEGENRDWSkDVFPQMLDNDDaLYGCHLEGYWADIGNTDSYLESCEDIAEGRVEINL 240
Cdd:COG1208 159 EEPPSNLINAGIYVLEPEIFDYIPEGEPFDLE-DLLPRLIAEGR-VYGYVHDGYWLDIGTPEDLLEANALLLSGKAPVVI 236
|
..
gi 1224025872 241 ME 242
Cdd:COG1208 237 WP 238
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-219 |
7.76e-89 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 280.24 E-value: 7.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYVTPLED 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEKPGWG 161
Cdd:cd04181 81 LGTAGAVRNAEDFLgDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPTLP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 162 EvfSDTINTGIYVLEPEVLDMIPEGENR--DWSKDVFPQMLDNDDaLYGCHLEGYWADIG 219
Cdd:cd04181 161 E--SNLANAGIYIFEPEILDYIPEILPRgeDELTDAIPLLIEEGK-VYGYPVDGYWLDIG 217
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
395-831 |
4.99e-68 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 232.46 E-value: 4.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 395 VRGLTNVELTPEFAAKLGAAYGSILPKDSFVLsGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYKLTTFGeS 474
Cdd:cd03087 7 IRGVVGEELTPELALKVGKALGTYLGGGTVVV-GRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAVRKLG-D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 475 GGIHFRQSPDDPMATDILFYDAEGIEISSATAKNIERIFFKENFRRVHYTDPGGISEIPRIYDYYHEGFLHALDRKAIAK 554
Cdd:cd03087 85 AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAIDEYIEAILDKVDIDGGKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 555 aaPKVVVDLNHSSAGEVLPALLNELGCEVIELNSQVTENCTGKGPEQDAKSMDQLSRIVVTLGAKAGFWMGPSGERLLLV 634
Cdd:cd03087 165 --LKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEPTPENLSELMELVRATGADLGIAHDGDADRAVFV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 635 DECGQAFSNIEALTTLAALVCKaEREGSLVVPVSAPSAIEQLAAEAGMQVKRTKTDPRSIIESAKERQVRFAASMDGRFA 714
Cdd:cd03087 243 DEKGRFIDGDKLLALLAKYLLE-EGGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNGGWI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 715 FPSFQYNFDALHTVAKILELLVRTGlTLGQTRQMLPRRFYEHVEVSCSQEFKGGIMRKMSEDSVDQEASF--IDGVRIQM 792
Cdd:cd03087 322 FPDHQLCRDGIMTAALLLELLAEEK-PLSELLDELPKYPLLREKVECPDEKKEEVMEAVEEELSDADEDVdtIDGVRIEY 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1224025872 793 NQDWALVLPDQYRPVTHIIAESAELSTARRLVESYRLKV 831
Cdd:cd03087 401 EDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-226 |
2.61e-64 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 215.15 E-value: 2.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSE-FGVRITYVTP 79
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKkLGIKITFSIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 80 LEDFGTAGAVKMAAKHL---DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKE-GKITKFL 155
Cdd:cd06425 81 TEPLGTAGPLALARDLLgddDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERFV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224025872 156 EKPgwgEVF-SDTINTGIYVLEPEVLDMIPEgENRDWSKDVFPQMLdNDDALYGCHLEGYWADIGNTDSYLE 226
Cdd:cd06425 161 EKP---KVFvGNKINAGIYILNPSVLDRIPL-RPTSIEKEIFPKMA-SEGQLYAYELPGFWMDIGQPKDFLK 227
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-232 |
7.74e-60 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 203.25 E-value: 7.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNR-PIMLHIIELLKKHGIDELVLLL--YHQPMViKNFFGDGSEFGVRITYVT 78
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILtqEHRFML-NELLGDGSKFGVQITYAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 79 PLEDFGTAGAVKMAAKHLDE---RFMIISGDLLTDFDLSQAIAFHEEHKAKATLT--LTSVKDPLQFGVVITNKEGKITK 153
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLGDeksDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTfgIVPVEPPTGYGVVEFDDNGRVIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 154 FLEKPGwGEVFSDTINTGIYVLEPEVLDMIPEGENRDWS-----KDVFPQMLDNDDALYGCHLEGY-WADIGNTDSYLES 227
Cdd:pfam00483 160 FVEKPK-LPKASNYASMGIYIFNSGVLDFLAKYLEELKRgedeiTDILPKALEDGKLAYAFIFKGYaWLDVGTWDSLWEA 238
|
....*
gi 1224025872 228 CEDIA 232
Cdd:pfam00483 239 NLFLL 243
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
3-224 |
5.65e-59 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 200.05 E-value: 5.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYVTPLED 82
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVKMAAKHLDERFMIISGDLLTDFDLSQAIAFHEEHKAKATL--TLTSVKDPlqFGVVITNkEGKITKFLEKPgw 160
Cdd:cd06426 81 LGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVcvREYEVQVP--YGVVETE-GGRITSIEEKP-- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224025872 161 geVFSDTINTGIYVLEPEVLDMIPEGENRDWSkDVFPQMLDNDDALYGCHLEGYWADIGNTDSY 224
Cdd:cd06426 156 --THSFLVNAGIYVLEPEVLDLIPKNEFFDMP-DLIEKLIKEGKKVGVFPIHEYWLDIGRPEDY 216
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
3-228 |
1.24e-56 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 193.92 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYV---TP 79
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYViepEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 80 LedfGTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEK- 157
Cdd:cd06915 81 L---GTGGAIKNALPKLpEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 158 ----PGWgevfsdtINTGIYVLEPEVLDMIPEGENRDwSKDVFPQMLDNDDaLYGCHLEGYWADIGNTDSYLESC 228
Cdd:cd06915 158 pgaaPGL-------INGGVYLLRKEILAEIPADAFSL-EADVLPALVKRGR-LYGFEVDGYFIDIGIPEDYARAQ 223
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-420 |
3.86e-54 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 192.81 E-value: 3.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYVTPL 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHLDERFMIISGDLLTDFDLSQAIAFHEEHkakaTLTLTSVKDPLQFGVVITNkEGKITKFLEKPGW 160
Cdd:TIGR03992 81 EQLGTADALGSAKEYVDDEFLVLNGDVLLDSDLLERLIRAEAP----AIAVVEVDDPSDYGVVETD-GGRVTGIVEKPEN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 161 GEvfSDTINTGIYVLEPEVLDMI------PEGEnRDWSKDVfpQMLDNDDALYGCHLEGYWADIGN-------TDSYLES 227
Cdd:TIGR03992 156 PP--SNLINAGIYLFSPEIFELLektklsPRGE-YELTDAL--QLLIDEGKVKAVELDGFWLDVGRpwdlldaNEALLDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 228 CEDIAEGRVEinlmekpvtparqdvrlflgeeasyvddENTSLKGMVVLGANTQVVGKARL-------SNCVVGRNCiie 300
Cdd:TIGR03992 231 LEPRIEGTVE----------------------------ENVTIKGPVVIGEGAVIRSGTYIegpvyigKNCDIGPNA--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 301 dgvelrnailwdniYVKKNStihgaVLCDNVRVGQKVVIEEgAVVAEETTI------GDeALIKKDVKIwprkvieGGAT 374
Cdd:TIGR03992 280 --------------YIRPYT-----VIGNNVHIGNAVEIKN-SIIMEGTKIphlsyvGD-SVIGENCNF-------GAGT 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 375 VTTNLiwgekwRksiFEGATVRGLTNVELTPEFAAKLGAAYG---------SILP 420
Cdd:TIGR03992 332 KVANL------R---HDDKPVKVTVKGKRVDTGRRKLGAIVGdgvktginvSINP 377
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-365 |
6.59e-44 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDEL-VLLLYHQPMVIKNFFGDGSEFGVRITYVTPL 80
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIgIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIA-FHEEHKAkATLTLTSVKDPLQFGVVITNKEGKITKFLEKP 158
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLgDDDFVVYLGDNLIQDGISRFVKsFEEKDYD-ALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 159 gwGEVFSDTINTGIYVLEPEVLDMI----PEGENRDWSKDVFPQMLDNDDALYGCHLEGYWADIGNTDSYLESCEDIaeg 234
Cdd:TIGR01208 160 --KEPPSNLAVVGLYMFRPLIFEAIknikPSWRGELEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLI--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 235 rveinLMEkpVTPARQDVrlflgeeasyvdDENTSLKGMVVLGANTQVVGKARLSNCVVGRNCIIEdgvelrnailwdNI 314
Cdd:TIGR01208 235 -----LDE--VEREVQGV------------DDESKIRGRVVVGEGAKIVNSVIRGPAVIGEDCIIE------------NS 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 315 YVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIgDEALIKKDVKIWP 365
Cdd:TIGR01208 284 YIGPYTSIGEGVVIRDAEVEHSIVLDESVIEGVQARI-VDSVIGKKVRIKG 333
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-226 |
1.27e-42 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 155.03 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEFGVRITYVTPL 80
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITnKEGKITKFLEKPg 159
Cdd:cd04189 81 EPLGLAHAVLAARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEKP- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224025872 160 wGEVFSDTINTGIYVLEPEVLDMIPEGENrdwSK-------DVFPQMLDNDDALYGCHLEGYWADIGNTDSYLE 226
Cdd:cd04189 159 -KEPPSNLALVGVYAFTPAIFDAISRLKP---SWrgeleitDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLE 228
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
395-828 |
1.21e-41 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 158.63 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 395 VRGLTNVELTPEFAAKLGAAYGSILP---KDSFVLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYKLTTF 471
Cdd:cd05803 7 IRGIVGEGLTPEVITRYVAAFATWQPertKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 472 GESGGIHFRQSPDDPMATDILFYDAEGIEISSATAKNIERIFFKENFRRVHYTDPGGISEIPriyDYYHEGFLHAL---- 547
Cdd:cd05803 87 QASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSE---DAIAEHIDKVLalvd 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 548 -DRKAIAKAAPKVVVDLNHSSAGEVLPALLNELGCEVIELNsqvtenCTGKG-----PEQDAKSMDQLSRIVVTLGAKAG 621
Cdd:cd05803 164 vDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLN------CEPTGlfphtPEPLPENLTQLCAAVKESGADVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 622 FWMGPSGERLLLVDECGQAFSniEALTtlaaLVCKAE-------REGSLVVPVSAPSAIEQLAAEAGMQVKRTKTDPRSI 694
Cdd:cd05803 238 FAVDPDADRLALVDEDGRPIG--EEYT----LALAVDyvlkyggRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 695 IESAKERQVRFAASMDGRFAFPSFQYNFDALHTVAKILELLVRTGLTLGQTRQMLPRRFYEHVEVSCSQEFKGGIMRKMS 774
Cdd:cd05803 312 VEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEALERLLKKLE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1224025872 775 EDSVDQEASFIDGVRIQMNQDWALVLPDQYRPVTHIIAESAELSTARRLVESYR 828
Cdd:cd05803 392 AYFKDAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-226 |
1.80e-41 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 153.71 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLL--YHQPMvIKNFFGDGSEFGVRITYV- 77
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIStpEDGPQ-FERLLGDGSQLGIKISYAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 78 --TPLedfGTAGAVKMAAKHL-DERFMIISGDLLTDFD-LSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITK 153
Cdd:COG1209 80 qpEPL---GLAHAFIIAEDFIgGDPVALVLGDNIFYGDgLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 154 FLEKPgwgEVF-SDTINTGIYVLEPEVLDMI------PEGE------NRdwskdvfpQMLDNDDALYGCHLEGY-WADIG 219
Cdd:COG1209 157 LEEKP---KEPkSNLAVTGLYFYDNDVVEIAknlkpsARGEleitdaNQ--------AYLERGKLVVELLGRGFaWLDTG 225
|
....*..
gi 1224025872 220 NTDSYLE 226
Cdd:COG1209 226 THESLLE 232
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-360 |
4.56e-41 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 155.23 E-value: 4.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPL---YnRPI------MLHiiellkkHGIDELVLLLYHQPMVIKNFFGDGSE--FG 71
Cdd:COG0448 4 AIILAGGRGSRLGPLTKDRAKPAVPFggkY-RIIdfplsnCVN-------SGIRRVGVLTQYKSHSLNDHIGSGKPwdLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 72 VRITYVTPL--------EDF--GTAGAVkmaAKHLD--ERF-----MIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSV 134
Cdd:COG0448 76 RKRGGVFILppyqqregEDWyqGTADAV---YQNLDfiERSdpdyvLILSGDHIYKMDYRQMLDFHIESGADITVACIEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 135 --KDPLQFGVVITNKEGKITKFLEKPGWGEvfSDTINTGIYVLEPEVL-----DMIPEGENrDWSKDVFPQMLDNDDAlY 207
Cdd:COG0448 153 prEEASRFGVMEVDEDGRITEFEEKPKDPK--SALASMGIYVFNKDVLielleEDAPNSSH-DFGKDIIPRLLDRGKV-Y 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 208 GCHLEGYWADIGNTDSYLESCEDIAEGRVEINLMEK--PV-TPARQDVRLFLGEEASYVDdentSL--KGMVVLGantqv 282
Cdd:COG0448 229 AYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPewPIyTKQKDLPPAKFVRGGKVKN----SLvsNGCIISG----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 283 vgkaRLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVI-EEGAVVAEETTIGDE-ALIKKD 360
Cdd:COG0448 300 ----TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIgEDPEEDRKRFTVSSGiVVVGKG 375
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
3-215 |
4.21e-39 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 145.79 E-value: 4.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGD----GSEFGV------ 72
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNyflhNSDVTIdlgtnr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 73 -----------RITYVTPLEDFGTAGAVKMAAKHL--DERFMIISGDLLTDFDLSQAIAFHEEHKAKAtlTLTSVKDPLQ 139
Cdd:cd02524 81 ielhnsdiedwKVTLVDTGLNTMTGGRLKRVRRYLgdDETFMLTYGDGVSDVNINALIEFHRSHGKLA--TVTAVHPPGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 140 FGVVITNKEGKITKFLEKP----GWgevfsdtINTGIYVLEPEVLDMIpEGENRDWSKDVFPQMLDnDDALYGCHLEGYW 215
Cdd:cd02524 159 FGELDLDDDGQVTSFTEKPqgdgGW-------INGGFFVLEPEVFDYI-DGDDTVFEREPLERLAK-DGELMAYKHTGFW 229
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
389-799 |
2.41e-37 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 145.73 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 389 IFEGATVRGLTNVELTPEFAAKLGAAYGSILPKDSF--VLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRY 466
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLEKGAkkVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 467 KLTTFGESGGIHFRQSPDDPMATDI-LFYDAEGIeiSSATAKNIERIFFKENFRRVhyTDPGGISEIPRIYDYYHegFLh 545
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFkIVIGGGPL--SGEDIQALRERAEKGDFAAA--TGRGSVEKVDILPDYID--RL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 546 aldRKAIAKAAP--KVVVDLNHSSAGEVLPALLNELGCEVIELnsqvteNCTGKG--------PEqDAKSMDQLSRIVVT 615
Cdd:cd03089 154 ---LSDIKLGKRplKVVVDAGNGAAGPIAPQLLEALGCEVIPL------FCEPDGtfpnhhpdPT-DPENLEDLIAAVKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 616 LGAKAGF-WMGpSGERLLLVDECGQAFSNiEALTTLAALVCKAEREGSLVV-PVSAPSAIEQLAAEAGMQVKRTKTDPRS 693
Cdd:cd03089 224 NGADLGIaFDG-DGDRLGVVDEKGEIIWG-DRLLALFARDILKRNPGATIVyDVKCSRNLYDFIEEAGGKPIMWKTGHSF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 694 IIESAKERQVRFAASMDGRFAFPSFQYNFD-ALHTVAKILELLVRTGLTLGQTRQMLPrRFYEHVE--VSCSQEFKGGIM 770
Cdd:cd03089 302 IKAKMKETGALLAGEMSGHIFFKDRWYGFDdGIYAALRLLELLSKSGKTLSELLADLP-KYFSTPEirIPVTEEDKFAVI 380
|
410 420 430
....*....|....*....|....*....|.
gi 1224025872 771 RKMSEDSVDQEA--SFIDGVRIQMNQDWALV 799
Cdd:cd03089 381 ERLKEHFEFPGAeiIDIDGVRVDFEDGWGLV 411
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-226 |
1.95e-35 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 133.85 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDgSEFGVRITY----V 77
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITIsdepD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 78 TPLEdfgTAGAVKMAAKHL-DERFMIISGDLLTDFDLSQAIAFHEEhKAKATLTLTSVKDPLQF---GVVITNKEGKITK 153
Cdd:cd06422 80 ELLE---TGGGIKKALPLLgDEPFLVVNGDILWDGDLAPLLLLHAW-RMDALLLLLPLVRNPGHngvGDFSLDADGRLRR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 154 FLEKPGWGEVFsdtinTGIYVLEPEVLDMIPEGenRDWSKDVFPQMLDNdDALYGCHLEGYWADIGNTDSYLE 226
Cdd:cd06422 156 GGGGAVAPFTF-----TGIQILSPELFAGIPPG--KFSLNPLWDRAIAA-GRLFGLVYDGLWFDVGTPERLLA 220
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-357 |
6.07e-32 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 128.45 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRpimLHIIEL----LKKHGIDELVLLLYHQPMVIKNFFGDGSEFGV-RI- 74
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGK---YRIIDFtlsnCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLdRIn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 75 TYVTPLEDF----------GTAGAVKMAAKHLD----ERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVkdPLQ- 139
Cdd:PRK05293 81 GGVTILPPYseseggkwykGTAHAIYQNIDYIDqydpEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEV--PWEe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 140 ---FGVVITNKEGKITKFLEKPGwgEVFSDTINTGIYVLEPEVL-DMIPEGEN-----RDWSKDVFPQMLDNDDALYGCH 210
Cdd:PRK05293 159 asrFGIMNTDENMRIVEFEEKPK--NPKSNLASMGIYIFNWKRLkEYLIEDEKnpnssHDFGKNVIPLYLEEGEKLYAYP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 211 LEGYWADIGNTDSYLESCEDIAEGRVEINLMEK--------PVTPARqdvrlFLGEEASyvddentslkgmvvlgantqv 282
Cdd:PRK05293 237 FKGYWKDVGTIESLWEANMELLRPENPLNLFDRnwriysvnPNLPPQ-----YIAENAK--------------------- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 283 vgkarLSNCVVGRNCIIEDGVElrNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEgAVVAEETTIGDEALI 357
Cdd:PRK05293 291 -----VKNSLVVEGCVVYGTVE--HSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIER-AIIGENAVIGDGVII 357
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
3-218 |
2.88e-31 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 123.13 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGG--FGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKK-HGIDELVLLLYHQPMVIKNFFGDGS-EFGVRITYVT 78
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQqEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 79 PLEDFGTAGAV----KMAAKHLDERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSV--KDPLQFGVVITN-KEGKI 151
Cdd:cd06428 81 EYKPLGTAGGLyhfrDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDpSTGEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 152 TKFLEKPgwgEVF-SDTINTGIYVLEPEVLDMI-------------PEGENRD-------WSKDVFPQMLDNdDALYGCH 210
Cdd:cd06428 161 LHYVEKP---ETFvSDLINCGVYLFSPEIFDTIkkafqsrqqeaqlGDDNNREgraevirLEQDVLTPLAGS-GKLYVYK 236
|
....*...
gi 1224025872 211 LEGYWADI 218
Cdd:cd06428 237 TDDFWSQI 244
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-378 |
6.16e-29 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 121.09 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEfgvritYVTPLED 82
Cdd:PRK14354 5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSE------FALQEEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVKMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEK 157
Cdd:PRK14354 76 LGTGHAVMQAEEFLadkEGTTLVICGDtpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKIVEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 158 pgwgevfSDT---------INTGIYVLEP----EVLDMI----PEGENrdWSKDVFPQMLDNDDALYGCHLEGYWADIGN 220
Cdd:PRK14354 156 -------KDAteeekqikeINTGTYCFDNkalfEALKKIsndnAQGEY--YLTDVIEILKNEGEKVGAYQTEDFEESLGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 221 TDSY-LESCEDIAEGRVEINLMEKPVTparqdvrlFLGEEASYVDDE-----NTSLKGMVVLGANTqVVGkarlSNCVVG 294
Cdd:PRK14354 227 NDRVaLAEAEKVMRRRINEKHMVNGVT--------IIDPESTYIDADveigsDTVIEPGVVIKGNT-VIG----EDCVIG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 295 -----RNCIIEDGVELRNAILWDNIyVKKNSTI----H---GAVLCDNVRVG-----QKVVIEEGAVVAEETTIGDeALI 357
Cdd:PRK14354 294 pgsriVDSTIGDGVTITNSVIEESK-VGDNVTVgpfaHlrpGSVIGEEVKIGnfveiKKSTIGEGTKVSHLTYIGD-AEV 371
|
410 420
....*....|....*....|.
gi 1224025872 358 KKDVKIwprkvieGGATVTTN 378
Cdd:PRK14354 372 GENVNI-------GCGTITVN 385
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1-378 |
6.87e-29 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 120.90 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHpltIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDgsefgVRITYVTPL 80
Cdd:COG1207 3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD-----LDVEFVLQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFL 155
Cdd:COG1207 75 EQLGTGHAVQQALPALpgdDGTVLVLYGDvpLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 156 EkpgwgevFSDT---------INTGIYVLEPEVLdmipegenrdwsKDVFPQmLDNDDA---LY---------------- 207
Cdd:COG1207 155 E-------EKDAteeqraireINTGIYAFDAAAL------------REALPK-LSNDNAqgeYYltdviaiaradglkva 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 208 GCHLEGYWADIG-NTDSYLESCEDIAEGRVEINLMEKPVT---PARQDVR--LFLGEEAsyVDDENTSLKGMVVLGANTq 281
Cdd:COG1207 215 AVQPEDPWEVLGvNDRVQLAEAERILQRRIAERLMRAGVTiidPATTYIDgdVEIGRDV--VIDPNVILEGKTVIGEGV- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 282 VVGkarlSNCVVgRNCIIEDGVELRNAILwDNIYVKKNSTI----H---GAVLCDNVRVG-----QKVVIEEGAVVAEET 349
Cdd:COG1207 292 VIG----PNCTL-KDSTIGDGVVIKYSVI-EDAVVGAGATVgpfaRlrpGTVLGEGVKIGnfvevKNSTIGEGSKVNHLS 365
|
410 420
....*....|....*....|....*....
gi 1224025872 350 TIGDeALIKKDVKIwprkvieGGATVTTN 378
Cdd:COG1207 366 YIGD-AEIGEGVNI-------GAGTITCN 386
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-183 |
7.42e-26 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 106.89 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDElVLLLY---HQPMVIKnFFGDGSEFGVRITY- 76
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIRE-ILIIStpeDLPLFKE-LLGDGSDLGIRITYa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 77 VTPLEDfGTAGAVKMAAKHL-DERFMIISGD-LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKF 154
Cdd:cd02538 79 VQPKPG-GLAQAFIIGEEFIgDDPVCLILGDnIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSI 157
|
170 180
....*....|....*....|....*....
gi 1224025872 155 LEKPgwGEVFSDTINTGIYVLEPEVLDMI 183
Cdd:cd02538 158 EEKP--KKPKSNYAVTGLYFYDNDVFEIA 184
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-378 |
7.90e-26 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 111.76 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEfgvrITYVTPLED 82
Cdd:PRK14355 6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD----VSFALQEEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVKMAAKHLDE---RFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEK 157
Cdd:PRK14355 79 LGTGHAVACAAPALDGfsgTVLILCGDvpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 158 PGWG--EVFSDTINTGIYVLEPEVL-------------------DMIPEGENRDWSKDVFPqmLDNDDALYGChlegywa 216
Cdd:PRK14355 159 KDATpeERSIREVNSGIYCVEAAFLfdaigrlgndnaqgeyyltDIVAMAAAEGLRCLAFP--VADPDEIMGV------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 217 digNTDSYLESCEDIAEGRVEINLMEKPVTparqdvrlFLGEEASYVDDEntslkgmVVLGANTQVVGKARLS-NCVVGR 295
Cdd:PRK14355 230 ---NDRAQLAEAARVLRRRINRELMLAGVT--------LIDPETTYIDRG-------VVIGRDTTIYPGVCISgDTRIGE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 296 NCIIEDGVELRNAILWDNIYVK-----KNSTIH-------------GAVLCDNVRVG-----QKVVIEEGAVVAEETTIG 352
Cdd:PRK14355 292 GCTIEQGVVIKGCRIGDDVTVKagsvlEDSVVGddvaigpmahlrpGTELSAHVKIGnfvetKKIVMGEGSKASHLTYLG 371
|
410 420
....*....|....*....|....*.
gi 1224025872 353 DeALIKKDVKIwprkvieGGATVTTN 378
Cdd:PRK14355 372 D-ATIGRNVNI-------GCGTITCN 389
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
387-520 |
2.06e-25 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 102.30 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 387 KSIFEGATVRGLTNV-ELTPEFAAKLGAAYGSILPKDSF---VLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLP 462
Cdd:pfam02878 1 RQLFGTSGIRGKVGVgELTPEFALKLGQAIASYLRAQGGggkVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224025872 463 VLRYKLTTFGESGGIHFRQSPDDPMATDILFYDAEGIEISSATAKNIERIFFKENFRR 520
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
3-180 |
4.79e-25 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 104.13 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSefgvrITYVTPLED 82
Cdd:cd02540 1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPN-----VEFVLQEEQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVKMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEk 157
Cdd:cd02540 73 LGTGHAVKQALPALkdfEGDVLVLYGDvpLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVE- 151
|
170 180 190
....*....|....*....|....*....|..
gi 1224025872 158 pgwgevFSD---------TINTGIYVLEPEVL 180
Cdd:cd02540 152 ------EKDateeekairEVNAGIYAFDAEFL 177
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-218 |
1.07e-22 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 97.62 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGdgsEFGVRITYVT-PL 80
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA---RPGPDVTFVYnPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 -EDFGTAGAVKMAAKHLDERFMIISGDLLTDFDLSQAIAfheEHKAKATLTL-TSVKDPLQFGV-VITNKEGKITKFLEK 157
Cdd:COG1213 78 yDETNNIYSLWLAREALDEDFLLLNGDVVFDPAILKRLL---ASDGDIVLLVdRKWEKPLDEEVkVRVDEDGRIVEIGKK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 158 PGWGEVFSDTIntGIYVLEPEVLD--------MIPEGENRDWSKDVFPQMLDNDDALYGCHLEG-YWADI 218
Cdd:COG1213 155 LPPEEADGEYI--GIFKFSAEGAAalrealeaLIDEGGPNLYYEDALQELIDEGGPVKAVDIGGlPWVEI 222
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-352 |
1.52e-22 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 101.46 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIP-----------LYNrpiMLHiiellkkHGIDE-LVLLLYHQPMVIK------NFF 64
Cdd:PRK00725 18 ALILAGGRGSRLKELTDKRAKPAVYfggkfriidfaLSN---CIN-------SGIRRiGVLTQYKAHSLIRhiqrgwSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 65 GdgSEFGVRITYVTPLEDF-------GTAGAV----KMAAKHLDERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTS 133
Cdd:PRK00725 88 R--EELGEFVDLLPAQQRVdeenwyrGTADAVyqnlDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 134 V--KDPLQFGVVITNKEGKITKFLEKPGWGEVFSDTINT-----GIYVLEPEVL------DMIPEGENRDWSKDVFPQML 200
Cdd:PRK00725 166 VprEEASAFGVMAVDENDRITAFVEKPANPPAMPGDPDKslasmGIYVFNADYLyelleeDAEDPNSSHDFGKDIIPKIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 201 DN--------DDALYGCHLEG--YWADIGNTDSYLESCEDIAEGRVEINLMEK---------PVTPARqdvrlflgeeas 261
Cdd:PRK00725 246 EEgkvyahpfSDSCVRSDPEEepYWRDVGTLDAYWQANLDLASVTPELDLYDRnwpiwtyqeQLPPAK------------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 262 YVDDENTSlKGMVVlgantqvvgkarlsNCVVGRNCIIEDGVeLRNAILWDNIYVKKNSTIHGAVLCDNVRVG-----QK 336
Cdd:PRK00725 314 FVFDRSGR-RGMAI--------------NSLVSGGCIISGAV-VRRSVLFSRVRVNSFSNVEDSVLLPDVNVGrscrlRR 377
|
410
....*....|....*.
gi 1224025872 337 VVIEEGAVVAEETTIG 352
Cdd:PRK00725 378 CVIDRGCVIPEGMVIG 393
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-137 |
6.17e-22 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 95.01 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPM-----VIKNFFGDGSEFGVRIT 75
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQaiiehLLKSKWSSLSSKMIVDV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 76 YVTPL-EDFGTAGAVKMAAKHLDERFMIISGDLLTDFDLSQAI-AFHEEHK-AKATLTLTSVKDP 137
Cdd:cd02507 81 ITSDLcESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLeERRKKDKnAIATLTVLLASPP 145
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-339 |
1.33e-21 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 98.42 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MK---AVIMAGGFGTRIHPLTIDLPKPMIPLYNR------PI-------MLHIIEL-------LKKHgidelvlllyhqp 57
Cdd:PRK02862 1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyrlidiPIsncinsgINKIYVLtqfnsasLNRH------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 58 mvIK---NF--FGDGseFgVRI-----TYVTPLEDFGTAGAVKMAAKHLDER----FMIISGDLLTDFDLSQAIAFHEEH 123
Cdd:PRK02862 68 --ISqtyNFdgFSGG--F-VEVlaaqqTPENPSWFQGTADAVRKYLWHFQEWdvdeYLILSGDQLYRMDYRLFVQHHRET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 124 KAKATLTLTSV--KDPLQFGVVITNKEGKITKFLEKPGwGEVF----SDT----------------INTGIYVLEPEVL- 180
Cdd:PRK02862 143 GADITLAVLPVdeKDASGFGLMKTDDDGRITEFSEKPK-GDELkamaVDTsrlglspeeakgkpylASMGIYVFSRDVLf 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 181 DMIPEGENR-DWSKDVFPQMLDnDDALYGCHLEGYWADIGNTDSYLEScediaegrvEINLMEKPvTPARQdvrlFLGEE 259
Cdd:PRK02862 222 DLLNKNPEYtDFGKEIIPEAIR-DYKVQSYLFDGYWEDIGTIEAFYEA---------NLALTQQP-NPPFS----FYDEK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 260 A-----------SYVDDENTSlKGMVVLGAntqVVGKARLSNCVVGRNCIIEDGVELRNAILW----------------- 311
Cdd:PRK02862 287 ApiytrarylppSKLLDATIT-ESIIAEGC---IIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrke 362
|
410 420 430
....*....|....*....|....*....|
gi 1224025872 312 --DNIYVKKNSTIHGAVLCDNVRVGQKVVI 339
Cdd:PRK02862 363 gkPPLGIGEGTTIKRAIIDKNARIGNNVRI 392
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-137 |
7.41e-21 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 91.95 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLY--HQPMV---IKNFFGDGSEFGVRIT 75
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPeeEQAEIstyLRSFPLNLKQKLDEVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224025872 76 YVtPLEDFGTAGAVKMAAKHLDERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDP 137
Cdd:cd04198 81 IV-LDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVS 141
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-375 |
1.20e-20 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 95.28 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIP--------------LYNRPIMlHIIELL--KKHGIDElvlllyH--QPMVIKNFF 64
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggsyrlidfvlsnLVNSGYL-RIYVLTqyKSHSLDR------HisQTWRLSGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 65 GdgsefgvriTYVTPL--------EDF-GTAGAVkMAAKHL--DER---FMIISGDLLTDFDLSQAIAFHEEHKAKATLT 130
Cdd:PRK00844 81 G---------NYITPVpaqqrlgkRWYlGSADAI-YQSLNLieDEDpdyVVVFGADHVYRMDPRQMVDFHIESGAGVTVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 131 ltSVKDPL----QFGVVITNKEGKITKFLEKPGW--------GEVFSdtiNTGIYVLEPEVL-DMIPEGENR-----DWS 192
Cdd:PRK00844 151 --AIRVPReeasAFGVIEVDPDGRIRGFLEKPADppglpddpDEALA---SMGNYVFTTDALvDALRRDAADedsshDMG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 193 KDVFPQMLDNDDA-LY--------GC--HLEGYWADIGNTDSYLESCEDIAEGRVEINLMEK---------PVTPARqdv 252
Cdd:PRK00844 226 GDIIPRLVERGRAyVYdfstnevpGAteRDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNRewpiytsspNLPPAK--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 253 rlFLGEEASYVDDENTslkgMVVLGAntqVVGKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVr 332
Cdd:PRK00844 303 --FVDGGGRVGSAQDS----LVSAGS---IISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNV- 372
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1224025872 333 vgqkvvieegaVVAEETTIGDEAliKKDVKIWprKVIEGGATV 375
Cdd:PRK00844 373 -----------VVPPGATIGVDL--EEDRRRF--TVSEGGIVV 400
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-232 |
4.69e-20 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 90.67 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFgDGSEF---------- 70
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHF-DRSYEleetlekkgk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 71 ------------GVRITYVTPLEDFGTAGAVKMAAKHL-DERFMIISGDLLTDFD---LSQAIAFHEEHKaKATLTLTSV 134
Cdd:cd02541 80 tdlleevriisdLANIHYVRQKEPLGLGHAVLCAKPFIgDEPFAVLLGDDLIDSKepcLKQLIEAYEKTG-ASVIAVEEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 135 --KDPLQFGVV----ITNKEGKITKFLEKPGWGEVFSDTINTGIYVLEPEVLDMIpegenrdwsKDVFP----------- 197
Cdd:cd02541 159 ppEDVSKYGIVkgekIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDIL---------ENTKPgkggeiqltda 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1224025872 198 -QMLDNDDALYGCHLEGYWADIGNTDSYLESCEDIA 232
Cdd:cd02541 230 iAKLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFA 265
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
275-353 |
6.17e-19 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 81.86 E-value: 6.17e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224025872 275 VLGANTQVVGKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGD 353
Cdd:cd05787 1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
275-353 |
6.24e-18 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 78.82 E-value: 6.24e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224025872 275 VLGANTQVVGKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGD 353
Cdd:cd03356 1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
3-218 |
2.13e-16 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 79.20 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDgsefGVRITYVTPlED 82
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK----YPNIKFVYN-PD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 FGTAGAVK---MAAKHLDERFMIISGDLLtdFDlSQAIAFHEEHKAKATLTLTS--------VKDPLQFGVVITNKEGKI 151
Cdd:cd02523 76 YAETNNIYslyLARDFLDEDFLLLEGDVV--FD-PSILERLLSSPADNAILVDKktkewedeYVKDLDDAGVLLGIISKA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 152 tKFLEKPGWgevfsdtINTGIYVLEPEVLD--------MIPEGENRDWSKDVFPQMLDNDDALYGCHLEGYWADI 218
Cdd:cd02523 153 -KNLEEIQG-------EYVGISKFSPEDADrlaealeeLIEAGRVNLYYEDALQRLISEEGVKVKDISDGFWYEI 219
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
539-638 |
7.64e-16 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 73.86 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 539 YHEGFLHALDRKAIAKAAPKVVVDLNHSSAGEVLPALLNELGCEVIELNSQVTENCTGKGPE-QDAKSMDQLSRIVVTLG 617
Cdd:pfam02879 2 YIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNpEEPEALALLIELVKSVG 81
|
90 100
....*....|....*....|.
gi 1224025872 618 AKAGFWMGPSGERLLLVDECG 638
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-232 |
1.46e-15 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 78.18 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMV-IKNFFGDGSEFGVRITY-VTP 79
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPrFQQLLGDGSQWGLNLQYkVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 80 LEDfGTAGAVKMAAKHL--DERFMIISGDLLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFLEK 157
Cdd:PRK15480 85 SPD-GLAQAFIIGEEFIggDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 158 PgwGEVFSDTINTGIYVLEPEVLDMI----PEGENRDWSKDVFPQMLDNDDALYGCHLEGY-WADIGNTDSYLESCEDIA 232
Cdd:PRK15480 164 P--LQPKSNYAVTGLYFYDNDVVEMAknlkPSARGELEITDINRIYMEQGRLSVAMMGRGYaWLDTGTHQSLIEASNFIA 241
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
275-350 |
5.79e-15 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 70.68 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 275 VLGANTQVVGKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVV-----IEEGAVVAEET 349
Cdd:cd04652 1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKlkdclVGSGYRVEAGT 80
|
.
gi 1224025872 350 T 350
Cdd:cd04652 81 E 81
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-361 |
1.81e-14 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 76.69 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQP-MVIKNFFGDGSEFgvrityVTPLE 81
Cdd:PRK14356 8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRAdMVRAAFPDEDARF------VLQEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 82 DFGTAGAVKMAAKHLD----ERFMIISGD--LLTDfdlsQAIAFHEEHKAKATLTLTSVK--DPLQFGVVItNKEGKITK 153
Cdd:PRK14356 79 QLGTGHALQCAWPSLTaaglDRVLVVNGDtpLVTT----DTIDDFLKEAAGADLAFMTLTlpDPGAYGRVV-RRNGHVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 154 FLEKPGWGEVF----SDTINTGIYVLEPEVLD-MIPEGENRDWSK----------------DVFPQMLDNDDALYGChle 212
Cdd:PRK14356 154 IVEAKDYDEALhgpeTGEVNAGIYYLRLDAVEsLLPRLTNANKSGeyyitdlvglavaegmNVLGVNCGEDPNLLGV--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 213 gywadigNTDSYLESCEDIAEGRVEINLMEKPVT-PARQDVRLflgeeasyvddentslKGMVVLGANTQVVGKARL-SN 290
Cdd:PRK14356 231 -------NTPAELVRSEELLRARIVEKHLESGVLiHAPESVRI----------------GPRATIEPGAEIYGPCEIyGA 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 291 CVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDV 361
Cdd:PRK14356 288 SRIARGAVIHSHCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAV 358
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-359 |
1.96e-14 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 76.34 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGiDELVLLLYHQPMVIKNFFGDGsefgVRItyVTPL 80
Cdd:PRK14357 1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEW----VKI--FLQE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVkMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNkEGKITKFL 155
Cdd:PRK14357 71 EQLGTAHAV-MCARDFiepGDDLLILYGDvpLISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRD-GGKYRIVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 156 EKPGWGEVFS-DTINTGIYVLEPE-VLDMIPEGENRDWSK-----DVFPQM-------LDNDDALYGChlegywadigNT 221
Cdd:PRK14357 149 DKDAPEEEKKiKEINTGIYVFSGDfLLEVLPKIKNENAKGeyyltDAVNFAekvrvvkTEDLLEITGV----------NT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 222 DSYLESCEDIAEGRVEINLMEKPVTparqdvrlflgeeasYVDDENTSLKGMVVLGANTQVV------GKARlsncvVGR 295
Cdd:PRK14357 219 RIQLAWLEKQLRMRILEELMENGVT---------------ILDPNTTYIHYDVEIGMDTIIYpmtfieGKTR-----IGE 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224025872 296 NCIIEDGVELRNAILWDNIYVKKnSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKK 359
Cdd:PRK14357 279 DCEIGPMTRIVDCEIGNNVKIIR-SECEKSVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKK 341
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-359 |
4.51e-13 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 72.27 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAV-IMAGGFGTRihpLTIDLPKPMIPLYNRPIM---LHIIELLKKHGIdeLVLLLYHQPMVIKNFFGDGSefgvrITY 76
Cdd:PRK14360 1 MLAVaILAAGKGTR---MKSSLPKVLHPLGGKSLVervLDSCEELKPDRR--LVIVGHQAEEVEQSLAHLPG-----LEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 77 VTPLEDFGTAGAVKMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKI 151
Cdd:PRK14360 71 VEQQPQLGTGHAVQQLLPVLkgfEGDLLVLNGDvpLLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNNLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 152 TKFLEKpgwgevfSDT---------INTGIYVLepevldmipegenrDWSK--DVFPQM-LDND-------DALYGC--- 209
Cdd:PRK14360 151 EQIVED-------RDCtpaqrqnnrINAGIYCF--------------NWPAlaEVLPKLsSNNDqkeyyltDTVSLLdpv 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 210 -HLEgyWADIG-----NTDSYLESCEDIAEGRVEINLMEKPVTparqdvrlfLGEEASYVDDENTSLKGMVVLGANTQVV 283
Cdd:PRK14360 210 mAVE--VEDYQeingiNDRKQLAQCEEILQNRIKEKWMLAGVT---------FIDPASCTISETVELGPDVIIEPQTHLR 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224025872 284 GkarlsNCVVGRNCIIEDGVELRNAILWDNIYVkKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKK 359
Cdd:PRK14360 279 G-----NTVIGSGCRIGPGSLIENSQIGENVTV-LYSVVSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKK 348
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-378 |
8.41e-13 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 71.60 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSefgvrITYVTPL 80
Cdd:PRK09451 6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEP-----LNWVLQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHL--DERFMIISGD--LLTDFDLSQAIAfheeHKAKATLTLTSVK--DPLQFGvVITNKEGKITKF 154
Cdd:PRK09451 78 EQLGTGHAMQQAAPFFadDEDILMLYGDvpLISVETLQRLRD----AKPQGGIGLLTVKldNPTGYG-RITRENGKVVGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 155 LEKPGWGE--VFSDTINTGIyvlepevldMIPEGEN-RDW-SKdvfpqmLDNDDAlygcHLEGYWADI------------ 218
Cdd:PRK09451 153 VEQKDATDeqRQIQEINTGI---------LVANGADlKRWlAK------LTNNNA----QGEYYITDIialahqegreiv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 219 ------------GNTDSYLESCEDIAEGRVEINLMEKPVT---PARQDVRLFLGEEASYVDDENTSLKGMVVLGANTQVV 283
Cdd:PRK09451 214 avhpqrlsevegVNNRLQLARLERVYQAEQAEKLLLAGVMlrdPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 284 GKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIH-GAVLCDNVRVG-----QKVVIEEGAVVAEETTIGDeALI 357
Cdd:PRK09451 294 AGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRpGAELAEGAHVGnfvemKKARLGKGSKAGHLTYLGD-AEI 372
|
410 420
....*....|....*....|.
gi 1224025872 358 KKDVKIwprkvieGGATVTTN 378
Cdd:PRK09451 373 GDNVNI-------GAGTITCN 386
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-303 |
8.98e-13 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 71.17 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 4 VIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGiDELVLLLYHQPMVIKNFFgdGSEF-GVRItYVTPLED 82
Cdd:PRK14359 6 IILAAGKGTRMKS---SLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQKERIKEAV--LEYFpGVIF-HTQDLEN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 83 F-GTAGAVK-MAAKHldERFMIISGD--LLTDFDLSQAIafheEHKAKATLTLTSVKDPLQFGVVItNKEGKITKFLEKP 158
Cdd:PRK14359 79 YpGTGGALMgIEPKH--ERVLILNGDmpLVEKDELEKLL----ENDADIVMSVFHLADPKGYGRVV-IENGQVKKIVEQK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 159 GWG--EVFSDTINTGIYVLEPEVLdmipegenrdwsKDVFPQmLDNDDAlygcHLEGYWADI------------------ 218
Cdd:PRK14359 152 DANeeELKIKSVNAGVYLFDRKLL------------EEYLPL-LKNQNA----QKEYYLTDIialaiekgetikavfvde 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 219 ----GNTDSYLESC-EDIAEGRVEINLMEKPVTparqdVRLflgEEASYVdDENTSLKGMVVLGANTQVVGKARLSNCVV 293
Cdd:PRK14359 215 enfmGVNSKFELAKaEEIMQERIKKNAMKQGVI-----MRL---PETIYI-ESGVEFEGECELEEGVRILGKSKIENSHI 285
|
330
....*....|
gi 1224025872 294 GRNCIIEDGV 303
Cdd:PRK14359 286 KAHSVIEESI 295
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-357 |
1.12e-12 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 71.04 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPL---YnRPIMLHIIELLKKhGIDEL-VLLLYHQ-----------PMVIKNFFGDG 67
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnY-RLIDIPMSNCINS-GINKIyVLTQFNSaslnrhlsrayNFGNGGNFGDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 68 S-EfgVRITYVTPLED--F-GTAGAVKM-------AAKHLDERFMIISGDLLTDFDLSQAIAFHEEHKAK---ATLTLTS 133
Cdd:PLN02241 84 FvE--VLAATQTPGEKgwFqGTADAVRQflwlfedAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADitiACLPVDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 134 VKDPlQFGVVITNKEGKITKFLEKPGWGEVFSDTINT-------------------GIYVLEPEVL-----DMIPEGEnr 189
Cdd:PLN02241 162 SRAS-DFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTtvlglspeeakekpyiasmGIYVFKKDVLlkllrWRFPTAN-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 190 DWSKDVFPQMLDNDDALYGCHLEGYWADIGNTDSYLESCEDIAEGRVEINLM--EKPV-TPARqdvrlFLG----EEASY 262
Cdd:PLN02241 239 DFGSEIIPGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSFYdpDAPIyTSPR-----FLPpskiEDCRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 263 VDdentSLKGMvvlGAntqVVGKARLSNCVVGRNCIIEDGVELRNAILWDNIY-------------------VKKNSTIH 323
Cdd:PLN02241 314 TD----SIISH---GC---FLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYyeteeeiasllaegkvpigIGENTKIR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 324 GAVLCDNVRVGQKVVI------------EEG-------AVVAEETTIGDEALI 357
Cdd:PLN02241 384 NAIIDKNARIGKNVVIinkdgvqeadreEEGyyirsgiVVILKNAVIPDGTVI 436
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-218 |
1.25e-12 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 67.57 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPL---YnRPI------MLHiiellkkHGIDELVLLLYHQPMVI-------KNFFGD 66
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrY-RLIdfplsnMVN-------SGIRNVGVLTQYKSRSLndhlgsgKEWDLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 67 GSEFGVRI--TYVTPLED--FGTAGAVKmaaKHLD-------ERFMIISGDLLTDFDLSQAIAFHEEHKAKATltltsvk 135
Cdd:cd02508 73 RKNGGLFIlpPQQRKGGDwyRGTADAIY---QNLDyiersdpEYVLILSGDHIYNMDYREMLDFHIESGADIT------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 136 dplqfgvVITnkegkitkflekpgwgevfsdTINTGIYVLEPEVL-DMIPEGENR---DWSKDVFPQMLDNDDAlYGCHL 211
Cdd:cd02508 143 -------VVY---------------------KASMGIYIFSKDLLiELLEEDAADgshDFGKDIIPAMLKKLKI-YAYEF 193
|
....*..
gi 1224025872 212 EGYWADI 218
Cdd:cd02508 194 NGYWADI 200
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-226 |
1.27e-12 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 69.29 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVlllyhqpMV-------IKNFFGDGSEF---- 70
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEII-------FVtgrgkraIEDHFDRSYELeatl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 71 -----------------GVRITYVT---PLedfGTAGAVKMAAKHL-DERFMIISGDLLTDFD---LSQAIAFHEEHKAk 126
Cdd:COG1210 78 eakgkeelleevrsispLANIHYVRqkePL---GLGHAVLCARPFVgDEPFAVLLGDDLIDSEkpcLKQMIEVYEETGG- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 127 ATLTLTSV--KDPLQFGVVITNKEG----KITKFLEKPGWGEVFSDTINTGIYVLEPEVLDMIPEGEnrdwskdvfP--- 197
Cdd:COG1210 154 SVIAVQEVppEEVSKYGIVDGEEIEggvyRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTK---------Pgag 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1224025872 198 ---------QMLDNDDALYGCHLEGYWADIGNTDSYLE 226
Cdd:COG1210 225 geiqltdaiAALAKEEPVYAYEFEGKRYDCGDKLGYLK 262
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
3-180 |
2.54e-11 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 64.17 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFF----GDGSEFGVRITYVT 78
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIekskWSKPKSSLMIVIII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 79 PLEDFGTAGAvkmAAKHLDER------FMIISGDLLTDFDLSQAIAFHEEHKAK-----ATLTLTSVKDPL-------QF 140
Cdd:cd04197 83 MSEDCRSLGD---ALRDLDAKglirgdFILVSGDVVSNIDLKEILEEHKERRKKdknaiMTMVLKEASPPHrtrrtgeEF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224025872 141 GVVITNKEGKITKFLEKPG---------WGEVFS---------DTINTGIYVLEPEVL 180
Cdd:cd04197 160 VIAVDPKTSRLLHYEELPGskyrsitdlPSELLGsnseveirhDLLDCHIDICSPDVL 217
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-193 |
1.51e-10 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 62.98 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEF---------- 70
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 71 ------------GVRITYVTPLEDFGTAGAVKMAAKHL-DERFMIISGDLLTD--------FDLSQAIAFHEE------- 122
Cdd:PRK10122 84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIgDNPFVVVLPDVVIDdasadplrYNLAAMIARFNEtgrsqvl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224025872 123 -HKAKATLTLTSV---KDPLQFgvviTNKEGKITKFLEKPGWGEVF-SDTINTGIYVLEPEVLDMIPEGENRDWSK 193
Cdd:PRK10122 164 aKRMPGDLSEYSViqtKEPLDR----EGKVSRIVEFIEKPDQPQTLdSDLMAVGRYVLSADIWPELERTEPGAWGR 235
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
390-744 |
1.88e-10 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 64.20 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 390 FEGATVRGLTNVELTPEFAAKLGAAYGSILPKDSFVLSGrDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYKLT 469
Cdd:PRK15414 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGG-DVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 470 TFGESGGIHFRQSpDDPMATDILFYDAEGIE-ISSATA-KNIERIFFKENFRRVHYTDPGGISEIpRIYDYYHEgflHAL 547
Cdd:PRK15414 86 HLGVDGGIEVTAS-HNPMDYNGMKLVREGARpISGDTGlRDVQRLAEANDFPPVDETKRGRYQQI-NLRDAYVD---HLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 548 DRKAIAKAAP-KVVVDLNHSSAGEVLPAL---LNELGCEVIELnsQVTENCTGKGPEQDAKSM-----DQLSRIVVTLGA 618
Cdd:PRK15414 161 GYINVKNLTPlKLVINSGNGAAGPVVDAIearFKALGAPVELI--KVHNTPDGNFPNGIPNPLlpecrDDTRNAVIKHGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 619 KAGFWMGPSGERLLLVDECGQAFSNIEALTTLA-ALVCKAEREGSLVVPVSAPSAIEQLAAEAGMQVKrTKTDPRSIIES 697
Cdd:PRK15414 239 DMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAeAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVM-SKTGHAFIKER 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1224025872 698 AKERQVRFAASMDGRFAFPSFQYNFDALHTVAKILELLVRTGLTLGQ 744
Cdd:PRK15414 318 MRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGE 364
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-173 |
3.91e-09 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 58.03 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 4 VIMAGGfGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLK-----------------KHGIDELVLLLYHqpmviknffgd 66
Cdd:cd04183 3 IPMAGL-GSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAkifdsrfificrdehntKFHLDESLKLLAP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 67 gsefGVRItYVTPLEDFGTAGAVKMAAKHL--DERFMIISGDLLTDFDLSQAIAFH-EEHKAKATLTLTSVKDPLQFgvV 143
Cdd:cd04183 71 ----NATV-VELDGETLGAACTVLLAADLIdnDDPLLIFNCDQIVESDLLAFLAAFrERDLDGGVLTFFSSHPRWSY--V 143
|
170 180 190
....*....|....*....|....*....|
gi 1224025872 144 ITNKEGKITKFLEKpgwgEVFSDTINTGIY 173
Cdd:cd04183 144 KLDENGRVIETAEK----EPISDLATAGLY 169
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
263-359 |
1.53e-08 |
|
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 55.50 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 263 VDDENTSLKGMVVLGANTQVVGKARLS-NCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEE 341
Cdd:cd03353 5 IDPETTYIDGDVEIGVDVVIDPGVILEgKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRP 84
|
90
....*....|....*...
gi 1224025872 342 GAVVAEETTIGDEALIKK 359
Cdd:cd03353 85 GTVLGEGVHIGNFVEIKK 102
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
282-363 |
3.02e-08 |
|
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.
Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 52.08 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 282 VVGKARLSNCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVV--AEETTIGDE-ALIK 358
Cdd:cd04651 20 IISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDPEEdrARFYVTEDGiVVVG 99
|
....*
gi 1224025872 359 KDVKI 363
Cdd:cd04651 100 KGMVI 104
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-180 |
2.26e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 54.17 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQ-----PMViknffgdgSEFGVRITYV 77
Cdd:PRK14352 7 VIVLAAGAGTRMRS---DTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDrervaPAV--------AELAPEVDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 78 TPLEDFGTAGAVKMAAKHLDERF----MIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKI 151
Cdd:PRK14352 76 VQDEQPGTGHAVQCALEALPADFdgtvVVTAGDvpLLDGETLADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDGEV 155
|
170 180 190
....*....|....*....|....*....|.
gi 1224025872 152 TKFLE-KPGWGEVFS-DTINTGIYVLEPEVL 180
Cdd:PRK14352 156 TAIVEqKDATPSQRAiREVNSGVYAFDAAVL 186
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
259-372 |
4.46e-07 |
|
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.
Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 50.10 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 259 EASYVDdENTSLKGMVVLGANT----QVVGKARLSNCVVGRNCIIEDGVELRNA-----ILWDNIYVKKNSTIHGAVLCD 329
Cdd:cd04645 4 PSAFIA-PNATVIGDVTLGEGSsvwfGAVLRGDVNPIRIGERTNIQDGSVLHVDpgyptIIGDNVTVGHGAVLHGCTIGD 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1224025872 330 NVRVGQKVVIEEGAVVAEETTIGDEALIKkdvkiwPRKVIEGG 372
Cdd:cd04645 83 NCLIGMGAIILDGAVIGKGSIVAAGSLVP------PGKVIPPG 119
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-227 |
9.62e-07 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 51.45 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 2 KAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIKNFFGDGSEF----------- 70
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 71 -----------GVRITYVTPLEDFGTAGAVkMAAKHL--DERFMIISGDLLTD---FDLSQ----AIAFHEEHKAKATLT 130
Cdd:PRK13389 90 lldevqsicppHVTIMQVRQGLAKGLGHAV-LCAHPVvgDEPVAVILPDVILDeyeSDLSQdnlaEMIRRFDETGHSQIM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 131 LTSVKDPLQFGVV----ITNKEGK---ITKFLEKPGWGEVFSDTINTGIYVLEPEVLDMI---PEGENRDWSKDVFPQML 200
Cdd:PRK13389 169 VEPVADVTAYGVVdckgVELAPGEsvpMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLaktPPGAGDEIQLTDAIDML 248
|
250 260
....*....|....*....|....*..
gi 1224025872 201 DNDDALYGCHLEGYWADIGNTDSYLES 227
Cdd:PRK13389 249 IEKETVEAYHMKGKSHDCGNKLGYMQA 275
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
661-753 |
1.23e-06 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 47.83 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 661 GSLVVPVSAPSAIEQLAAEAGMQVKRTKTDPRSIIESAKERQVRFAASMDGRFAFPSFQYNFDALHTVAKILELLVRTGL 740
Cdd:pfam02880 23 AGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHATTKDGILAALLVLEILARTGK 102
|
90
....*....|...
gi 1224025872 741 TLGQTRQMLPRRF 753
Cdd:pfam02880 103 SLSELLEELPEKY 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
395-667 |
4.72e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 49.75 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 395 VRGLTNVE-LTPEFAAKLGAAYGSIL-----PKdsfVLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYkL 468
Cdd:PRK10887 9 IRGKVGQApITPDFVLKLGWAAGKVLarqgrPK---VLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPAVAY-L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 469 T-TFGESGGIHFRQS----PDDpmatDILFYDAEGIEISSATAKNIERIFFKEnfrrVHYTDPGGISEIPRIYD---YYH 540
Cdd:PRK10887 85 TrTLRAEAGIVISAShnpyYDN----GIKFFSADGTKLPDEVELAIEAELDKP----LTCVESAELGKASRINDaagRYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 541 E----GFLHALDRKAIakaapKVVVDLNHSSAGEVLPALLNELGCEVIELNSQ-----VTENCtGkgpeqdAKSMDQLSR 611
Cdd:PRK10887 157 EfcksTFPNELSLRGL-----KIVVDCANGATYHIAPNVFRELGAEVIAIGCEpnglnINDEC-G------ATDPEALQA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224025872 612 IVVTLGAKAGFWMGPSGERLLLVDECGQAFSNIEAlttLAALVCKAEREGSLVVPV 667
Cdd:PRK10887 225 AVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQL---LYIIARDRLRRGQLRGGV 277
|
|
| LbH_paaY_like |
cd04745 |
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
258-371 |
4.82e-06 |
|
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.
Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 47.36 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 258 EEASYVDdENTSLKGMVVLGANTQV---------VGKARLSN-CVVGRNCIIEdGVELRNAILWDNIYVKKNSTIHGAVL 327
Cdd:cd04745 4 DPSSFVH-PTAVLIGDVIIGKNCYIgphaslrgdFGRIVIRDgANVQDNCVIH-GFPGQDTVLEENGHIGHGAILHGCTI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1224025872 328 CDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVIEG 371
Cdd:cd04745 82 GRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAG 125
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
1-353 |
5.36e-06 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 49.98 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPLtidLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLLYHQPMVIknffgDGSEFGVRITYVTPL 80
Cdd:PRK14358 8 LDVVILAAGQGTRMKSA---LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQV-----EAALQGSGVAFARQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 81 EDFGTAGAVKMAAKHL---DERFMIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGVVITNKEGKITKFL 155
Cdd:PRK14358 80 QQLGTGDAFLSGASALtegDADILVLYGDtpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 156 EKPGW--GEVFSDTINTGIYVLE---PEVLDMI----PEGE---------NRDWSKDVFPQMLDNDDALYGchlegywad 217
Cdd:PRK14358 160 EQKDAtdAEKAIGEFNSGVYVFDaraPELARRIgndnKAGEyyltdllglYRAGGAQVRAFKLSDPDEVLG--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 218 iGNTDSYLESCEDIAEGRVEINLMEKPVTpaRQDVRLFLGEEASYVDDENTSLKGmVVLGANTQVVGKArlsncVVGRNC 297
Cdd:PRK14358 231 -ANDRAGLAQLEATLRRRINEAHMKAGVT--LQDPGTILIEDTVTLGRDVTIEPG-VLLRGQTRVADGV-----TIGAYS 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224025872 298 IIEDGVelrnaiLWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGD 353
Cdd:PRK14358 302 VVTDSV------LHEGAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGN 351
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
274-346 |
5.51e-06 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 44.93 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 274 VVLGANTQVVGKARL-SNCVVGRNCIIEDGVELRNA---------ILWDNIYVKKNSTIHGavlcdNVRVGQKVVIEEGA 343
Cdd:cd00208 1 VFIGEGVKIHPKAVIrGPVVIGDNVNIGPGAVIGAAtgpneknptIIGDNVEIGANAVIHG-----GVKIGDNAVIGAGA 75
|
...
gi 1224025872 344 VVA 346
Cdd:cd00208 76 VVT 78
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
395-660 |
5.81e-06 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 49.59 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 395 VRGLTNVELTPEFAAKLGAAYGSILPKD--SFVLSGRDSIRSSRMLKRSFAGGLLSAGINVRDTKMISLPVLRYKLTTFG 472
Cdd:PRK09542 6 VRGVVGEQIDEDLVRDVGAAFARLMRAEgaTTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 473 ESGGIhFRQSpDDPMAtdilfYDaeGIEISSATAKNIERIFFKENFRRV-------HYTDPGGISEIPRIYDYyhEGFLH 545
Cdd:PRK09542 86 CPGAM-FTAS-HNPAA-----YN--GIKLCRAGAKPVGQDTGLAAIRDDliagvpaYDGPPGTVTERDVLADY--AAFLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 546 AL-DRKAIakaAP-KVVVDLNHSSAGEVLPALLNELGCEVI----ELNsqvtenctGKGPEQDAKSMD-----QLSRIVV 614
Cdd:PRK09542 155 SLvDLSGI---RPlKVAVDAGNGMGGHTVPAVLGGLPITLLplyfELD--------GTFPNHEANPLDpanlvDLQAFVR 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1224025872 615 TLGAKAGFWMGPSGERLLLVDECGQAFSNiealTTLAALVckAERE 660
Cdd:PRK09542 224 ETGADIGLAFDGDADRCFVVDERGQPVSP----SAVTALV--AARE 263
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
274-397 |
7.06e-06 |
|
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.
Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 47.48 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 274 VVLGANTQVvgkarLSNCVVGRNCIIEDGVelrnaILWDNIYVKKNSTIH-------GAVLCDNVRVGQKVVIEEGAVVA 346
Cdd:cd03360 97 AVIGEGCVI-----MAGAVINPDARIGDNV-----IINTGAVIGHDCVIGdfvhiapGVVLSGGVTIGEGAFIGAGATII 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 347 EETTIGDEAlikkdvkiwprkVIEGGATVTtnliwgekwrKSIFEGATVRG 397
Cdd:cd03360 167 QGVTIGAGA------------IIGAGAVVT----------KDVPDGSVVVG 195
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
290-345 |
1.76e-05 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 47.70 E-value: 1.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224025872 290 NCVVGRNCIIEDGVELR-NAILWDNIYVKKNSTIH-GAVLCDNVRVGQKVVIEEGAVV 345
Cdd:COG1044 120 FAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHpNVTIYERCVIGDRVIIHSGAVI 177
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-156 |
2.00e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 47.93 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLllyhqpmVIknffGDGSE--------FGVRI 74
Cdd:PRK14353 8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAV-------VV----GPGAEavaaaaakIAPDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 75 TYVTPLEDFGTAGAVKMAAKHLdERF----MIISGD--LLTDFDLSQAIAFHEEHKAKATLTLTSvKDPLQFGVVITnKE 148
Cdd:PRK14353 74 EIFVQKERLGTAHAVLAAREAL-AGGygdvLVLYGDtpLITAETLARLRERLADGADVVVLGFRA-ADPTGYGRLIV-KG 150
|
....*...
gi 1224025872 149 GKITKFLE 156
Cdd:PRK14353 151 GRLVAIVE 158
|
|
| LicC |
COG4750 |
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
1-48 |
2.27e-05 |
|
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 46.36 E-value: 2.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1224025872 1 MKAVIMAGGFGTRIHPLTIDLPKPMIPLYNRPIMLHIIELLKKHGIDE 48
Cdd:COG4750 1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITD 48
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
3-51 |
3.83e-05 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 45.59 E-value: 3.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHG-IDELVL 51
Cdd:cd02516 3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
|
|
| LbH_Dynactin_6 |
cd04646 |
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ... |
266-370 |
5.70e-05 |
|
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100052 [Multi-domain] Cd Length: 164 Bit Score: 44.24 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 266 ENTSLKGMVVLGANTQVVGKARL----SNCVVGRNCIIEDGVELRNAILwDNIYVKKNSTI------HGAVLCDNVRVGQ 335
Cdd:cd04646 10 QESEIRGDVTIGPGTVVHPRATIiaeaGPIIIGENNIIEEQVTIVNKKP-KDPAEPKPMIIgsnnvfEVGCKCEALKIGN 88
|
90 100 110
....*....|....*....|....*....|....*
gi 1224025872 336 KVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVIE 370
Cdd:cd04646 89 NNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILP 123
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
290-357 |
5.79e-05 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 46.29 E-value: 5.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224025872 290 NCVVGRNCIIEDGVELRNailwdniyvkkNSTIH-GAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALI 357
Cdd:PRK00892 118 GVSIGPNAVIGAGVVIGD-----------GVVIGaGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
290-357 |
1.70e-04 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 44.62 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224025872 290 NCVVGRNCIIEDGVELRNailwdniyvkkNSTIH-GAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALI 357
Cdd:COG1044 114 GVSIGPFAVIGAGVVIGD-----------GVVIGpGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVII 171
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
316-369 |
1.98e-04 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 43.55 E-value: 1.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1224025872 316 VKKNSTIH-GAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVI 369
Cdd:cd03352 4 IGENVSIGpNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII 58
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
289-378 |
1.99e-04 |
|
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.
Pssm-ID: 100048 [Multi-domain] Cd Length: 119 Bit Score: 41.72 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 289 SNCVVGRNCIIEDGVelrnaILWDNIYVKKNSTI-HGAVLCDNVRVG---------------------QKVVIEEGAvva 346
Cdd:cd03358 3 DNCIIGTNVFIENDV-----KIGDNVKIQSNVSIyEGVTIEDDVFIGpnvvftndlyprskiyrkwelKGTTVKRGA--- 74
|
90 100 110
....*....|....*....|....*....|..
gi 1224025872 347 eetTIGDEALIKKDVKIWPRKVIEGGATVTTN 378
Cdd:cd03358 75 ---SIGANATILPGVTIGEYALVGAGAVVTKD 103
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-142 |
2.20e-04 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 42.95 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 6 MAGGFGTRIhpltiDLP-KPMIPLYNRPIMLHIIELLKKHGIDE-LVLLLYHQPMViKNFFgdgSEFGVRItYVTPLEDF 83
Cdd:COG2266 1 MAGGKGTRL-----GGGeKPLLEICGKPMIDRVIDALEESCIDKiYVAVSPNTPKT-REYL---KERGVEV-IETPGEGY 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 84 gtAGAVKMAAKHLDERFMIISGDL--LTDFDLSQAIAFHEEHKAKATLTLTSVKDPLQFGV 142
Cdd:COG2266 71 --VEDLNEALESISGPVLVVPADLplLTPEIIDDIIDAYLESGKPSLTVVVPAALKRELGV 129
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
259-371 |
2.73e-04 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 42.32 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 259 EASYVDDeNTSLKGMVVLGANTQVvgkarLSNCV---------VGRNCIIEDGVELR-----NAILWDNIYVKKNSTIHG 324
Cdd:COG0663 15 PSAFVAP-TAVVIGDVTIGEDVSV-----WPGAVlrgdvgpirIGEGSNIQDGVVLHvdpgyPLTIGDDVTIGHGAILHG 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1224025872 325 AVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVIEG 371
Cdd:COG0663 89 CTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVG 135
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-127 |
5.79e-04 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 41.68 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRihpltIDLPKPMIPLYNRPIMLHIIELLKKHGIDELVLLL-YHQPMVIKNFfgdgSEFGVRITYVTPLE 81
Cdd:COG2068 6 AIILAAGASSR-----MGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgADAEEVAAAL----AGLGVRVVVNPDWE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 82 DfGTAGAVKMAAKHLDER---FMIISGD--LLTDFDLSQAIAFHEEHKAKA 127
Cdd:COG2068 77 E-GMSSSLRAGLAALPADadaVLVLLGDqpLVTAETLRRLLAAFRESPASI 126
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
265-363 |
6.04e-04 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 42.01 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 265 DENTSLKGMVVLGANTQVVGKARL-SNCVVGRNCIIEDGVELR-NAILWDNIYVKKNSTIH-GAVL-CD----------- 329
Cdd:cd03352 5 GENVSIGPNAVIGEGVVIGDGVVIgPGVVIGDGVVIGDDCVIHpNVTIYEGCIIGDRVIIHsGAVIgSDgfgfapdgggw 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1224025872 330 -------NVRVGQKVVIeeGAvvaeETTI----GDEALIKKDVKI 363
Cdd:cd03352 85 vkipqlgGVIIGDDVEI--GA----NTTIdrgaLGDTVIGDGTKI 123
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-107 |
1.40e-03 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 40.26 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltidlPKPMIPLYNRPIMLHIIELLKKHGiDELVLLLYHQPmvIKNFFgdgSEFGVRITYvTPLED 82
Cdd:pfam12804 1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEE--VLAAL---AGLGVPVVP-DPDPG 68
|
90 100
....*....|....*....|....*..
gi 1224025872 83 FGTAGAVKMAAKHLD--ERFMIISGDL 107
Cdd:pfam12804 69 QGPLAGLLAALRAAPgaDAVLVLACDM 95
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
320-375 |
1.93e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 41.16 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 320 STIH-GAVLCDNVRVGQKVVIEEGAVVAEETTI------GDEALIKKDVKIWPRKVIEGGATV 375
Cdd:COG1044 103 AVIDpSAKIGEGVSIGPFAVIGAGVVIGDGVVIgpgvviGDGVVIGDDCVLHPNVTIYERCVI 165
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
291-376 |
2.01e-03 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 37.61 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 291 CVVGRNCIIEDgvelrNAILWDNIYVKKNSTIHGAVL---CDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVkiwprk 367
Cdd:cd00208 1 VFIGEGVKIHP-----KAVIRGPVVIGDNVNIGPGAVigaATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNA------ 69
|
....*....
gi 1224025872 368 VIEGGATVT 376
Cdd:cd00208 70 VIGAGAVVT 78
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
292-369 |
2.06e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 41.28 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224025872 292 VVGRNCIIEDGVelrnailwdniyvkknsTI-HGAVLCDNVRVGQKVVIEEGAVVAEETTIGDealikkDVKIWPRKVI 369
Cdd:PRK00892 108 VIDPSAKIGEGV-----------------SIgPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGA------DCRLHANVTI 163
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-51 |
2.27e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 40.50 E-value: 2.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1224025872 4 VIMAGGFGTRIHPltiDLPKPMIPLYNRPIMLHIIELLKKHG-IDELVL 51
Cdd:COG1211 1 IIPAAGSGSRMGA---GIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVV 46
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-100 |
3.08e-03 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 40.25 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 1 MKAVIMAGGFGTRIHPL-TIDLPKPMIPLYNRPIMLHI-IELLKKHGIDELVLLLY---HQPMVIKNFFGDGSEFGVrit 75
Cdd:cd02509 1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGDKSLLQQtLDRLKGLVPPDRILVVTneeYRFLVREQLPEGLPEENI--- 77
|
90 100
....*....|....*....|....*..
gi 1224025872 76 yvtPLEDFG--TAGAVKMAAKHLDERF 100
Cdd:cd02509 78 ---ILEPEGrnTAPAIALAALYLAKRD 101
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
274-345 |
4.81e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 40.12 E-value: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 274 VVLGANTqVVGkarlSNCVVGRNCIIEDGvelrnAILWDNIYVKKNSTIH-GAVLCDNVRVGQKVVIEEGAVV 345
Cdd:PRK00892 119 VSIGPNA-VIG----AGVVIGDGVVIGAG-----AVIGDGVKIGADCRLHaNVTIYHAVRIGNRVIIHSGAVI 181
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
229-358 |
5.15e-03 |
|
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 38.72 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 229 EDIAEGRVEINLMEKPvtparqdvRLFLGEEAsyVDDENTSLKGMVVLGANTQVVGKARL-SNCVVGRNCIIEDGVELRN 307
Cdd:cd05636 1 KDEIEGTVEEGVTIKG--------PVWIGEGA--IVRSGAYIEGPVIIGKGCEIGPNAYIrGYTVLGDGCVVGNSVEVKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 308 AILWDNI------YV-----------------------KKNSTIH-------------GAVLCDNVRVGQKVVIEEGAVV 345
Cdd:cd05636 71 SIIMDGTkvphlnYVgdsvlgenvnlgagtitanlrfdDKPVKVRlkgervdtgrrklGAIIGDGVKTGINVSLNPGVKI 150
|
170
....*....|...
gi 1224025872 346 AEETTIGDEALIK 358
Cdd:cd05636 151 GPGSWVYPGCVVR 163
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
322-383 |
5.20e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 40.12 E-value: 5.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224025872 322 IH-GAVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVIEGGATVTTNLIWGE 383
Cdd:PRK00892 109 IDpSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGN 171
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
325-375 |
5.63e-03 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 38.93 E-value: 5.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1224025872 325 AVLCDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVIEGGATV 375
Cdd:cd03352 2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
|
|
| LbH_M1P_guanylylT_C |
cd05824 |
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
290-353 |
7.38e-03 |
|
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100062 [Multi-domain] Cd Length: 80 Bit Score: 36.36 E-value: 7.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224025872 290 NCVVGRNCIIEDGVELRNAILWDNIYVKKNSTIHGAVLCDNVRVGQKVVIEEGAVVAEETTIGD 353
Cdd:cd05824 17 NVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
290-375 |
9.14e-03 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 38.54 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 290 NCVVGRNCIIEDGVelrnailwdniYVKKNSTIHgavlcDNVRVGQKVVIEEGAVVAEETTIGDEALIKKDVKIWPRKVI 369
Cdd:cd03352 1 SAKIGENVSIGPNA-----------VIGEGVVIG-----DGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVII 64
|
....*.
gi 1224025872 370 EGGATV 375
Cdd:cd03352 65 HSGAVI 70
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-126 |
9.91e-03 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 37.92 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224025872 3 AVIMAGGFGTRIHPltidlPKPMIPLYNRPIMLHIIELLKKHGIDELVLLL-YHQPMVIKNFfgdgSEFGVRITYVtPLE 81
Cdd:cd04182 3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgAEADAVRAAL----AGLPVVVVIN-PDW 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1224025872 82 DFGTAGAVKMAAKHLDER---FMIISGD--LLTDFDLSQAIAFHEEHKAK 126
Cdd:cd04182 73 EEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAG 122
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