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Conserved domains on  [gi|1566446403|gb|QAZ79848|]
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UDP-N-acetyl-D-mannosamine dehydrogenase (plasmid) [Escherichia coli]

Protein Classification

nucleotide sugar dehydrogenase( domain architecture ID 11485179)

nucleotide sugar dehydrogenase catalyzes the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 1-417 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


:

Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 799.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   1 MSFKTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEPADAFL 80
Cdd:PRK11064    1 MSFETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  81 IAVPTPFLPCskneiPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQDAGDKSDINIA 160
Cdd:PRK11064   81 IAVPTPFKGD-----HEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFPQQAGEQADINIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:PRK11064  156 YCPERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICAD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTPNEAKIIHTARIVNDSKPDWVISKVKQALADFLLVNk 320
Cdd:PRK11064  236 QGINVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAAT- 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 321 NKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFHPGRVIAVEPNIHTVPPKLN-NIELVDLNFAMQHADIHLLLV 399
Cdd:PRK11064  315 DKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLDgLVTLVSLDEALATADVLVMLV 394

                         410       420
                  ....*....|....*....|.
gi 1566446403 400 DHKEFK---GKSVNNGIVIDT 417
Cdd:PRK11064  395 DHSQFKainGDNVHQQWVVDT 415
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 1-417 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 799.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   1 MSFKTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEPADAFL 80
Cdd:PRK11064    1 MSFETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  81 IAVPTPFLPCskneiPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQDAGDKSDINIA 160
Cdd:PRK11064   81 IAVPTPFKGD-----HEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFPQQAGEQADINIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:PRK11064  156 YCPERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICAD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTPNEAKIIHTARIVNDSKPDWVISKVKQALADFLLVNk 320
Cdd:PRK11064  236 QGINVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAAT- 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 321 NKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFHPGRVIAVEPNIHTVPPKLN-NIELVDLNFAMQHADIHLLLV 399
Cdd:PRK11064  315 DKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLDgLVTLVSLDEALATADVLVMLV 394

                         410       420
                  ....*....|....*....|.
gi 1566446403 400 DHKEFK---GKSVNNGIVIDT 417
Cdd:PRK11064  395 DHSQFKainGDNVHQQWVVDT 415
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
5-421 0e+00

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 522.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   5 TISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPElDVVVQTAVEEGYLKAVIKPEP---ADAFLI 81
Cdd:COG0677     1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEAlaeADVVII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  82 AVPTPFlpcskNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQDagdksdINIAY 161
Cdd:COG0677    80 AVPTPL-----DEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGED------FFLAY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 162 CPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVE-GDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:COG0677   149 SPERINPGNKLHELRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTP---NEAKIIHTARIVNDSKPDWVISKVKQALADfll 317
Cdd:COG0677   229 LGIDVWEVIEAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARelgYHPRLILAAREINDSMPEYVVERVVKALNE--- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 318 vnKNKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFHpGRVIAVEPNIHTVPPKLNNIELVDLNFAMQHADIHLL 397
Cdd:COG0677   306 --AGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYG-AEVDVHDPYVDEEEVEGEYGELVDLEEALEGADAVVL 382

                         410       420       430
                  ....*....|....*....|....*....|
gi 1566446403 398 LVDHKEFKGKSV------NNGIVIDTKGIW 421
Cdd:COG0677   383 AVDHDEFDELDPeelrlkGAKVVVDTRGVL 412
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 4-419 3.05e-126

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 370.79  E-value: 3.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   4 KTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEP----ADAF 79
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEairdADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  80 LIAVPTPFlpcskNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKElrpdlsfpqDAGDK--SDI 157
Cdd:TIGR03026  81 IICVPTPL-----KEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILE---------RSGLKlgEDF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 158 NIAYCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMI 237
Cdd:TIGR03026 147 YLAYNPEFLREGNAVHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 238 CSELDINVWELISLSNRHPR--VNILQPGPGVGGHCIAVDPWFIVSKTPN---EAKIIHTARIVNDSKPDWVISKVKQAL 312
Cdd:TIGR03026 227 CEALGIDVYEVIEAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDLL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 313 adfllvnknKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFhpG-RVIAVEPNIhtVPPKLNNIELV-DLNFAMQ 390
Cdd:TIGR03026 307 ---------GPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEK--GaKVKAYDPLV--PEEEVKGLPSIdDLEEALK 373

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1566446403 391 HADIHLLLVDHKEFK-------GKSVNNGIVIDTKG 419
Cdd:TIGR03026 374 GADALVILTDHSEFKdldlekiKDLMKGKVVVDTRN 409
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
6-420 4.00e-108

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 325.18  E-value: 4.00e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   6 ISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEP---ADAFLIA 82
Cdd:NF040825    3 IAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFIIC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  83 VPTPFLPCSkneipaPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELrpdlsfpqdAGDKS--DINIA 160
Cdd:NF040825   83 VQTPLKEDK------PDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEEL---------TGLKEgeDFYMA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:NF040825  148 HAPERVMPGRIFKELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQ 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTPNEAKIIHTARIVNDSKPDWVISKVKQALADFllvnk 320
Cdd:NF040825  228 YGVNVFEAIELANTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEEA----- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 321 NKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISefhpGRVIAVEpnihTVPPKLNNIElVDLNFAMQHADIHLLLVD 400
Cdd:NF040825  303 NVPPEEAVVTVLGLAYKGDTDDTRNSPALKFVELIE----DDVKEVR----TYDPYVGGTH-ESLEDAVKGADAIVIATD 373

                         410       420
                  ....*....|....*....|....*..
gi 1566446403 401 HKEFK-------GKSVNNGIVIDTKGI 420
Cdd:NF040825  374 HSEFKslnweelGKLMRTKILIDGRHI 400
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 4-195 7.34e-62

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 198.24  E-value: 7.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   4 KTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVE---EGYLKAVIKPEPADAFL 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  81 IAVPTPFLPCSKneipAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFpqdagdkSDINIA 160
Cdd:pfam03721  81 IAVGTPSKKGGG----AADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVG-------VDFDVA 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVE 195
Cdd:pfam03721 150 SNPEFLREGSAVYDLFNPDRVVIGVTEKCAEAALE 184
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 330-421 5.12e-18

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 78.70  E-value: 5.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  330 ACYGLAFKADIDDLRESPAMQVTKAISEFHpGRVIAVEPNIHTVPPKLNNIELVDLNFAMQHADIHLLLVDHKEFKG--- 406
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAMEEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSldp 79

                           90
                   ....*....|....*....
gi 1566446403  407 ----KSVNNGIVIDTKGIW 421
Cdd:smart00984  80 eelkDLMKKPVVVDGRNIL 98
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 1-417 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 799.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   1 MSFKTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEPADAFL 80
Cdd:PRK11064    1 MSFETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  81 IAVPTPFLPCskneiPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQDAGDKSDINIA 160
Cdd:PRK11064   81 IAVPTPFKGD-----HEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFPQQAGEQADINIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:PRK11064  156 YCPERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICAD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTPNEAKIIHTARIVNDSKPDWVISKVKQALADFLLVNk 320
Cdd:PRK11064  236 QGINVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAAT- 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 321 NKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFHPGRVIAVEPNIHTVPPKLN-NIELVDLNFAMQHADIHLLLV 399
Cdd:PRK11064  315 DKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLDgLVTLVSLDEALATADVLVMLV 394

                         410       420
                  ....*....|....*....|.
gi 1566446403 400 DHKEFK---GKSVNNGIVIDT 417
Cdd:PRK11064  395 DHSQFKainGDNVHQQWVVDT 415
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
5-421 0e+00

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 522.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   5 TISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPElDVVVQTAVEEGYLKAVIKPEP---ADAFLI 81
Cdd:COG0677     1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEAlaeADVVII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  82 AVPTPFlpcskNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQDagdksdINIAY 161
Cdd:COG0677    80 AVPTPL-----DEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGED------FFLAY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 162 CPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVE-GDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:COG0677   149 SPERINPGNKLHELRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTP---NEAKIIHTARIVNDSKPDWVISKVKQALADfll 317
Cdd:COG0677   229 LGIDVWEVIEAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARelgYHPRLILAAREINDSMPEYVVERVVKALNE--- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 318 vnKNKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFHpGRVIAVEPNIHTVPPKLNNIELVDLNFAMQHADIHLL 397
Cdd:COG0677   306 --AGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYG-AEVDVHDPYVDEEEVEGEYGELVDLEEALEGADAVVL 382

                         410       420       430
                  ....*....|....*....|....*....|
gi 1566446403 398 LVDHKEFKGKSV------NNGIVIDTKGIW 421
Cdd:COG0677   383 AVDHDEFDELDPeelrlkGAKVVVDTRGVL 412
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 4-419 3.05e-126

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 370.79  E-value: 3.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   4 KTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEP----ADAF 79
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEairdADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  80 LIAVPTPFlpcskNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKElrpdlsfpqDAGDK--SDI 157
Cdd:TIGR03026  81 IICVPTPL-----KEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILE---------RSGLKlgEDF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 158 NIAYCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMI 237
Cdd:TIGR03026 147 YLAYNPEFLREGNAVHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 238 CSELDINVWELISLSNRHPR--VNILQPGPGVGGHCIAVDPWFIVSKTPN---EAKIIHTARIVNDSKPDWVISKVKQAL 312
Cdd:TIGR03026 227 CEALGIDVYEVIEAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDLL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 313 adfllvnknKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFhpG-RVIAVEPNIhtVPPKLNNIELV-DLNFAMQ 390
Cdd:TIGR03026 307 ---------GPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEK--GaKVKAYDPLV--PEEEVKGLPSIdDLEEALK 373

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1566446403 391 HADIHLLLVDHKEFK-------GKSVNNGIVIDTKG 419
Cdd:TIGR03026 374 GADALVILTDHSEFKdldlekiKDLMKGKVVVDTRN 409
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
6-420 4.00e-108

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 325.18  E-value: 4.00e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   6 ISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYLKAVIKPEP---ADAFLIA 82
Cdd:NF040825    3 IAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFIIC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  83 VPTPFLPCSkneipaPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELrpdlsfpqdAGDKS--DINIA 160
Cdd:NF040825   83 VQTPLKEDK------PDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEEL---------TGLKEgeDFYMA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVEGDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSE 240
Cdd:NF040825  148 HAPERVMPGRIFKELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQ 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 241 LDINVWELISLSNRHPRVNILQPGPGVGGHCIAVDPWFIVSKTPNEAKIIHTARIVNDSKPDWVISKVKQALADFllvnk 320
Cdd:NF040825  228 YGVNVFEAIELANTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEEA----- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 321 NKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISefhpGRVIAVEpnihTVPPKLNNIElVDLNFAMQHADIHLLLVD 400
Cdd:NF040825  303 NVPPEEAVVTVLGLAYKGDTDDTRNSPALKFVELIE----DDVKEVR----TYDPYVGGTH-ESLEDAVKGADAIVIATD 373

                         410       420
                  ....*....|....*....|....*..
gi 1566446403 401 HKEFK-------GKSVNNGIVIDTKGI 420
Cdd:NF040825  374 HSEFKslnweelGKLMRTKILIDGRHI 400
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-416 1.30e-63

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 210.65  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   6 ISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVEEGYL-------KAVikpEPADA 78
Cdd:COG1004     3 IAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLrfttdlaEAV---AEADV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  79 FLIAVPTPFLPCSkneipAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKElrpdlsfpQDAGDKSDIN 158
Cdd:COG1004    80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAE--------ELRGAGVDFD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 159 IAYCPERVLPGKVVQELVTNDR-VIGGMSERCSLRAVELYKTFVEGDC--VITNTRTAEMAKLTENSFRDVQIAFANELS 235
Cdd:COG1004   147 VVSNPEFLREGSAVEDFLRPDRiVIGVDSERAAEVLRELYAPFVRNGTpiIVTDLRSAELIKYAANAFLATKISFINEIA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 236 MICSELDINVWEL---ISLSNRhprvnI----LQPGPGVGGHCIAVDpwfiVS---KTPNE----AKIIHTARIVNDSKP 301
Cdd:COG1004   227 NLCEKVGADVEEVargIGLDSR-----IgpkfLYAGIGYGGSCFPKD----VRaliATARElgydLRLLEAVEEVNERQK 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 302 DWVISKVKQALADFLlvnKNKkidevTIACYGLAFKADIDDLRESPAMQVTKAISEFHpGRVIAVEP----NIHTVPPkl 377
Cdd:COG1004   298 RRLVEKIREHLGGDL---KGK-----TIAVLGLAFKPNTDDMRESPALDIIEALLEAG-ARVRAYDPvameNARRLLP-- 366

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1566446403 378 NNIELV-DLNFAMQHADIHLLLVDHKEFK-------GKSVNNGIVID 416
Cdd:COG1004   367 DDITYAdDAYEALEGADALVILTEWPEFRaldfarlKALMKGPVIFD 413
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 4-195 7.34e-62

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 198.24  E-value: 7.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   4 KTISVIGLGYIGLPTAAMFASKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTAVE---EGYLKAVIKPEPADAFL 80
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  81 IAVPTPFLPCSKneipAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFpqdagdkSDINIA 160
Cdd:pfam03721  81 IAVGTPSKKGGG----AADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVG-------VDFDVA 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1566446403 161 YCPERVLPGKVVQELVTNDRVIGGMSERCSLRAVE 195
Cdd:pfam03721 150 SNPEFLREGSAVYDLFNPDRVVIGVTEKCAEAALE 184
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
6-405 3.06e-43

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 156.77  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   6 ISVIGLGYIGLPTAAMFAsKKKKVIGVDVNKHAIETINQGkihiVEPELDVVVQTAVEEGYLK---AVIKPEPADAFLIA 82
Cdd:PRK15182    9 IAIIGLGYVGLPLAVEFG-KSRQVVGFDVNKKRILELKNG----VDVNLETTEEELREARYLKftsEIEKIKECNFYIIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  83 VPTPFlpcskNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPQdagdksDINIAYC 162
Cdd:PRK15182   84 VPTPI-----NTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTFNQ------DFYVGYS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 163 PERVLPGKVVQELVTNDRVIGGMSERCSLRAVELYKTFVE-GDCVITNTRTAEMAKLTENSFRDVQIAFANELSMICSEL 241
Cdd:PRK15182  153 PERINPGDKKHRLTNIKKITSGSTAQIAELIDEVYQQIISaGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 242 DINVWELISLSNRhpRVNILQPGPG-VGGHCIAVDPWFIVSKTPN---EAKIIHTARIVNDSKPDWVISKVKQAladflL 317
Cdd:PRK15182  233 NIDTEAVLRAAGS--KWNFLPFRPGlVGGHCIGVDPYYLTHKSQGigyYPEIILAGRRLNDNMGNYVSEQLIKA-----M 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 318 VNKNKKIDEVTIACYGLAFKADIDDLRESPAMQVTKAISEFhPGRVIAVEP--NIHTVPPKLNNIELVDLNFAmqHADIH 395
Cdd:PRK15182  306 IKKGINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKY-SCKVDIFDPwvDAEEVRREYGIIPVSEVKSS--HYDAI 382

                         410
                  ....*....|
gi 1566446403 396 LLLVDHKEFK 405
Cdd:PRK15182  383 IVAVGHQQFK 392
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 212-298 1.29e-32

UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 460015 [Multi-domain]  Cd Length: 92  Bit Score: 118.25  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 212 TAEMAKLTENSFRDVQIAFANELSMICSELDINVWELISLSNRHPR--VNILQPGPGVGGHCIAVDPWFIVSKTPN---E 286
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYLARElgvP 80

                          90
                  ....*....|..
gi 1566446403 287 AKIIHTARIVND 298
Cdd:pfam00984  81 ARLLEAAREVNE 92
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 5-355 3.09e-25

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 107.07  E-value: 3.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   5 TISVIGLGYIGLPTAAMFASK--KKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQ----------TAVEegylKAVIK 72
Cdd:PLN02353    3 KICCIGAGYVGGPTMAVIALKcpDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKqcrgknlffsTDVE----KHVAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  73 pepADAFLIAVPTPFLPCSKNEIPAPDLSFIAEATKAISQILKKGDLVILESTSPVGTTEQMAIWMKELRPDLSFPqdag 152
Cdd:PLN02353   79 ---ADIVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQ---- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 153 dksdinIAYCPERVLPGKVVQELVTNDRV-IGGMSERCSLRAVE----LYKTFVEGDCVIT-NTRTAEMAKLTENSFRDV 226
Cdd:PLN02353  152 ------ILSNPEFLAEGTAIEDLFKPDRVlIGGRETPEGQKAVQalkdVYAHWVPEERIITtNLWSAELSKLAANAFLAQ 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 227 QIAFANELSMICSELDINVWELISLSNRHPRV--NILQPGPGVGGHCIAVDPWFIV-----SKTPNEAKIIHTARIVNDS 299
Cdd:PLN02353  226 RISSVNAMSALCEATGADVSQVSHAVGKDSRIgpKFLNASVGFGGSCFQKDILNLVyicecNGLPEVAEYWKQVIKMNDY 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1566446403 300 KPDWVISKVKQALadFLLVnKNKKidevtIACYGLAFKADIDDLRESPAMQVTKAI 355
Cdd:PLN02353  306 QKSRFVNRVVSSM--FNTV-SGKK-----IAVLGFAFKKDTGDTRETPAIDVCKGL 353
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 330-421 5.12e-18

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 78.70  E-value: 5.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  330 ACYGLAFKADIDDLRESPAMQVTKAISEFHpGRVIAVEPNIHTVPPKLNNIELVDLNFAMQHADIHLLLVDHKEFKG--- 406
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAMEEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSldp 79

                           90
                   ....*....|....*....
gi 1566446403  407 ----KSVNNGIVIDTKGIW 421
Cdd:smart00984  80 eelkDLMKKPVVVDGRNIL 98
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 6-394 3.27e-17

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 82.76  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403   6 ISVIGLGYIGLPTAAMFAsKKKKVIGVDVNKHAIETINQGKIHIVEPELDVVVQTavEEGYLKAVIKP----EPADAFLI 81
Cdd:PRK15057    3 ITISGTGYVGLSNGLLIA-QNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS--DKIHFNATLDKneayRDADYVII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  82 AVPTPFLPCSKNEIPAPDLSFIAEATKaisqiLKKGDLVILESTSPVGTTEQMAiwmKELRPDlsfpqdagdksdiNIAY 161
Cdd:PRK15057   80 ATPTDYDPKTNYFNTSSVESVIKDVVE-----INPYAVMVIKSTVPVGFTAAMH---KKYRTE-------------NIIF 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 162 CPERVLPGKVVQELVTNDR-VIGGMSERCSLRAVELYKTFVEGD--CVITNTRTAEMAKLTENSFRDVQIAFANELSMIC 238
Cdd:PRK15057  139 SPEFLREGKALYDNLHPSRiVIGERSERAERFAALLQEGAIKQNipTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 239 SELDINVWELISLSNRHPRV--NILQPGPGVGGHCIAVDPWFIVSK---TPNeaKIIHTARIVNDSKPDWViskvkqalA 313
Cdd:PRK15057  219 ESLGLNTRQIIEGVCLDPRIgnHYNNPSFGYGGYCLPKDTKQLLANyqsVPN--NLISAIVDANRTRKDFI--------A 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 314 DFLLVNKNKkidevTIACYGLAFKADIDDLRESPAMQVTKAISEfHPGRVIAVEPNIHTVPPKLNNIELvDLNFAMQHAD 393
Cdd:PRK15057  289 DAILSRKPQ-----VVGIYRLIMKSGSDNFRASSIQGIMKRIKA-KGVEVIIYEPVMKEDSFFNSRLER-DLATFKQQAD 361


                  .
gi 1566446403 394 I 394
Cdd:PRK15057  362 V 362
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 330-421 2.55e-13

UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 427462 [Multi-domain]  Cd Length: 103  Bit Score: 65.67  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403 330 ACYGLAFKADIDDLRESPAMQVTKAISEFHPgRVIAVEPNIHTVPPK--LNNIELV-DLNFAMQHADIHLLLVDHKEFK- 405
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGA-EVKVYDPYVPEEAIEalGDGVTLVdDLEEALKGADAIVILTDHDEFKs 79

                          90       100
                  ....*....|....*....|..
gi 1566446403 406 ------GKSVNNGIVIDTKGIW 421
Cdd:pfam03720  80 ldweklKKLMKPPVVFDGRNVL 101
PRK06718 PRK06718
NAD(P)-binding protein;
24-140 4.57e-03

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 38.09  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566446403  24 SKKKKVI---GVDVNKHAIETINQGK-IHIVEPELDVVVQTAVEEG----YLKAVIKPEPADAFLIAVPT--PFLpcskN 93
Cdd:PRK06718    9 SNKRVVIvggGKVAGRRAITLLKYGAhIVVISPELTENLVKLVEEGkirwKQKEFEPSDIVDAFLVIAATndPRV----N 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1566446403  94 EIPAPDLS------FIAEATK---AISQILKKGDLVILESTSpvGTTEQMAIWMKE 140
Cdd:PRK06718   85 EQVKEDLPenalfnVITDAESgnvVFPSALHRGKLTISVSTD--GASPKLAKKIRD 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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