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Conserved domains on  [gi|1012000324|ref|XP_015972770|]
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sucrose synthase [Arachis duranensis]

Protein Classification

sucrose synthase( domain architecture ID 11476401)

sucrose synthase is a sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-806 0e+00

sucrose synthase


:

Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1736.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324   1 MASDR-LTRVHSLRERLDETLTANRNEILALLSRIEAKGKGILQHHQVIAEFEEI--PEENRQKLTDGAFGEVLRSTQEA 77
Cdd:PLN00142    1 AAAAPvLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  78 IVLPPWVALAVRPRPGVWEYLRVNVHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGV 157
Cdd:PLN00142   81 IVLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 158 QFLNRHLSAKLFHDKESLHPLLEFLRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLE 237
Cdd:PLN00142  161 QFLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 238 RGWGDTAERVLESIQLLLDLLEAPDPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEM 317
Cdd:PLN00142  241 KGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 318 LHRIKQQGLDIVPRILIITRLLPDAVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHE 397
Cdd:PLN00142  321 LLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 398 LAKELQGKPDLIVGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFII 477
Cdd:PLN00142  401 ILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFII 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 478 TSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLYSSVE 557
Cdd:PLN00142  481 TSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQ 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 558 NEEHICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGD-RRKESKDLEEKAEMKKMYGLIETYKL 636
Cdd:PLN00142  561 NDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNL 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 637 NGQFRWISSQMNRVRNGELYRVICDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGD 716
Cdd:PLN00142  641 KGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGD 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 717 RAADLLVDFFDKCKVDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRRESRRYLEMFYALKYRKL 796
Cdd:PLN00142  721 EAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFREL 800

                         810
                  ....*....|
gi 1012000324 797 AESVPLAVEE 806
Cdd:PLN00142  801 AKTVPLAVDD 810
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-806 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1736.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324   1 MASDR-LTRVHSLRERLDETLTANRNEILALLSRIEAKGKGILQHHQVIAEFEEI--PEENRQKLTDGAFGEVLRSTQEA 77
Cdd:PLN00142    1 AAAAPvLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  78 IVLPPWVALAVRPRPGVWEYLRVNVHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGV 157
Cdd:PLN00142   81 IVLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 158 QFLNRHLSAKLFHDKESLHPLLEFLRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLE 237
Cdd:PLN00142  161 QFLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 238 RGWGDTAERVLESIQLLLDLLEAPDPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEM 317
Cdd:PLN00142  241 KGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 318 LHRIKQQGLDIVPRILIITRLLPDAVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHE 397
Cdd:PLN00142  321 LLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 398 LAKELQGKPDLIVGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFII 477
Cdd:PLN00142  401 ILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFII 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 478 TSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLYSSVE 557
Cdd:PLN00142  481 TSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQ 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 558 NEEHICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGD-RRKESKDLEEKAEMKKMYGLIETYKL 636
Cdd:PLN00142  561 NDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNL 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 637 NGQFRWISSQMNRVRNGELYRVICDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGD 716
Cdd:PLN00142  641 KGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGD 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 717 RAADLLVDFFDKCKVDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRRESRRYLEMFYALKYRKL 796
Cdd:PLN00142  721 EAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFREL 800

                         810
                  ....*....|
gi 1012000324 797 AESVPLAVEE 806
Cdd:PLN00142  801 AKTVPLAVDD 810
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
 24-803 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1510.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  24 RNEILALLSRIEAKGKGILQHHQVIAEFEE-IPEENR-QKLTDGAFGEVLRSTQEAIVLPPWVALAVRPRPGVWEYLRVN 101
Cdd:TIGR02470   1 RAELRQLLSRYVSQGKRYLLRHQLLDEFEQyCSDADKeKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 102 VHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGVQFLNRHLSAKLFHDKESLHPLLEF 181
Cdd:TIGR02470  81 VEELSVEELTISEYLDFKEQLVNGHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPESMEPLLNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 182 LRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLERGWGDTAERVLESIQLLLDLLEAP 261
Cdd:TIGR02470 161 LRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 262 DPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEMLHRIKQQGLDIVPRILIITRLLPD 341
Cdd:TIGR02470 241 DPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 342 AVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIV-RKWISRFEVWPYLETYTEDVAHELAKELQGKPDLIVGNYSDGNIVA 420
Cdd:TIGR02470 321 AEGTTCNQRLEKVYGTEHAWILRVPFRTENGIIlRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 421 SLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAF 500
Cdd:TIGR02470 401 SLLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAF 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 501 TLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLYSSVENEEHICVLKDRSKPIIFTMARLD 580
Cdd:TIGR02470 481 TMPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLD 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 581 RVKNITGLVEWYGKNARLRELVNLVVVAGDRR-KESKDLEEKAEMKKMYGLIETYKLNGQFRWISSQMNRVRNGELYRVI 659
Cdd:TIGR02470 561 RVKNLTGLVECYGRSPKLRELVNLVVVAGKLDaKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYI 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 660 CDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDKCKVDPTHWDKI 739
Cdd:TIGR02470 641 ADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKI 720

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012000324 740 SQGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRRESRRYLEMFYALKYRKLAESVPLA 803
Cdd:TIGR02470 721 SQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVPLA 784
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
 16-553 0e+00

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 1082.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  16 LDETLTANRNEILALLSRIEAKGKGILQHHQVIAEFEEIPEEN--RQKLTDGAFGEVLRSTQEAIVLPPWVALAVRPRPG 93
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKkeRSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  94 VWEYLRVNVHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGVQFLNRHLSAKLFHDKE 173
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESWNDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFRDSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 174 SLHPLLEFLRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLERGWGDTAERVLESIQL 253
Cdd:pfam00862 161 SLEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 254 LLDLLEAPDPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEMLHRIKQQGLDIVPRIL 333
Cdd:pfam00862 241 LSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQIL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 334 IITRLLPDAVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHELAKELQGKPDLIVGNY 413
Cdd:pfam00862 321 VVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNY 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 414 SDGNIVASLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQ 493
Cdd:pfam00862 401 SDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQ 480

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 494 YESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLY 553
Cdd:pfam00862 481 YESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 278-762 3.50e-147

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 437.83  E-value: 3.50e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 278 NVVILSPHGYFAQDNVLGypDTGGQVVYILDQVRALenemlhrikqqgLDIVPRILIITRLLPDAVGTTcgqrlekVFGT 357
Cdd:cd03800     1 RIALISVHGSPLAQPGGA--DTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADPEV-------VEIA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 358 EHSHILRVPFRTEKGIVRKwisrfEVWPYLETYTEDVAHELAKELqGKPDLIVGNYSDGNIVASLLAHKLGVTQCTIAHA 437
Cdd:cd03800    60 PGARVIRVPAGPPEYLPKE-----ELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 438 LEKTKYPESDIYWKkfeekYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfdp 517
Cdd:cd03800   134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR-------------------- 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 518 kFNIVSPGADQTIYFPYTDGSRRLTAFhpeieellyssveneehicvLKDRSKPIIFTMARLDRVKNITGLVEWYGKNAR 597
Cdd:cd03800   189 -INVVPPGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 598 LRELVNLVVVAGDRR-KESKDLEEKAEMKKMYGLIETYKLNGQfrwissqMNRVRNGELYRVicdtKGAFVQPAVYEAFG 676
Cdd:cd03800   248 LRELANLVLVGGPSDdPLSMDREELAELAEELGLIDRVRFPGR-------VSRDDLPELYRA----ADVFVVPSLYEPFG 316

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 677 LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQRIEEKYTWQIY 756
Cdd:cd03800   317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392


                  ....*.
gi 1012000324 757 SQRLLT 762
Cdd:cd03800   393 ADQLLT 398
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 665-763 2.70e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.05  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 665 AFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGL 744
Cdd:COG0438    23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPELRRRLGEAAR 98

                          90
                  ....*....|....*....
gi 1012000324 745 QRIEEKYTWQIYSQRLLTL 763
Cdd:COG0438    99 ERAEERFSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-806 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1736.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324   1 MASDR-LTRVHSLRERLDETLTANRNEILALLSRIEAKGKGILQHHQVIAEFEEI--PEENRQKLTDGAFGEVLRSTQEA 77
Cdd:PLN00142    1 AAAAPvLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  78 IVLPPWVALAVRPRPGVWEYLRVNVHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGV 157
Cdd:PLN00142   81 IVLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 158 QFLNRHLSAKLFHDKESLHPLLEFLRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLE 237
Cdd:PLN00142  161 QFLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 238 RGWGDTAERVLESIQLLLDLLEAPDPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEM 317
Cdd:PLN00142  241 KGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEM 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 318 LHRIKQQGLDIVPRILIITRLLPDAVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHE 397
Cdd:PLN00142  321 LLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 398 LAKELQGKPDLIVGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFII 477
Cdd:PLN00142  401 ILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFII 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 478 TSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLYSSVE 557
Cdd:PLN00142  481 TSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQ 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 558 NEEHICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGD-RRKESKDLEEKAEMKKMYGLIETYKL 636
Cdd:PLN00142  561 NDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNL 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 637 NGQFRWISSQMNRVRNGELYRVICDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGD 716
Cdd:PLN00142  641 KGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGD 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 717 RAADLLVDFFDKCKVDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRRESRRYLEMFYALKYRKL 796
Cdd:PLN00142  721 EAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFREL 800

                         810
                  ....*....|
gi 1012000324 797 AESVPLAVEE 806
Cdd:PLN00142  801 AKTVPLAVDD 810
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
 24-803 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1510.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  24 RNEILALLSRIEAKGKGILQHHQVIAEFEE-IPEENR-QKLTDGAFGEVLRSTQEAIVLPPWVALAVRPRPGVWEYLRVN 101
Cdd:TIGR02470   1 RAELRQLLSRYVSQGKRYLLRHQLLDEFEQyCSDADKeKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 102 VHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGVQFLNRHLSAKLFHDKESLHPLLEF 181
Cdd:TIGR02470  81 VEELSVEELTISEYLDFKEQLVNGHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPESMEPLLNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 182 LRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLERGWGDTAERVLESIQLLLDLLEAP 261
Cdd:TIGR02470 161 LRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 262 DPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEMLHRIKQQGLDIVPRILIITRLLPD 341
Cdd:TIGR02470 241 DPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 342 AVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIV-RKWISRFEVWPYLETYTEDVAHELAKELQGKPDLIVGNYSDGNIVA 420
Cdd:TIGR02470 321 AEGTTCNQRLEKVYGTEHAWILRVPFRTENGIIlRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 421 SLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAF 500
Cdd:TIGR02470 401 SLLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAF 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 501 TLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLYSSVENEEHICVLKDRSKPIIFTMARLD 580
Cdd:TIGR02470 481 TMPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLD 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 581 RVKNITGLVEWYGKNARLRELVNLVVVAGDRR-KESKDLEEKAEMKKMYGLIETYKLNGQFRWISSQMNRVRNGELYRVI 659
Cdd:TIGR02470 561 RVKNLTGLVECYGRSPKLRELVNLVVVAGKLDaKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYI 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 660 CDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDKCKVDPTHWDKI 739
Cdd:TIGR02470 641 ADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKI 720

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012000324 740 SQGGLQRIEEKYTWQIYSQRLLTLTGVYGFWKHVSNLDRRESRRYLEMFYALKYRKLAESVPLA 803
Cdd:TIGR02470 721 SQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVPLA 784
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
 16-553 0e+00

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 1082.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  16 LDETLTANRNEILALLSRIEAKGKGILQHHQVIAEFEEIPEEN--RQKLTDGAFGEVLRSTQEAIVLPPWVALAVRPRPG 93
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKkeRSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  94 VWEYLRVNVHALVVEELQAAEYLRFKEELVDGSSNANFVLELDFEPFTASFPRPTLNKSIGNGVQFLNRHLSAKLFHDKE 173
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESWNDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFRDSE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 174 SLHPLLEFLRLHSYKGKTLMLNDRIHNPDSLQHVLRKAEEYLGTLPAETPYSEFEHKFQEIGLERGWGDTAERVLESIQL 253
Cdd:pfam00862 161 SLEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 254 LLDLLEAPDPCTLETFLDRIPMVFNVVILSPHGYFAQDNVLGYPDTGGQVVYILDQVRALENEMLHRIKQQGLDIVPRIL 333
Cdd:pfam00862 241 LSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQIL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 334 IITRLLPDAVGTTCGQRLEKVFGTEHSHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHELAKELQGKPDLIVGNY 413
Cdd:pfam00862 321 VVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNY 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 414 SDGNIVASLLAHKLGVTQCTIAHALEKTKYPESDIYWKKFEEKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQ 493
Cdd:pfam00862 401 SDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQ 480

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 494 YESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEIEELLY 553
Cdd:pfam00862 481 YESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 278-762 3.50e-147

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 437.83  E-value: 3.50e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 278 NVVILSPHGYFAQDNVLGypDTGGQVVYILDQVRALenemlhrikqqgLDIVPRILIITRLLPDAVGTTcgqrlekVFGT 357
Cdd:cd03800     1 RIALISVHGSPLAQPGGA--DTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADPEV-------VEIA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 358 EHSHILRVPFRTEKGIVRKwisrfEVWPYLETYTEDVAHELAKELqGKPDLIVGNYSDGNIVASLLAHKLGVTQCTIAHA 437
Cdd:cd03800    60 PGARVIRVPAGPPEYLPKE-----ELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 438 LEKTKYPESDIYWKkfeekYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfdp 517
Cdd:cd03800   134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR-------------------- 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 518 kFNIVSPGADQTIYFPYTDGSRRLTAFhpeieellyssveneehicvLKDRSKPIIFTMARLDRVKNITGLVEWYGKNAR 597
Cdd:cd03800   189 -INVVPPGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 598 LRELVNLVVVAGDRR-KESKDLEEKAEMKKMYGLIETYKLNGQfrwissqMNRVRNGELYRVicdtKGAFVQPAVYEAFG 676
Cdd:cd03800   248 LRELANLVLVGGPSDdPLSMDREELAELAEELGLIDRVRFPGR-------VSRDDLPELYRA----ADVFVVPSLYEPFG 316

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 677 LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQRIEEKYTWQIY 756
Cdd:cd03800   317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392


                  ....*.
gi 1012000324 757 SQRLLT 762
Cdd:cd03800   393 ADQLLT 398
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 279-753 8.02e-38

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 152.63  E-value: 8.02e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  279 VVILSPHGYFAQDNV-LGY-PDTGGQVVYILDQVRALEnemlhriKQQGldiVPRILIITRLL--PDaVGTTCGQ----- 349
Cdd:TIGR02468  172 IVLISLHGLVRGENMeLGRdSDTGGQVKYVVELARALG-------SMPG---VYRVDLLTRQVssPD-VDWSYGEpteml 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  350 --RLEKVFGTEHS-----HILRVPFrtekGIVRKWISRFEVWPYLETYTE-------DVAHELAKELQGK----PDLIVG 411
Cdd:TIGR02468  241 tpRSSENDGDEMGessgaYIIRIPF----GPRDKYIPKEELWPYIPEFVDgalshivNMSKVLGEQIGSGhpvwPYVIHG 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  412 NYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPE---------SDIywkkfEEKYHFSCQFTADLFAMNHTDFIITSTFQ 482
Cdd:TIGR02468  317 HYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQllkqgrmskEEI-----NSTYKIMRRIEAEELSLDASEIVITSTRQ 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  483 EIAGskdtvgQYESHTAFTlPGLYRVV----------HGidVFDPKFNIVSPGADQTIYFPYTDGSRRLTAFHPEI---- 548
Cdd:TIGR02468  392 EIEE------QWGLYDGFD-VILERKLrararrgvscYG--RFMPRMAVIPPGMEFSHIVPHDGDMDGETEGNEEHpakp 462

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  549 EELLYSSVeneehICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGDRrkesKDLEEKAEMK--- 625
Cdd:TIGR02468  463 DPPIWSEI-----MRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNR----DDIDEMSSGSssv 533

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324  626 --KMYGLIETYKLNGQFRWiSSQMNRVRNGELYRVICDTKGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVH 703
Cdd:TIGR02468  534 ltSVLKLIDKYDLYGQVAY-PKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRV 612

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1012000324  704 GKSGFHIDPYHGDRAADLLVdffdKCKVDPTHWDKISQGGLQRIeEKYTW 753
Cdd:TIGR02468  613 LDNGLLVDPHDQQAIADALL----KLVADKQLWAECRQNGLKNI-HLFSW 657
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 570-722 2.60e-26

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 105.43  E-value: 2.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 570 KPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVaGDrrkeskdLEEKAEMKKmygLIETYKLNGQFRWISsQMNR 649
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIA-GD-------GEEEKRLKK---LAEKLGLGDNVIFLG-FVSD 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012000324 650 VRNGELYRvICDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLL 722
Cdd:pfam00534  70 EDLPELLK-IAD---VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAI 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 665-763 2.70e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.05  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 665 AFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGL 744
Cdd:COG0438    23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPELRRRLGEAAR 98

                          90
                  ....*....|....*....
gi 1012000324 745 QRIEEKYTWQIYSQRLLTL 763
Cdd:COG0438    99 ERAEERFSWEAIAERLLAL 117
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 564-763 7.98e-19

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 89.13  E-value: 7.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 564 VLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGDRrkeskdlEEKAEMKKMyglieTYKLNGQFRWI 643
Cdd:cd03801   186 LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDG-------PLRAELEEL-----ELGLGDRVRFL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 644 SSQM-NRVRngELYRvICDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLL 722
Cdd:cd03801   254 GFVPdEELP--ALYA-AAD---VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADAL 327

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1012000324 723 VDFFDkckvDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTL 763
Cdd:cd03801   328 LRLLA----DPELRARLGRAARERVAERFSWERVAERLLDL 364
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 558-761 1.33e-14

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 76.09  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 558 NEEHICVLKD--RSKPIIFTM-ARLDRVKNITGLVE------WYGKNARLrelvnlvVVAGDRrkeskDLEEKAEMkkmy 628
Cdd:cd03808   174 DLDRFQYSPEslPSEKVVFLFvARLLKDKGIDELIEaakilkKKGPNVRF-------LLVGDG-----ELENPSEI---- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 629 gLIETYKLNGQFRWISSQMNrVRngELYRvICDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGF 708
Cdd:cd03808   238 -LIEKLGLEGRIEFLGFRSD-VP--ELLA-ESD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1012000324 709 HIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQRIEEKYTWQIYSQRLL 761
Cdd:cd03808   310 LVPPGDVEALADAIEKLIE----DPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 332-763 2.58e-14

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 75.49  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 332 ILIITRLLPDAVGTTCG-----------QRLEKV----FGTEHSHILRvpfRTEKGIVRKWISRFEVWPYLETYTEDVAH 396
Cdd:cd03798     1 VLILTNIYPNANSPGRGifvrrqvralsRRGVDVevlaPAPWGPAAAR---LLRKLLGEAVPPRDGRRLLPLKPRLRLLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 397 -----ELAKEL----QGKPDLIVGN--YSDGnIVASLLAHKLGVTQCTIAHalektkypESDIYwkKFEEKYHFSCQFta 465
Cdd:cd03798    78 plrapSLAKLLkrrrRGPPDLIHAHfaYPAG-FAAALLARLYGVPYVVTEH--------GSDIN--VFPPRSLLRKLL-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 466 dLFAMNHTDFIITSTfqeiagskdtvgqyeshtaftlPGLYRVVHGIDVfdPKFNIVspgadqTIYFPYtDGSRrltaFH 545
Cdd:cd03798   145 -RWALRRAARVIAVS----------------------KALAEELVALGV--PRDRVD------VIPNGV-DPAR----FQ 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 546 PEIEELLYSSveneehicvlkdrSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGDRRKEskdleekaemk 625
Cdd:cd03798   189 PEDRGLGLPL-------------DAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLRE----------- 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 626 KMYGLIETYKLNGQFRWISsqmnRVRNGELYRVI--CDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVH 703
Cdd:cd03798   245 ALRALAEDLGLGDRVTFTG----RLPHEQVPAYYraCD---VFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGD 317

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1012000324 704 GKSGFHIDPYHGDRAADLLVDFFDKckvdptHWDKIS-QGGLQRIEEKYTWQIYSQRLLTL 763
Cdd:cd03798   318 PETGLLVPPGDADALAAALRRALAE------PYLRELgEAARARVAERFSWVKAADRIAAA 372
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 570-759 2.34e-13

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 72.39  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 570 KPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVaGDRrkeskdlEEKAEMKKmygLIETYKLNGQFRWISSQMNr 649
Cdd:cd03811   188 GPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVIL-GDG-------PLREELEK---LAKELGLAERVIFLGFQSN- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 650 vrngeLYRVI--CDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFD 727
Cdd:cd03811   256 -----PYPYLkkAD---LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQ 327

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1012000324 728 KCKVDpthwdkisqggLQRIEEKYTWQIYSQR 759
Cdd:cd03811   328 KKLDA-----------ALRERLAKAQEAVFRE 348
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 538-761 7.20e-13

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 70.86  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 538 SRRLTAFHPEIEELlYSSVENEEHICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVaGDRRKESKD 617
Cdd:cd03809   161 PEKIVVIPLGVDPS-FFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIV-GGKGWEDEE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 618 LEEkaemkkmygLIETYKLNGQFRWISsqmnRVRNGELYRVICDTKgAFVQPAVYEAFGLTVVEAMTCGLPTFATcNGGP 697
Cdd:cd03809   239 LLD---------LVKKLGLGGRVRFLG----YVSDEDLPALYRGAR-AFVFPSLYEGFGLPVLEAMACGTPVIAS-NISV 303

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012000324 698 -AEIIvhGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQRIeEKYTWQIYSQRLL 761
Cdd:cd03809   304 lPEVA--GDAALYFDPLDPESIADAILRLLE----DPSLREELIRKGLERA-KKFSWEKTAEKTL 361
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 567-763 4.57e-12

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 68.50  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 567 DRSKPIIFTMARLDRVKNITGLVEWYGK------NARLrelvnLVVVAGDRRkeskdlEEKAEMKKMYGLIETYKLNGQf 640
Cdd:cd03807   187 AEDRRVIGIVGRLHPVKDHSDLLRAAALlvethpDLRL-----LLVGRGPER------PNLERLLLELGLEDRVHLLGE- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 641 rwissqmnRVRNGELYRVIcDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVhGKSGFHIDPyhgdRAAD 720
Cdd:cd03807   255 --------RSDVPALLPAM-D---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPA----GDPQ 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1012000324 721 LLVDFFDKCKVDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTL 763
Cdd:cd03807   318 ALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETL 360
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 570-749 1.24e-10

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 63.84  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 570 KPIIFTMARLDRVKNITGLVEWYgknARLRELVNL-VVVAGDRrKESKDLEEKA-EMKKMYGLIETYKLNgqfrwissqm 647
Cdd:cd03817   201 EPILLYVGRLAKEKNIDFLLRAF---AELKKEPNIkLVIVGDG-PEREELKELArELGLADKVIFTGFVP---------- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 648 nRVRNGELYRvICDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHgdraaDLLVDFFD 727
Cdd:cd03817   267 -REELPEYYK-AAD---LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND-----ETLAEKLL 336

                         170       180
                  ....*....|....*....|..
gi 1012000324 728 KCKVDPTHWDKISQGGLQRIEE 749
Cdd:cd03817   337 HLRENLELLRKLSKNAEISARE 358
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 672-762 2.17e-10

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 63.12  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 672 YEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhgDRAADLLVDFFdKCKVDPTHWDKISQGGLQRIEEKY 751
Cdd:cd03823   271 PEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAP---GDAEDLAAAMR-RLLTDPALLERLRAGAEPPRSTES 346

                          90
                  ....*....|.
gi 1012000324 752 TWQIYSQRLLT 762
Cdd:cd03823   347 QAEEYLKLYRD 357
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 663-713 2.57e-10

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 62.69  E-value: 2.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1012000324 663 KGAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPY 713
Cdd:cd03802   241 RALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV 291
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
570-712 9.05e-10

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 57.52  E-value: 9.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 570 KPIIFTMARLD-RVKNITGLVE-WygknARLRELVNLV--VVAGDRrkESKDLEEKAEmkkmyglietyKLNGQFRWiss 645
Cdd:pfam13692   1 RPVILFVGRLHpNVKGVDYLLEaV----PLLRKRDNDVrlVIVGDG--PEEELEELAA-----------GLEDRVIF--- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012000324 646 qMNRVRN-GELYRViCDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIvHGKSGFHIDP 712
Cdd:pfam13692  61 -TGFVEDlAELLAA-AD---VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPP 122
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 544-722 9.40e-10

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 61.22  E-value: 9.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 544 FHPEIEEllyssvenEEHICVLKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGdrrkeskdlEEKAE 623
Cdd:cd03819   164 FPPEAEA--------EERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDG---------PERDE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 624 MKKmygLIETYKLNGQFRWISsqmNRVRNGELYRvICDTkgaFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVH 703
Cdd:cd03819   227 IRR---LVERLGLRDRVTFTG---FREDVPAALA-ASDV---VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVH 296

                         170
                  ....*....|....*....
gi 1012000324 704 GKSGFHIDPYHGDRAADLL 722
Cdd:cd03819   297 GRTGLLVPPGDAEALADAI 315
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 565-713 9.75e-10

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 61.10  E-value: 9.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 565 LKDRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVV-AGDRRKESKDLeekaemkkmyglIETYKLNGQFRWi 643
Cdd:cd03820   176 STNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYgDGPEREELEKL------------IDKLGLEDRVKL- 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012000324 644 ssqMNRVRN-GELYRvicdTKGAFVQPAVYEAFGLTVVEAMTCGLP--TFAtCNGGPAEIIVHGKSGFHIDPY 713
Cdd:cd03820   243 ---LGPTKNiAEEYA----NSSIFVLSSRYEGFPMVLLEAMAYGLPiiSFD-CPTGPSEIIEDGENGLLVPNG 307
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 576-710 1.67e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 58.95  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 576 MARLDRVKNITGLVEWYGK-NARLRELVNLVVVAGDRRKESKDLEEKAemkkmyglietyKLNGQFRWISSQMNRVRNGE 654
Cdd:cd01635   116 VGRLVPEKGIDLLLEALALlKARLPDLVLVLVGGGGEREEEEALAAAL------------GLLERVVIIGGLVDDEVLEL 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1012000324 655 LYRViCDtkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHI 710
Cdd:cd01635   184 LLAA-AD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 666-753 9.69e-09

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 58.20  E-value: 9.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 666 FVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQ 745
Cdd:TIGR03088 276 FVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVS----DPAARRAHGAAGRA 351


                  ....*...
gi 1012000324 746 RIEEKYTW 753
Cdd:TIGR03088 352 RAEQQFSI 359
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 666-751 1.68e-08

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 57.36  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 666 FVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDpyHGD------RAADLLvdffdkckVDPTHWDKI 739
Cdd:cd04962   273 FLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSD--VGDvdamakSALSIL--------EDDELYNRM 342

                          90
                  ....*....|..
gi 1012000324 740 SQGGLQRIEEKY 751
Cdd:cd04962   343 GRAARKRAAERF 354
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 672-760 2.33e-08

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 56.83  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 672 YEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhgdrAADLLVDFFDKCKVDPTHWDKISQGGLQRIEEKY 751
Cdd:cd03805   309 NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-----TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKF 383


                  ....*....
gi 1012000324 752 TWQIYSQRL 760
Cdd:cd03805   384 SREAFAERL 392
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 665-753 2.80e-08

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 56.53  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 665 AFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFdkckVDPTHWDKISQGGL 744
Cdd:cd03814   270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALL----EDPELRRRMAARAR 345


                  ....*....
gi 1012000324 745 QRIEEkYTW 753
Cdd:cd03814   346 AEAER-YSW 353
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 665-763 1.23e-07

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 54.65  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 665 AFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhGDRAAdlLVDFFDKCKVDPTHWDKISQGGL 744
Cdd:cd03825   266 LFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPP--GDVQA--LAEAIEWLLANPKERESLGERAR 341

                          90
                  ....*....|....*....
gi 1012000324 745 QRIEEKYTWQIYSQRLLTL 763
Cdd:cd03825   342 ALAENHFDQRVQAQRYLEL 360
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 567-763 1.74e-07

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 54.25  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 567 DRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAG---DRRKESKDLEEKAEMKKMYGLIETYKLNGQFRWI 643
Cdd:cd03792   194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHgavDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEI 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 644 SSQMNRVRngelyrVIcdtkgafVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhGDRAADLLV 723
Cdd:cd03792   274 NALQRAAT------VV-------LQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRIL 338

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1012000324 724 DFFdkckVDPTHWDKISQGGLQRIEEKYTWQIYSQRLLTL 763
Cdd:cd03792   339 RLL----TDPELRRKMGLAAREHVRDNFLITGNLRAWLYL 374
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 679-761 6.90e-07

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 52.34  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 679 VVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhGDraADLLVDFFDKCKVDPTHWDKISQGGLQRIEEKYTWQIYSQ 758
Cdd:cd03794   313 LFEYMAAGKPILASDDGGSDLAVEINGCGLVVEP--GD--PEALADAILELLDDPELRRAMGENGRELAEEKFSREKLAD 388


                  ...
gi 1012000324 759 RLL 761
Cdd:cd03794   389 RLL 391
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 569-761 7.81e-07

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 51.99  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 569 SKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGDrrkeskDLEEKAEMKKMYglietyKLNGQfrwissqmN 648
Cdd:cd03821   203 DRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPD------DGAYPAFLQLQS------SLGLG--------D 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 649 RVR-NGELYRvicDTKGA-------FVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGkSGFHIDPyHGDRAAD 720
Cdd:cd03821   263 RVTfTGPLYG---EAKWAlyasadlFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAE 337

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1012000324 721 LLVDFFDkckvDPTHWDKISQGGLQ--RIEEKYTWQIYSQRLL 761
Cdd:cd03821   338 ALAEALR----DPADRKRLGEMARRarQVEENFSWEAVAGQLG 376
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 572-701 1.19e-06

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 51.68  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 572 IIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVA-GDRRKEskdLEEKAemkKMYGLIETYKLNGQFRWISSQMNrv 650
Cdd:cd04951   190 VILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGdGPLRNE---LERLI---CNLNLVDRVILLGQISNISEYYN-- 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1012000324 651 rngelyrvICDTkgaFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEII 701
Cdd:cd04951   262 --------AADL---FVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV 301
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 672-758 1.65e-06

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 50.76  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 672 YEAFGLTVVEAMTCGLPTFA-TCNGGPAEIIVHGKSGFHIdPYHG-DRAADLLVDFFDkckvDPTHWDKISQGGLQRIEE 749
Cdd:cd04949   244 MEGFGLTLMEAIGHGLPVVSyDVKYGPSELIEDGENGYLI-EKNNiDALADKIIELLN----DPEKLQQFSEESYKIAEK 318


                  ....*....
gi 1012000324 750 KYTWQIYSQ 758
Cdd:cd04949   319 YSTENVMEK 327
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
567-759 3.11e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 50.17  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 567 DRSKPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVaGDRRKESKDleEKAEMKKMygLIETYK--------LNG 638
Cdd:PRK15484  190 SPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVV-GDPTASSKG--EKAAYQKK--VLEAAKrigdrcimLGG 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 639 QfrwISSQMNrvrngELYRvICDTkgAFVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHI-DPYhgdr 717
Cdd:PRK15484  265 Q---PPEKMH-----NYYP-LADL--VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLaEPM---- 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1012000324 718 AADLLVDFFDKCKVDPTHwDKISQGGLQRIEEKYTWQIYSQR 759
Cdd:PRK15484  330 TSDSIISDINRTLADPEL-TQIAEQAKDFVFSKYSWEGVTQR 370
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 570-752 1.39e-05

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 48.04  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 570 KPIIFTMARLDRVKNITGLVEwygkNARLRELVNLVVVAGDrrkESKDLEEKAEmkkmYGLIETYKLNGqfrwissqmnR 649
Cdd:cd03795   191 KKIFLFIGRLVYYKGLDYLIE----AAQYLNYPIVIGGEGP---LKPDLEAQIE----LNLLDNVKFLG----------R 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 650 VRNGEL--YRVICDtkgAFVQPAVY--EAFGLTVVEAMTCGLPTFAT-CNGGPAEIIVHGKSGFHIDPyhGDRAAdlLVD 724
Cdd:cd03795   250 VDDEEKviYLHLCD---VFVFPSVLrsEAFGIVLLEAMMCGKPVISTnIGTGVPYVNNNGETGLVVPP--KDPDA--LAE 322

                         170       180
                  ....*....|....*....|....*...
gi 1012000324 725 FFDKCKVDPTHWDKISQGGLQRIEEKYT 752
Cdd:cd03795   323 AIDKLLSDEELRESYGENAKKRFEELFT 350
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 671-752 2.15e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 47.71  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 671 VYEAFGLTVVEAMTCGLPTFATCNGGPAEII-----VHGKSGFHIDPYHGDRAADLLVDFFDkckvDPTHWDKISQGGLQ 745
Cdd:cd03813   379 ISEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLR----DPELRQAFGEAGRK 454


                  ....*..
gi 1012000324 746 RIEEKYT 752
Cdd:cd03813   455 RVEKYYT 461
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 665-760 4.88e-05

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 46.29  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 665 AFVQPAVY------EAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDPyhGDRAAdlLVDFFDKCKVDPTHWDK 738
Cdd:cd05844   265 IFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPE--GDVDA--LADALQALLADRALADR 340

                          90       100
                  ....*....|....*....|..
gi 1012000324 739 ISQGGLQRIEEKYTWQIYSQRL 760
Cdd:cd05844   341 MGGAARAFVCEQFDIRVQTAKL 362
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 666-775 8.43e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.86  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 666 FVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEII---VHGKSGFHIDPYHGDRAADLLVDFFDKCKVdpthwdKISQG 742
Cdd:PLN02871  335 FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPEL------RERMG 408

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1012000324 743 GLQRIE-EKYTWQIYSQRLLTLTGVYGFWKHVSN 775
Cdd:PLN02871  409 AAAREEvEKWDWRAATRKLRNEQYSAAIWFWRKK 442
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 665-708 3.73e-04

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 43.43  E-value: 3.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1012000324 665 AFVQPAVyEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGF 708
Cdd:cd03804   268 AFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGI 310
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 659-751 4.26e-04

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 43.21  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 659 ICDTKGAFVQPAVYEAFG------LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDpyhgDRAADLLVDFFDKCKVD 732
Cdd:cd03799   247 ILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVP----ERDAEAIAEKLTYLIEH 322

                          90
                  ....*....|....*....
gi 1012000324 733 PTHWDKISQGGLQRIEEKY 751
Cdd:cd03799   323 PAIWPEMGKAGRARVEEEY 341
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 666-751 3.36e-03

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 40.52  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012000324 666 FVQPAVYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFHIDpyhGDRAADLLVDFFDKCKVDPTHWDKISQGGLQ 745
Cdd:cd04946   308 FVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLD---KDPTPNEIVSSIMKFYLDGGDYKTMKISARE 384


                  ....*.
gi 1012000324 746 RIEEKY 751
Cdd:cd04946   385 CWEERF 390
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
665-728 3.42e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 40.46  E-value: 3.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012000324 665 AFVQPAVYEAFGLTVVEAMTCGLPTFAT-CNGGPAEIIVHGKSGFHIDPYHGDRAADLLVDFFDK 728
Cdd:PRK09922  260 ALLLTSKFEGFPMTLLEAMSYGIPCISSdCMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISG 324
 
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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